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Human Metabolome Database Version 2.5

 

Showing metabocard for NADPH (HMDB00221)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:46
Accession Number HMDB00221
Secondary Accession Numbers HMDB00799; HMDB06341
Common Name NADPH
Description Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed.)
Synonyms
  1. 2'-(dihydrogen phosphate) 5'-(trihydrogen pyrophosphate) Adenosine 5'-ester with 1,4-dihydro-1-b-D-ribofuranosylnicotinamide
  2. Adenosine 5'-(trihydrogen diphosphate) 2'-(dihydrogen phosphate) P'-5'-ester with 1,4-dihydro-1-beta-D-ribofuranosyl-3-pyridinecarboxamide
  3. Dihydrocodehydrogenase II
  4. NADP-reduced
  5. NADPH
  6. Nicotinamide-adenine-dinucleotide-phosphorate
  7. Nicotinamide-adenine-dinucleotide-phosphoric acid
  8. Reduced triphosphopyridine nucleotide
  9. Triphosphopyridine nucleotide reduced
  10. b-NADPH
  11. b-Nicotinamide-adenine-dinucleotide-phosphorate
  12. b-Nicotinamide-adenine-dinucleotide-phosphoric acid
  13. dihydronicotinamide adenine dinucleotide phosphate
  14. dihydronicotinamide adenine dinucleotide-P
  15. dihydrotriphosphopyridine nucleotide reduced
  16. reduced Codehydrase II
  17. reduced Coenzyme II
  18. reduced Cozymase II
  19. beta-NADPH
  20. beta-Nicotinamide-adenine-dinucleotide-phosphorate
  21. beta-Nicotinamide-adenine-dinucleotide-phosphoric acid
  22. 2'-(dihydrogen phosphate) 5'-(trihydrogen pyrophosphate) Adenosine 5'-ester with 1,4-dihydro-1-beta-delta-ribofuranosylnicotinamide
  23. Adenosine 5'-(trihydrogen diphosphate) 2'-(dihydrogen phosphate) P'-5'-ester with 1,4-dihydro-1-beta-delta-ribofuranosyl-3-pyridinecarboxamide
Chemical IUPAC Name [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methyl [[(2R,3S,4R,5R)-5-(3-carbamoyl-4H-pyridin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] hydrogen phosphate
Chemical Formula C21H30N7O17P3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide triphosphates
Family
  • Mammalian Metabolite
Species
  • hemiaminal
  • enamine
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • primary carboxylic acid amide
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Androgen and estrogen metabolism
  • Component of Arginine and proline metabolism
  • Component of beta-Alanine metabolism
  • Component of Bile acid biosynthesis
  • Component of C21-Steroid hormone metabolism
  • Component of Folate biosynthesis
  • Component of Fructose and mannose metabolism
  • Component of Glutamate metabolism
  • Component of Glutathione metabolism
  • Component of Glycerolipid metabolism
  • Component of Glyoxylate and dicarboxylate metabolism
  • Component of Monoterpenoid biosynthesis
  • Component of Nicotinate and nicotinamide metabolism
  • Component of Pantothenate and CoA biosynthesis
  • Component of Porphyrin and chlorophyll metabolism
  • Component of Prostaglandin and leukotriene metabolism
  • Component of Purine metabolism
  • Component of Pyrimidine metabolism
  • Component of Pyruvate metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 745.421
Monoisotopic Molecular Weight 745.091125
Isomeric SMILES NC(=O)C1=CN(C=CC1)[C@H]1O[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2O[C@@H]([C@@H](OP(O)(O)=O)[C@H]2O)N2C=NC3=C(N)N=CN=C23)[C@H](O)[C@@H]1O
Canonical SMILES NC(=O)C1=CN(C=CC1)C1OC(COP(O)(=O)OP(O)(=O)OCC2OC(C(OP(O)(O)=O)C2O)N2C=NC3=C(N)N=CN=C23)C(O)C1O
KEGG Compound ID C00005 Link Image
BioCyc ID NADPH Link Image
BiGG ID 33486 Link Image
Wikipedia Link NADPH Link Image
NuGOwiki Link HMDB00221 Link Image
Metagene Link HMDB00221 Link Image
METLIN ID 3691 Link Image
PubChem Compound 5884 Link Image
PubChem Substance 8145663 Link Image
ChEBI ID 16474 Link Image
CAS Registry Number 53-57-6
InChI Identifier InChI=1/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m0/s1
Synthesis Reference Seelbach, Karsten; Riebel, Bettina; Hummel, Werner; Kula, Maria-Regina; Tishkov, Vladimir I.; Egorov, Alexey M.; Wandrey, Christian; Kragl, Udo. A novel, efficient regenerating method of NADPH using a new formate dehydrogenase. Tetrahedron Letters (1996), 37(9), 1377-80.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.45 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.13 [Predicted by ALOGPS]; -6.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 51.0 (34.0-81.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
Ethanol Degradation SMP00449 Link Image
Folate Metabolism SMP00053 Link Image map00670 Link Image
Glucose-Alanine Cycle SMP00127 Link Image
Glutathione Metabolism SMP00015 Link Image map00480 Link Image
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
Histidine Metabolism SMP00044 Link Image map00340 Link Image
Phytanic Acid Peroxisomal Oxidation SMP00450 Link Image
Plasmalogen Synthesis SMP00479 Link Image
Pterine Biosynthesis SMP00005 Link Image map00790 Link Image
Transfer of Acetyl Groups into Mitochondria SMP00466 Link Image
Vitamin K Metabolism SMP00464 Link Image
General References
  1. Shindo Y, Witt E, Han D, Epstein W, Packer L: Enzymic and non-enzymic antioxidants in epidermis and dermis of human skin. J Invest Dermatol. 1994 Jan;102(1):122-4. [PubMed Link Image]
  2. Iwata H, Tezuka Y, Kadota S, Hiratsuka A, Watabe T: Mechanism-based inactivation of human liver microsomal CYP3A4 by rutaecarpine and limonin from Evodia fruit extract. Drug Metab Pharmacokinet. 2005 Feb;20(1):34-45. [PubMed Link Image]
  3. Birkmayer GJ, Birkmayer W: Stimulation of endogenous L-dopa biosynthesis--a new principle for the therapy of Parkinson's disease. The clinical effect of nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotidephosphate (NADPH). Acta Neurol Scand Suppl. 1989;126:183-7. [PubMed Link Image]
  4. Lee AJ, Zhu BT: NADPH-dependent formation of polar and nonpolar estrogen metabolites following incubations of 17 beta-estradiol with human liver microsomes. Drug Metab Dispos. 2004 Aug;32(8):876-83. [PubMed Link Image]
  5. Kochansky CJ, Xia YQ, Wang S, Cato B, Creighton M, Vincent SH, Franklin RB, Reed JR: Species differences in the elimination of a peroxisome proliferator-activated receptor agonist highlighted by oxidative metabolism of its acyl glucuronide. Drug Metab Dispos. 2005 Dec;33(12):1894-904. Epub 2005 Sep 23. [PubMed Link Image]
  6. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  7. Karanam BV, Hop CE, Liu DQ, Wallace M, Dean D, Satoh H, Komuro M, Awano K, Vincent SH: In vitro metabolism of MK-0767 [(+/-)-5-[(2,4-dioxothiazolidin-5-yl)methyl]-2-methoxy-N-[[(4-trifluoromet hyl) phenyl]methyl]benzamide], a peroxisome proliferator-activated receptor alpha/gamma agonist. I. Role of cytochrome P450, methyltransferases, flavin monooxygenases, and esterases. Drug Metab Dispos. 2004 Sep;32(9):1015-22. [PubMed Link Image]
  8. Soglia JR, Contillo LG, Kalgutkar AS, Zhao S, Hop CE, Boyd JG, Cole MJ: A semiquantitative method for the determination of reactive metabolite conjugate levels in vitro utilizing liquid chromatography-tandem mass spectrometry and novel quaternary ammonium glutathione analogues. Chem Res Toxicol. 2006 Mar;19(3):480-90. [PubMed Link Image]
  9. Afanas'ev IB, Suslova TB, Cheremisina ZP, Abramova NE, Korkina LG: Study of antioxidant properties of metal aspartates. Analyst. 1995 Mar;120(3):859-62. [PubMed Link Image]
  10. Lin CC, Wong BK, Burgey CS, Gibson CR, Singh R: In vitro metabolism of a thrombin inhibitor and quantitation of metabolically generated cyanide. J Pharm Biomed Anal. 2005 Oct 4;39(5):1014-20. Epub 2005 Jul 14. [PubMed Link Image]
  11. Conley AJ, Pattison JC, Bird IM: Variations in adrenal androgen production among (nonhuman) primates. Semin Reprod Med. 2004 Nov;22(4):311-26. [PubMed Link Image]
  12. Wikipedia Link Image
Metabolic Enzymes
  1. Fatty acid synthase
  2. Aldo-keto reductase family 1 member C4
  3. Carbonyl reductase [NADPH] 1
  4. Dehydrogenase/reductase SDR family member 4
  5. Carbonyl reductase [NADPH] 3
  6. Aldose reductase
  7. Thioredoxin reductase 1, cytoplasmic
  8. Lathosterol oxidase
  9. Dimethylaniline monooxygenase [N-oxide-forming] 5
  10. Heme oxygenase 2
  11. Dimethylaniline monooxygenase [N-oxide-forming] 2
  12. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
  13. Thioredoxin reductase 2, mitochondrial
  14. Dimethylaniline monooxygenase [N-oxide-forming] 4
  15. Dimethylaniline monooxygenase [N-oxide-forming] 3
  16. NADPH--cytochrome P450 reductase
  17. Dimethylaniline monooxygenase [N-oxide-forming] 1
  18. Methylenetetrahydrofolate reductase
  19. Glutathione reductase, mitochondrial
  20. Heme oxygenase 1
  21. NADPH:adrenodoxin oxidoreductase, mitochondrial
  22. Squalene synthase
  23. Delta(14)-sterol reductase
  24. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
  25. Lanosterol 14-alpha demethylase
  26. 4-trimethylaminobutyraldehyde dehydrogenase
  27. Alpha-aminoadipic semialdehyde dehydrogenase
  28. Aldehyde dehydrogenase family 1 member A3
  29. Aldehyde dehydrogenase, mitochondrial
  30. Fatty aldehyde dehydrogenase
  31. Aldehyde dehydrogenase X, mitochondrial
  32. Pyrroline-5-carboxylate reductase 1, mitochondrial
  33. Pyrroline-5-carboxylate reductase 2
  34. L-xylulose reductase
  35. Glucose-6-phosphate 1-dehydrogenase
  36. GDH/6PGL endoplasmic bifunctional protein
  37. Aldo-keto reductase family 1 member C3
  38. Aldo-keto reductase family 1 member C1
  39. Aldo-keto reductase family 1 member C2
  40. Glyoxylate reductase/hydroxypyruvate reductase
  41. Cytochrome P450 4A11
  42. Methionine synthase reductase
  43. Sepiapterin reductase
  44. Estradiol 17-beta-dehydrogenase 2
  45. Estradiol 17-beta-dehydrogenase 8
  46. 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
  47. Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
  48. Cholesterol 7-alpha-monooxygenase
  49. Alcohol dehydrogenase [NADP+]
  50. Aldehyde dehydrogenase family 3 member B2
  51. 7-dehydrocholesterol reductase
  52. 3-oxo-5-beta-steroid 4-dehydrogenase
  53. Glutamate dehydrogenase 2, mitochondrial
  54. GMP reductase 2
  55. GMP reductase 1
  56. Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
  57. Glutamate dehydrogenase 1, mitochondrial
  58. Glyceraldehyde-3-phosphate dehydrogenase
  59. Biliverdin reductase A
  60. Flavin reductase
  61. Corticosteroid 11-beta-dehydrogenase isozyme 1
  62. Dihydropyrimidine dehydrogenase [NADP+]
  63. Alcohol dehydrogenase class-3
  64. Alcohol dehydrogenase 1B
  65. Alcohol dehydrogenase 1A
  66. Alcohol dehydrogenase 6
  67. Alcohol dehydrogenase 1C
  68. Dihydrofolate reductase
  69. Testosterone 17-beta-dehydrogenase 3
  70. Estradiol 17-beta-dehydrogenase 1
  71. 3-keto-steroid reductase
  72. Alpha-aminoadipic semialdehyde synthase, mitochondrial
  73. Delta-1-pyrroline-5-carboxylate synthase
  74. NADP-dependent malic enzyme
  75. NADP-dependent malic enzyme, mitochondrial
  76. NAD-dependent malic enzyme, mitochondrial
  77. Isocitrate dehydrogenase [NADP], mitochondrial
  78. Isocitrate dehydrogenase [NADP] cytoplasmic
  79. 3-hydroxy-3-methylglutaryl-coenzyme A reductase
  80. NAD(P) transhydrogenase, mitochondrial
  81. C-1-tetrahydrofolate synthase, cytoplasmic
  82. GDP-L-fucose synthase
  83. Nitric oxide synthase, inducible
  84. Nitric oxide synthase, brain
  85. Nitric oxide synthase, endothelial
  86. 10-formyltetrahydrofolate dehydrogenase
  87. Cysteine dioxygenase type 1
  88. Trans-2-enoyl-CoA reductase, mitochondrial
  89. Peroxisomal trans-2-enoyl-CoA reductase
  90. Leukotriene-B(4) omega-hydroxylase 1
  91. Leukotriene-B(4) omega-hydroxylase 2
  92. Cytochrome P450 3A4
  93. Cytochrome P450 2C9
  94. Sterol 26-hydroxylase, mitochondrial
  95. Cytochrome P450 2C19
  96. 6-phosphogluconate dehydrogenase, decarboxylating
  97. 2,4-dienoyl-CoA reductase, mitochondrial
  98. Quinone oxidoreductase
  99. 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
  100. Steroid 17-alpha-hydroxylase/17,20 lyase
  101. Peroxisomal 2,4-dienoyl-CoA reductase
  102. Cytochrome P450 2E1
  103. Cytochrome P450 1B1
  104. Cytochrome P450 2C18
  105. Cytochrome P450 2F1
  106. Cytochrome P450 2B6
  107. Cytochrome P450 3A5
  108. Cytochrome P450 1A1
  109. Cytochrome P450 2A13
  110. Cytochrome P450 3A7
  111. Cytochrome P450 4B1
  112. Cytochrome P450 4Z1
  113. Cytochrome P450 1A2
  114. Cytochrome P450 19A1
  115. Cytochrome P450 2C8
  116. Cytochrome P450 2S1
  117. Cytochrome P450 2J2
  118. Cytochrome P450 2A7
  119. Cytochrome P450 2A6
  120. Neutrophil cytosol factor 2
  121. Neutrophil cytosol factor 4
  122. 25-hydroxycholesterol 7-alpha-hydroxylase
  123. NAD(P)H dehydrogenase [quinone] 1
  124. Glutaredoxin-1
  125. Cytochrome b-245 heavy chain
  126. Ras-related C3 botulinum toxin substrate 2
  127. 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
  128. Putative dimethylaniline monooxygenase [N-oxide-forming] 6
  129. 24-dehydrocholesterol reductase
  130. Neutrophil cytosol factor 1
  131. Cytochrome b-245 light chain
  132. Kynurenine 3-monooxygenase
  133. Dehydrogenase/reductase SDR family member 9
  134. Vitamin D 25-hydroxylase
  135. Retinol dehydrogenase 12
  136. 3-ketodihydrosphingosine reductase
  137. Dual oxidase 2
  138. Not Available
  139. Cholesterol 24-hydroxylase
  140. Retinol dehydrogenase 8
  141. Retinol dehydrogenase 14
  142. Retinol dehydrogenase 11
  143. 24-hydroxycholesterol 7-alpha-hydroxylase
  144. 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase
  145. Retinol dehydrogenase 10
  146. Dual oxidase 1
  147. Thioredoxin reductase 3
  148. Probable 10-formyltetrahydrofolate dehydrogenase ALDH1L2
  149. Fatty acyl-CoA reductase 1
  150. Fatty acyl-CoA reductase 2
  151. Cytochrome P450 4A22
  152. cDNA, FLJ95780, Homo sapiens carbonyl reductase 1 (CBR1), mRNA (Carbonyl reductase 1, isoform CRA_d)
  153. cDNA FLJ78181, highly similar to Homo sapiens aldo-keto reductase family 1, member C3
  154. cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
  155. cDNA FLJ76781, highly similar to Homo sapiens cytochrome P450, family 27, subfamily A, polypeptide 1
  156. cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
  157. Putative uncharacterized protein DKFZp686B0215
  158. Dihydrofolate reductase
  159. Monofunctional C1-tetrahydrofolate synthase, mitochondrial
  160. Glyoxylate reductase/hydroxypyruvate reductase
  161. Acyl-CoA synthetase family member 4
  162. Aminoadipate-semialdehyde synthase
  163. Putative uncharacterized protein PGD
  164. Cytochrome P450, family 1, subfamily A, polypeptide 1
  165. NADPH oxidase 5
  166. NADPH oxidase 3
  167. NADPH oxidase 4
  168. Iodotyrosine dehalogenase 1
  169. Peroxisomal coenzyme A diphosphatase NUDT7
  170. Prostaglandin reductase 2
  171. Short-chain dehydrogenase/reductase 3
  172. Uncharacterized protein ENSP00000310075
  173. Oxidoreductase HTATIP2
  174. Putative neutrophil cytosol factor 1B
  175. Putative neutrophil cytosol factor 1C
  176. NADPH oxidase activator 1
  177. HSD3B2 protein
  178. Cytochrome P450, family 21, subfamily A, polypeptide 2
  179. Aldehyde dehydrogenase 3 family, member B1, isoform CRA_c
  180. cDNA FLJ76220, highly similar to Homo sapiens quinoid dihydropteridine reductase (QDPR), mRNA (Quinoid dihydropteridine reductase, isoform CRA_d)
  181. Cytochrome P450, family 3, subfamily A, polypeptide 7
  182. Cytochrome P450 2D6
  183. Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
  184. Cytochrome P450
  185. Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e
  186. Hydroxysteroid (11-beta) dehydrogenase 2
  187. cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
  188. Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
  189. Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
  190. cDNA FLJ77672
  191. cDNA FLJ78495, highly similar to Homo sapiens leukotriene B4 12- hydroxydehydrogenase (LTB4DH), mRNA (Leukotriene B4 12- hydroxydehydrogenase, isoform CRA_a)
  192. cDNA FLJ77934, highly similar to Homo sapiens flavin containing monooxygenase 1 (FMO1), mRNA (Flavin containing monooxygenase 1, isoform CRA_a)
  193. Flavin containing monooxygenase 2
  194. Nitric oxide synthase 2A (Inducible, hepatocytes)
  195. Putative uncharacterized protein SC4MOL
  196. 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
  197. Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c)
  198. cDNA, FLJ92898, Homo sapiens aminoadipate-semialdehydedehydrogenase-phosphopantetheinyl transferase (AASDHPPT), mRNA (Aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, isoform CRA_b)
  199. cDNA, FLJ93424, highly similar to Homo sapiens cytochrome P450, family 2, subfamily A, polypeptide 6 (CYP2A6), mRNA (Cytochrome P450, family 2, subfamily A, polypeptide 6)
  200. cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b)
  201. cDNA, FLJ94621, Homo sapiens hydroxysteroid (11-beta) dehydrogenase 1 (HSD11B1), mRNA (Hydroxysteroid (11-beta) dehydrogenase 1, isoform CRA_a)
  202. cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
  203. cDNA, FLJ93978, Homo sapiens aldo-keto reductase family 1, member B1 (aldosereductase) (AKR1B1), mRNA (Aldo-keto reductase family 1, member B1 (Aldose reductase), isoform CRA_a)
  204. Putative uncharacterized protein
  205. cDNA FLJ45935 fis, clone PLACE7003985, highly similar to Estradiol 17-beta-dehydrogenase 1 (Hydroxysteroid (17-beta) dehydrogenase 1)
  206. cDNA, FLJ93594, Homo sapiens hydroxysteroid (17-beta) dehydrogenase 2 (HSD17B2),mRNA (Hydroxysteroid (17-beta) dehydrogenase 2)
  207. cDNA, FLJ93011, Homo sapiens isocitrate dehydrogenase 2 (NADP+), mitochondrial(IDH2), mRNA (Isocitrate dehydrogenase 2 (NADP+), mitochondrial, isoform CRA_a)
  208. cDNA, FLJ92680, Homo sapiens follicular lymphoma variant translocation 1 (FVT1),mRNA (Follicular lymphoma variant translocation 1, isoform CRA_a)
  209. cDNA, FLJ94122, Homo sapiens tissue specific transplantation antigen P35B (TSTA3),mRNA (Tissue specific transplantation antigen P35B, isoform CRA_b)
  210. cDNA, FLJ92690, Homo sapiens NAD(P)H dehydrogenase, quinone 1 (NQO1), mRNA (NAD(P)H dehydrogenase, quinone 1, isoform CRA_c)
  211. cDNA, FLJ93696, highly similar to Homo sapiens flavin containing monooxygenase 3 (FMO3), mRNA (Flavin containing monooxygenase 3, isoform CRA_b)
  212. NOS1 mutant
  213. Cytochrome P450, family 7, subfamily B, polypeptide 1
  214. cDNA, FLJ94971, highly similar to Homo sapiens cysteine dioxygenase, type I (CDO1), mRNA (Cysteine dioxygenase, type I)
  215. L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
Enzyme 1 [top]
Enzyme 1 ID 5264
Enzyme 1 Name Fatty acid synthase
Enzyme 1 Synonyms
  1. [Acyl-carrier-protein] S-acetyltransferase
  2. [Acyl-carrier-protein] S-malonyltransferase
  3. 3-oxoacyl-[acyl-carrier-protein] synthase
  4. 3-oxoacyl-[acyl-carrier-protein] reductase
  5. 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
  6. Enoyl-[acyl-carrier-protein] reductase
  7. Oleoyl-[acyl-carrier-protein] hydrolase
Enzyme 1 Gene Name FASN
Enzyme 1 Protein Sequence >Fatty acid synthase 
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
Enzyme 1 Number of Residues 2511
Enzyme 1 Molecular Weight 273424.1
Enzyme 1 Theoretical pI 6.41
Enzyme 1 GO Classification
Function
  • acyl carrier activity
  • amino acid binding
  • binding
  • carboxylic acid binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • phosphopantetheine binding
  • substrate-specific transporter activity
  • transferase activity
  • transition metal ion binding
  • transporter activity
  • zinc ion binding
Process
  • biosynthetic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 1 General Function Involved in transferase activity
Enzyme 1 Specific Function Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein
Enzyme 1 Pathways
Enzyme 1 Reactions
  • a (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = a hexadec-2-enoyl-[acyl-carrier protein] + H2O [RN:R04462]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 41872631 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P49327 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FAS_HUMAN Link Image
Enzyme 1 PDB ID 1XKT Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >7536 bp 
ATGGAGGAGGTGGTGATTGCCGGCATGTCCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCGGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGTCACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAATGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCCGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
CGGGTGTACGCCACCATCCTGAACGCCGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCCTCAGGGGATATCCAGGAGCAGCTCATCCGCTCGTTGTACCAGTCGGCC
GGAGTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGCACAGGCACCAAGGTGGGC
GACCCCCAGGAGCTGAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTG
CTCATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTGGCAGCC
CTGGCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCAT
AGCCCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCC
CTGCCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACGTG
CACATCATCCTGAGGCCCAACACGCAGCCGCCCCCCGCACCCGCCCCACATGCCACCCTG
CCCCGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAG
GGCCTCCGGCACAGCCAGGACCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTC
CCCGCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGCGCGGTGGCCCA
GAGGTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGC
ACACAGTGGCGCGGGATGGGGCTGAGCCTCATGCGCCTGGACCGCTTCCGAGATTCCATC
CTACGCTCCGATGAGGCTGTGAAGCCATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGC
ACAGACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAG
ATAGGCCTCATAGACCTGCTGAGCTGCATGGGGCTGAGGCCAGATGGCATCGTCGGCCAC
TCCCTGGGGGAGGTGGCCTGTGGCTACGCCGACGGCTGCCTGTCCCAGGAGGAGGCCGTC
CTCGCTGCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCATCTCCCGCCGGGCGCCATG
GCAGCCGTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCGGGCGTGGTGCCC
GCCTGCCACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAG
TTCGTGGAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATG
GCCTTCCACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAG
GTGATCCGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCC
CAGTGGCACAGCAGCCTGGCACGCACGTCCTCCGCCGAGTACAATGTCAACAACCTGGTG
AGCCCTGTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAG
ATCGCGCCCCACGCCCTGCTGCAGGCTGTCCTGAAGCGTGGCCTGAAGCCGAGCTGCACC
ATCATCCCCCTGATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATC
GGCAGGCTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAG
TTCCCAGCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTG
GCCTGGGACGTGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCGCC
ATCTACAACATCGACACCAGCTCCGAGTCTCCTGACCACTACCTGGTGGACCACACCCTC
GACGGTCGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCC
CGCGCCCTGGGCCTGGGCGTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCTGCAC
CAGGCCACCATCCTGCCCAAGACTGGGACAGTGTCCCTGGAGGTACGGCTCCTGGAGGCC
TCCCGTGCCTTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAG
TGGGATGACCCTGACCCCAGGCTCTTCGACCACCCGGAAAGCCCCACCCCCAACCCCACG
GAGCCCCTCTTCCTGGCCCAGGCTGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGAC
TACGGCCCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTG
CTGTGGAAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGC
TCGGCCAAGCACGGCCTGTACCTGCCCACCCGTGTCACCGCCATCCACATCGACCCTGCC
ACCCACAGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTG
AGCAGGTGGCTGAGGGTCACAGTGGCCGGAGGCGTCCACATCTCCGGGCTCCACACTGAG
TCGGCCCCGCGGCGGCAGCAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACT
CCCCACACGGAGGAGGGGTGCCTGTCTGAGCGCGCTGCCCTGCAGGAGGAGCTGCAACTG
TGCAAGGGGCTGGTGCAGGCACTGCAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTG
GTGCCCGGACTGGATGGGGCCCAGATCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGG
CTGTTGTCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAG
GTGCTGGCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGAC
TCCCCGGCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATG
AAGGTGGTGGAGGTGCTGGCTGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTC
AGCCCCCATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTG
GAGGCTGCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCA
GACCCTGCCCCCAGCGCCCTGGGCAGCGCCGACCTCCTGGTGTGCAACTGTGCTGTGGCT
GCCCTCGGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGC
TTTCTGCTCCTGCACACACTGCTCCGGGGGCACCCCCTCGGGGACATCGTGGCCTTCCTC
ACCTCCACTGAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTC
TTCTCCAGGGTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCTCCACGCTC
TTCCTGTGCCGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACC
AGCTTCCGCTGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCT
GTGTGGCTGAAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTC
CGCCGAGAGCCCGGCGGGAACCGCCTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACC
TCCCACGTCCCGGAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGAC
CTGGTGATGAACGTCTACCGCGACGGGGCCTGGGGGGCTTTCCGCCACTTCCTGCTGGAG
GAGGACAAGCCTGAGGAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGAC
CTGTCCTCCATCCGCTGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGC
GCCCAGCTCTGCACGGTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACT
GGCAAGCTGTCCCCTGATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGT
ATGGAGTTCTCGGGCCGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAG
GGCCTGGCCACCTCTGTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGG
ACGCTGGAGGAGGCGGCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTG
GTGCGTGGGCGGGTGCGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTG
GGCCAGGCCGCCATCGCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGG
TCGGCTGAGAAGCGGGCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTC
GCCAACTCCCGGGACACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGC
GTTGACCTGGTCTTGAACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTG
GCTACGCACGGTCGCTTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTC
GGCATGGCTATCTTCCTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTC
AACGAGAGCAGTGCTGACTGGCGGGAGGTGTGGGCGCTTGTGCAGGCCGGCATCCGGGAT
GGGGTGGTACGGCCCCTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTC
CGCTACATGGCCCAAGGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAG
CCGGAGGCAGTGCTGAAGGGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTC
TGCCCGGCCCACAAGAGCTACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTG
GCGCAGTGGCTGATACAGCGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATC
CGGACAGGCTACCAGGCCAAGCAGGTCCGCCGGTGGAGGCGCCAGGGCGTACAGGTGCAG
GTGTCCACCAGCAACATCAGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCG
CAGCTTGGGCCCGTGGGCGGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTG
GAGAACCAGACCCCAGAGTTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTG
AACCTGGACAGGGTGACCCGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCC
TCTGTGAGCTGCGGGCGTGGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCC
ATGGAGCGTATCTGTGAGAAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGG
GGCGCCATCGGCGACGTGGGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTC
AGTGGCACGCTGCCCCAGCGCATGGCGTCCTGCCTGGAGGTGCTGGACCTCTTCCTGAAC
CAGCCCCACATGGTCCTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGAC
AGGGACAGCCAGCGGGACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTG
GCTGCTGTCAACCTGGACAGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGTG
GAGGTGCGCCAGACGCTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGG
CAACTCACGCTCCGGAAACTGCAGGAGCTGTCCTCAAAGGCGGATGAGGCCAGCGAGCTG
GCATGCCCCACGCCCAAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGC
TCCCTGCTGGTGAACCCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCG
GAGCGGCCCCTGTTCCTGGTGCACCCAATCGAGGGCTCCACCACCGTGTTCCACAGCCTG
GCCTCCCGGCTCAGCATCCCCACCTATGGCCTGCAGTGCACCCGAGCTGCGCCCCTTGAC
AGCATCCACAGCCTGGCTGCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGC
CCCTACCGCGTGGCCGGCTACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAG
CTGCAGGCCCAGCAGAGCCCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCG
CCCACCTACGTACTGGCCTACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTGAG
GCTGAGGCTGAGACGGAGGCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCAC
AACAGGGTGCTGGAGGCGCTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCC
GTGGACCTGATCATCAAGAGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCC
CGGTCCTTCTACTACAAGCTGCGTGCCGCTGAGCAGTACACACCCAAGGCCAAGTACCAT
GGCAACGTGATGCTACTGCGCGCCAAGACGGGTGGCGCCTACGGCGAGGACCTGGGCGCG
GACTACAACCTCTCCCAGGTATGCGACGGGAAAGTATCCGTCCACGTCATCGAGGGTGAC
CACCGCACGCTGCTGGAGGGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCC
CTGGCTGAGCCACGCGTGAGCGTGCGGGAGGGCTAG
Enzyme 1 GenBank Gene ID NM_004104.4 Link Image
Enzyme 1 GeneCard ID FASN Link Image
Enzyme 1 GenAtlas ID FASN Link Image
Enzyme 1 HGNC ID HGNC:3594 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17q25
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed Link Image]
  2. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed Link Image]
  5. Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  14. Brink J, Ludtke SJ, Yang CY, Gu ZW, Wakil SJ, Chiu W: Quaternary structure of human fatty acid synthase by electron cryomicroscopy. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):138-43. Epub 2001 Dec 26. [PubMed Link Image]
  15. Chakravarty B, Gu Z, Chirala SS, Wakil SJ, Quiocho FA: Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15567-72. Epub 2004 Oct 26. [PubMed Link Image]
  16. Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U: Mechanism and substrate recognition of human holo ACP synthase. Chem Biol. 2007 Nov;14(11):1243-53. [PubMed Link Image]
  17. Pemble CW 4th, Johnson LC, Kridel SJ, Lowther WT: Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat Struct Mol Biol. 2007 Aug;14(8):704-9. Epub 2007 Jul 8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5303
Enzyme 2 Name Aldo-keto reductase family 1 member C4
Enzyme 2 Synonyms
  1. 3-alpha-HSD1
  2. 3-alpha-hydroxysteroid dehydrogenase type I
  3. Chlordecone reductase
  4. CDR
  5. Dihydrodiol dehydrogenase 4
  6. DD-4
  7. DD4
  8. HAKRA
Enzyme 2 Gene Name AKR1C4
Enzyme 2 Protein Sequence >Aldo-keto reductase family 1 member C4 
MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPM
ALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKP
GLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPV
LCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN
RNYRYVVMDFLMDHPDYPFSDEY
Enzyme 2 Number of Residues 323
Enzyme 2 Molecular Weight 37066.5
Enzyme 2 Theoretical pI 6.93
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha- androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20- alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route
Enzyme 2 Pathways
Enzyme 2 Reactions
  • chlordecone alcohol + NADP+ = chlordecone + NADPH + H+ [RN:R03716]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 7328948 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P17516 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AK1C4_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >972 bp 
ATGGATCCCAAATATCAGCGTGTAGAGCTAAATGATGGTCACTTCATGCCCGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGGAACAGAGCTGTAGAGGTCACCAAATTA
GCAATAGAAGCTGGCTTCCGCCATATTGATTCTGCTTATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCACTTTCTTTCAACCACAGATGGTCCAACCAGCCTTGGAA
AGCTCACTGAAAAAACTTCAACTGGACTATGTTGACCTCTATCTTCTTCATTTCCCAATG
GCTCTCAAGCCAGGTGAGACGCCACTACCAAAAGATGAAAATGGAAAAGTAATATTCGAC
ACAGTGGATCTCTCTGCCACATGGGAGGTCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCAAACTTCAACTGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCTTACCTCAACCAGAGC
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCCACAGTGCTCTGGGA
ACCCAACGACATAAACTATGGGTGGACCCAAACTCCCCAGTTCTTTTGGAGGACCCAGTT
CTTTGTGCCTTAGCAAAGAAACACAAACGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGGATCAGAGAGAAC
ATCCAGGTTTTTGAATTCCAGTTGACATCAGAGGATATGAAAGTTCTAGATGGTCTAAAC
AGAAATTATCGATATGTTGTCATGGATTTTCTTATGGACCATCCTGATTATCCATTTTCA
GATGAATATTAG
Enzyme 2 GenBank Gene ID AB031085 Link Image
Enzyme 2 GeneCard ID AKR1C4 Link Image
Enzyme 2 GenAtlas ID AKR1C4 Link Image
Enzyme 2 HGNC ID HGNC:387 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 10p15.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  2. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed Link Image]
  3. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  4. Kume T, Iwasa H, Shiraishi H, Yokoi T, Nagashima K, Otsuka M, Terada T, Takagi T, Hara A, Kamataki T: Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver. Pharmacogenetics. 1999 Dec;9(6):763-71. [PubMed Link Image]
  5. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  6. Dufort I, Labrie F, Luu-The V: Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution. J Clin Endocrinol Metab. 2001 Feb;86(2):841-6. [PubMed Link Image]
  7. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Winters CJ, Molowa DT, Guzelian PS: Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry. 1990 Jan 30;29(4):1080-7. [PubMed Link Image]
  10. Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed Link Image]
  11. Binstock JM, Iyer RB, Hamby CV, Fried VA, Schwartz IS, Weinstein BI, Southren AL: Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase. Biochem Biophys Res Commun. 1992 Sep 16;187(2):760-6. [PubMed Link Image]
  12. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5304
Enzyme 3 Name Carbonyl reductase [NADPH] 1
Enzyme 3 Synonyms
  1. 15-hydroxyprostaglandin dehydrogenase [NADP+]
  2. NADPH-dependent carbonyl reductase 1
  3. Prostaglandin 9-ketoreductase
  4. Prostaglandin-E(2) 9-reductase
Enzyme 3 Gene Name CBR1
Enzyme 3 Protein Sequence >Carbonyl reductase [NADPH] 1 
MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD
VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK
KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA
TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
Enzyme 3 Number of Residues 277
Enzyme 3 Molecular Weight 30374.7
Enzyme 3 Theoretical pI 8.49
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+ [RN:R04552]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P16152 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CBR1_HUMAN Link Image
Enzyme 3 PDB ID 1WMA Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >834 bp 
ATGTCGTCCGGCATCCATGTAGCGCTGGTGACTGGAGGCAACAAGGGCATCGGCTTGGCC
ATCGTGCGCGACCTGTGCCGGCTGTTCTCGGGGGACGTGGTGCTCACGGCGCGGGACGTG
ACGCGGGGCCAGGCGGCCGTACAGCAGCTGCAGGCGGAGGGCCTGAGCCCGCGCTTCCAC
CAGCTGGACATCGACGATCTGCAGAGCATCCGCGCCCTGCGCGACTTCCTGCGCAAGGAG
TACGGGGGCCTGGACGTGCTGGTCAACAACGCGGGCATCGCCTTCAAGGTTGCTGATCCC
ACACCCTTTCATATTCAAGCTGAAGTGACGATGAAAACAAATTTCTTTGGTACCCGAGAT
GTGTGCACAGAATTACTCCCTCTAATAAAACCCCAAGGGAGAGTGGTGAACGTATCTAGC
ATCATGAGCGTCAGAGCCCTTAAAAGCTGCAGCCCAGAGCTGCAGCAGAAGTTCCGCAGT
GAGACCATCACTGAGGAGGAGCTGGTGGGGCTCATGAACAAGTTTGTGGAGGATACAAAG
AAGGGAGTGCACCAGAAGGAGGGCTGGCCCAGCAGCGCATACGGGGTGACGAAGATTGGC
GTCACCGTTCTGTCCAGGATCCACGCCAGGAAACTGAGTGAGCAGAGGAAAGGGGACAAG
ATCCTCCTGAATGCCTGCTGCCCAGGGTGGGTGAGAACTGACATGGCGGGACCCAAGGCC
ACCAAGAGCCCAGAAGAAGGTGCAGAGACCCCTGTGTACTTGGCCCTTTTGCCCCCAGAT
GCTGAGGGTCCCCATGGACAATTTGTTTCAGAGAAGAGAGTTGAACAGTGGTGA
Enzyme 3 GenBank Gene ID J04056 Link Image
Enzyme 3 GeneCard ID CBR1 Link Image
Enzyme 3 GenAtlas ID CBR1 Link Image
Enzyme 3 HGNC ID HGNC:1548 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 21q22.13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Wermuth B, Bohren KM, Heinemann G, von Wartburg JP, Gabbay KH: Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein. J Biol Chem. 1988 Nov 5;263(31):16185-8. [PubMed Link Image]
  2. Forrest GL, Akman S, Krutzik S, Paxton RJ, Sparkes RS, Doroshow J, Felsted RL, Glover CJ, Mohandas T, Bachur NR: Induction of a human carbonyl reductase gene located on chromosome 21. Biochim Biophys Acta. 1990 Apr 6;1048(2-3):149-55. [PubMed Link Image]
  3. Forrest GL, Akman S, Doroshow J, Rivera H, Kaplan WD: Genomic sequence and expression of a cloned human carbonyl reductase gene with daunorubicin reductase activity. Mol Pharmacol. 1991 Oct;40(4):502-7. [PubMed Link Image]
  4. Watanabe K, Sugawara C, Ono A, Fukuzumi Y, Itakura S, Yamazaki M, Tashiro H, Osoegawa K, Soeda E, Nomura T: Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. Genomics. 1998 Aug 15;52(1):95-100. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Krook M, Ghosh D, Stromberg R, Carlquist M, Jornvall H: Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):502-6. [PubMed Link Image]
  9. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  10. Gonzalez-Covarrubias V, Kalabus JL, Blanco JG: Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER). Pharm Res. 2008 Jul;25(7):1730-4. Epub 2008 May 1. [PubMed Link Image]
  11. Tanaka M, Bateman R, Rauh D, Vaisberg E, Ramachandani S, Zhang C, Hansen KC, Burlingame AL, Trautman JK, Shokat KM, Adams CL: An unbiased cell morphology-based screen for new, biologically active small molecules. PLoS Biol. 2005 May;3(5):e128. Epub 2005 Apr 5. [PubMed Link Image]
  12. Bateman R, Rauh D, Shokat KM: Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct. Org Biomol Chem. 2007 Oct 21;5(20):3363-7. Epub 2007 Aug 29. [PubMed Link Image]
  13. Bateman RL, Rauh D, Tavshanjian B, Shokat KM: Human carbonyl reductase 1 is an S-nitrosoglutathione reductase. J Biol Chem. 2008 Dec 19;283(51):35756-62. Epub 2008 Sep 29. [PubMed Link Image]
  14. Gonzalez-Covarrubias V, Ghosh D, Lakhman SS, Pendyala L, Blanco JG: A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity. Drug Metab Dispos. 2007 Jun;35(6):973-80. Epub 2007 Mar 7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5305
Enzyme 4 Name Dehydrogenase/reductase SDR family member 4
Enzyme 4 Synonyms
  1. NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase
  2. CR
  3. PHCR
  4. NADPH-dependent retinol dehydrogenase/reductase
  5. NRDR
  6. humNRDR
  7. Peroxisomal short-chain alcohol dehydrogenase
  8. PSCD
  9. SCAD-SRL
  10. Short-chain dehydrogenase/reductase family member 4
Enzyme 4 Gene Name DHRS4
Enzyme 4 Protein Sequence >Dehydrogenase/reductase SDR family member 4 
MHKAGLLGLCARAWNSVRMASSGMTRRDPLANKVALVTASTDGIGFAIARRLAQDGAHVV
VSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVKLHGGIDILVSNAAVN
PFFGSIMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFS
PYNVSKTALLGLTKTLAIELAPRNIRVNCLAPGLIKTSFSRMLWMDKEKEESMKETLRIR
RLGEPEDCAGIVSFLCSEDASYITGETVVVGGGTPSRL
Enzyme 4 Number of Residues 278
Enzyme 4 Molecular Weight 29536.9
Enzyme 4 Theoretical pI 8.76
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 4 General Function Involved in oxidoreductase activity
Enzyme 4 Specific Function Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co- factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones
Enzyme 4 Pathways
Enzyme 4 Reactions
  • R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ [RN:R03557]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 32483357 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9BTZ2 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DHRS4_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >837 bp 
ATGCACAAGGCGGGGCTGCTAGGCCTCTGTGCCCGGGCTTGGAATTCGGTGCGGATGGCC
AGCTCCGGGATGACCCGCCGGGACCCGCTCGCAAATAAGGTGGCCCTGGTAACGGCCTCC
ACCGACGGGATCGGCTTCGCCATCGCCCGGCGTTTGGCCCAGGACGGGGCCCATGTGGTC
GTCAGCAGCCGGAAGCAGCAGAATGTGGACCAGGCGGTGGCCACGCTGCAGGGGGAGGGG
CTGAGCGTGACGGGCACCGTGTGCCATGTGGGGAAGGCGGAGGACCGGGAGCGGCTGGTG
GCCACGGCTGTGAAGCTTCATGGAGGTATCGATATCCTAGTCTCCAATGCTGCTGTCAAC
CCTTTCTTTGGAAGCATAATGGATGTCACTGAGGAGGTGTGGGACAAGACTCTGGACATT
AATGTGAAGGCCCCAGCCCTGATGACAAAGGCAGTGGTGCCAGAAATGGAGAAACGAGGA
GGCGGCTCAGTGGTGATCGTGTCTTCCATAGCAGCCTTCAGTCCATCTCCTGGCTTCAGT
CCTTACAATGTCAGTAAAACAGCCTTGCTGGGCCTGACCAAGACCCTGGCCATAGAGCTG
GCCCCAAGGAACATTAGGGTGAACTGCCTAGCACCTGGACTTATCAAGACTAGCTTCAGC
AGGATGCTCTGGATGGACAAGGAAAAAGAGGAAAGCATGAAAGAAACCCTGCGGATAAGA
AGGTTAGGCGAGCCAGAGGATTGTGCTGGCATCGTGTCTTTCCTGTGCTCTGAAGATGCC
AGCTACATCACTGGGGAAACAGTGGTGGTGGGTGGAGGAACCCCGTCCCGCCTCTGA
Enzyme 4 GenBank Gene ID NM_021004.2 Link Image
Enzyme 4 GeneCard ID DHRS4 Link Image
Enzyme 4 GenAtlas ID DHRS4 Link Image
Enzyme 4 HGNC ID HGNC:16985 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 14q11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Fransen M, Van Veldhoven PP, Subramani S: Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase. Biochem J. 1999 Jun 1;340 ( Pt 2):561-8. [PubMed Link Image]
  2. Du J, Huang DY, Liu GF, Wang GL, Xu XL, Wang B, Zhu L: CDNA cloning of a short isoform of human liver NADP (H) -dependent retinol dehydrogenase/reductase and analysis of its characteristics. Yi Chuan Xue Bao. 2004 Jul;31(7):661-7. [PubMed Link Image]
  3. Song XH, Liang B, Liu GF, Li R, Xie JP, Du K, Huang DY: Expression of a novel alternatively spliced variant of NADP(H)-dependent retinol dehydrogenase/reductase with deletion of exon 3 in cervical squamous carcinoma. Int J Cancer. 2007 Apr 15;120(8):1618-26. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  6. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5306
Enzyme 5 Name Carbonyl reductase [NADPH] 3
Enzyme 5 Synonyms
  1. NADPH-dependent carbonyl reductase 3
Enzyme 5 Gene Name CBR3
Enzyme 5 Protein Sequence >Carbonyl reductase [NADPH] 3 
MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFH
QLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRN
MCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTK
NEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDS
IRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW
Enzyme 5 Number of Residues 277
Enzyme 5 Molecular Weight 30850.0
Enzyme 5 Theoretical pI 6.06
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 5 General Function Involved in oxidoreductase activity
Enzyme 5 Specific Function Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ [RN:R03557]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 3702679 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O75828 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CBR3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >834 bp 
ATGTCGTCCGGCATCCATGTAGCGCTGGTGACTGGAGGCAACAAGGGCATCGGCTTGGCC
ATCGTGCGCGACCTGTGCCGGCTGTTCTCGGGGGACGTGGTGCTCACGGCGCGGGACGTG
ACGCGGGGCCAGGCGGCCGTACAGCAGCTGCAGGCGGAGGGCCTGAGCCCGCGCTTCCAC
CAGCTGGACATCGACGATCTGCAGAGCATCCGCGCCCTGCGCGACTTCCTGCGCAAGGAG
TACGGGGGCCTGGACGTGCTGGTCAACAACGCGGGCATCGCCTTCAAGGTTGCTGATCCC
ACACCCTTTCATATTCAAGCTGAAGTGACGATGAAAACAAATTTCTTTGGTACCCGAGAT
GTGTGCACAGAATTACTCCCTCTAATAAAACCCCAAGGGAGAGTGGTGAACGTATCTAGC
ATCATGAGCGTCAGAGCCCTTAAAAGCTGCAGCCCAGAGCTGCAGCAGAAGTTCCGCAGT
GAGACCATCACTGAGGAGGAGCTGGTGGGGCTCATGAACAAGTTTGTGGAGGATACAAAG
AAGGGAGTGCACCAGAAGGAGGGCTGGCCCAGCAGCGCATACGGGGTGACGAAGATTGGC
GTCACCGTTCTGTCCAGGATCCACGCCAGGAAACTGAGTGAGCAGAGGAAAGGGGACAAG
ATCCTCCTGAATGCCTGCTGCCCAGGGTGGGTGAGAACTGACATGGCGGGACCCAAGGCC
ACCAAGAGCCCAGAAGAAGGTGCAGAGACCCCTGTGTACTTGGCCCTTTTGCCCCCAGAT
GCTGAGGGTCCCCATGGACAATTTGTTTCAGAGAAGAGAGTTGAACAGTGGTGA
Enzyme 5 GenBank Gene ID AB003151 Link Image
Enzyme 5 GeneCard ID CBR3 Link Image
Enzyme 5 GenAtlas ID CBR3 Link Image
Enzyme 5 HGNC ID HGNC:1549 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 21q22.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Watanabe K, Sugawara C, Ono A, Fukuzumi Y, Itakura S, Yamazaki M, Tashiro H, Osoegawa K, Soeda E, Nomura T: Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. Genomics. 1998 Aug 15;52(1):95-100. [PubMed Link Image]
  2. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Miura T, Nishinaka T, Terada T: Different functions between human monomeric carbonyl reductase 3 and carbonyl reductase 1. Mol Cell Biochem. 2008 Aug;315(1-2):113-21. Epub 2008 May 21. [PubMed Link Image]
  5. Lakhman SS, Ghosh D, Blanco JG: Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3). Drug Metab Dispos. 2005 Feb;33(2):254-7. Epub 2004 Nov 10. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5320
Enzyme 6 Name Aldose reductase
Enzyme 6 Synonyms
  1. AR
  2. Aldehyde reductase
  3. Aldo-keto reductase family 1 member B1
Enzyme 6 Gene Name AKR1B1
Enzyme 6 Protein Sequence >Aldose reductase 
MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQ
EKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK
EFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKP
AVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAK
HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCA
LLSCTSHKDYPFHEEF
Enzyme 6 Number of Residues 316
Enzyme 6 Molecular Weight 35853.1
Enzyme 6 Theoretical pI 6.99
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 6 General Function Involved in oxidoreductase activity
Enzyme 6 Specific Function Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies
Enzyme 6 Pathways
Enzyme 6 Reactions
  • alditol + NAD(P)+ = aldose + NAD(P)H + H+ [RN:R02819 R02820]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2687578 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P15121 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ALDR_HUMAN Link Image
Enzyme 6 PDB ID 1T40 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >951 bp 
ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC
TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC
CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG
GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG
TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG
AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG
GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC
ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC
AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT
GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC
CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG
GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG
CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG
ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA
CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC
TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA
Enzyme 6 GenBank Gene ID AF032455 Link Image
Enzyme 6 GeneCard ID AKR1B1 Link Image
Enzyme 6 GenAtlas ID AKR1B1 Link Image
Enzyme 6 HGNC ID HGNC:381 Link Image
Enzyme 6 Chromosome Location 7
Enzyme 6 Locus 7q35
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed Link Image]
  2. Chung S, LaMendola J: Cloning and sequence determination of human placental aldose reductase gene. J Biol Chem. 1989 Sep 5;264(25):14775-7. [PubMed Link Image]
  3. Graham A, Hedge PJ, Powell SJ, Riley J, Brown L, Gammack A, Carey F, Markham AF: Nucleotide sequence of cDNA for human aldose reductase. Nucleic Acids Res. 1989 Oct 25;17(20):8368. [PubMed Link Image]
  4. Grundmann U, Bohn H, Obermeier R, Amann E: Cloning and prokaryotic expression of a biologically active human placental aldose reductase. DNA Cell Biol. 1990 Apr;9(3):149-57. [PubMed Link Image]
  5. Nishimura C, Matsuura Y, Kokai Y, Akera T, Carper D, Morjana N, Lyons C, Flynn TG: Cloning and expression of human aldose reductase. J Biol Chem. 1990 Jun 15;265(17):9788-92. [PubMed Link Image]
  6. Graham A, Brown L, Hedge PJ, Gammack AJ, Markham AF: Structure of the human aldose reductase gene. J Biol Chem. 1991 Apr 15;266(11):6872-7. [PubMed Link Image]
  7. Ko BC, Ruepp B, Bohren KM, Gabbay KH, Chung SS: Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J Biol Chem. 1997 Jun 27;272(26):16431-7. [PubMed Link Image]
  8. Hartmann TB, Thiel D, Dummer R, Schadendorf D, Eichmuller S: SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma. Br J Dermatol. 2004 Feb;150(2):252-8. [PubMed Link Image]
  9. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  10. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  11. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  12. Ferraretto A, Negri A, Giuliani A, De Grada L, Fuhrman Conti AM, Ronchi S: Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. Biochim Biophys Acta. 1993 Feb 17;1175(3):283-8. [PubMed Link Image]
  13. Morjana NA, Lyons C, Flynn TG: Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem. 1989 Feb 15;264(5):2912-9. [PubMed Link Image]
  14. Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK: Identification of the reactive cysteine residue in human placenta aldose reductase. Biochim Biophys Acta. 1993 Aug 7;1164(3):268-72. [PubMed Link Image]
  15. Jaquinod M, Potier N, Klarskov K, Reymann JM, Sorokine O, Kieffer S, Barth P, Andriantomanga V, Biellmann JF, Van Dorsselaer A: Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. Eur J Biochem. 1993 Dec 15;218(3):893-903. [PubMed Link Image]
  16. Tarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM: Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem. 1993 Dec 5;268(34):25687-93. [PubMed Link Image]
  17. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  18. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  20. Wilson DK, Bohren KM, Gabbay KH, Quiocho FA: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science. 1992 Jul 3;257(5066):81-4. [PubMed Link Image]
  21. Borhani DW, Harter TM, Petrash JM: The crystal structure of the aldose reductase.NADPH binary complex. J Biol Chem. 1992 Dec 5;267(34):24841-7. [PubMed Link Image]
  22. Wilson DK, Tarle I, Petrash JM, Quiocho FA: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):9847-51. [PubMed Link Image]
  23. Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH: The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry. 1997 Dec 23;36(51):16134-40. [PubMed Link Image]
  24. Ruiz F, Hazemann I, Mitschler A, Joachimiak A, Schneider T, Karplus M, Podjarny A: The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48. Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1347-54. Epub 2004 Jul 21. [PubMed Link Image]
  25. Howard EI, Sanishvili R, Cachau RE, Mitschler A, Chevrier B, Barth P, Lamour V, Van Zandt M, Sibley E, Bon C, Moras D, Schneider TR, Joachimiak A, Podjarny A: Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A. Proteins. 2004 Jun 1;55(4):792-804. [PubMed Link Image]
  26. Steuber H, Zentgraf M, Podjarny A, Heine A, Klebe G: High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group. J Mol Biol. 2006 Feb 10;356(1):45-56. Epub 2005 Nov 10. [PubMed Link Image]
  27. Biadene M, Hazemann I, Cousido A, Ginell S, Joachimiak A, Sheldrick GM, Podjarny A, Schneider TR: The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop. Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):665-72. Epub 2007 May 15. [PubMed Link Image]
  28. Steuber H, Zentgraf M, La Motta C, Sartini S, Heine A, Klebe G: Evidence for a novel binding site conformer of aldose reductase in ligand-bound state. J Mol Biol. 2007 May 25;369(1):186-97. Epub 2007 Mar 15. [PubMed Link Image]
  29. Steuber H, Heine A, Klebe G: Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution. J Mol Biol. 2007 May 4;368(3):618-38. Epub 2006 Dec 15. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5366
Enzyme 7 Name Thioredoxin reductase 1, cytoplasmic
Enzyme 7 Synonyms
  1. TR
  2. Gene associated with retinoic and interferon-induced mortality 12 protein
  3. GRIM-12
  4. Gene associated with retinoic and IFN-induced mortality 12 protein
  5. KM-102-derived reductase-like factor
  6. Thioredoxin reductase TR1
Enzyme 7 Gene Name TXNRD1
Enzyme 7 Protein Sequence >Thioredoxin reductase 1, cytoplasmic 
MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQ
AYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDL
PVVFVKQRKIGGHGPTLKAYQEGRLQKLLKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKE
AAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKV
EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEK
IYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLA
GIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVV
AQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIY
AIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKA
VEKFGEENIEVYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQ
GFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCUG
Enzyme 7 Number of Residues 649
Enzyme 7 Molecular Weight 70905.6
Enzyme 7 Theoretical pI 7.42
Enzyme 7 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • antioxidant activity
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron carrier activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
  • protein disulfide oxidoreductase activity
  • purine nucleoside binding
  • thioredoxin-disulfide reductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 7 General Function Involved in oxidoreductase activity
Enzyme 7 Specific Function Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid
Enzyme 7 Pathways
Enzyme 7 Reactions
  • thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ [RN:R02016]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 148277071 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q16881 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name TRXR1_HUMAN Link Image
Enzyme 7 PDB ID 1H6V Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1950 bp 
ATGGGCTGCGCCGAGGGCAAGGCAGTGGCGGCGGCCGCCCCAACGGAGCTGCAGACGAAA
GGCAAGAACGGCGATGGCCGCCGTAGGTCAGCTAAAGATCATCACCCTGGTAAAACTTTG
CCAGAGAACCCAGCAGGATTCACCAGCACGGCCACTGCAGACTCCAGAGCCCTGCTTCAG
GCCTATATAGATGGTCACTCTGTGGTCATCTTCAGTAGGTCCACATGCACACGCTGTACT
GAGGTAAAGAAGTTATTTAAATCTCTGTGTGTTCCTTATTTTGTGCTTGAACTTGATCAA
ACAGAGGACGGTCGGGCCCTGGAAGGAACGCTCTCGGAATTGGCCGCGGAAACCGATCTG
CCCGTTGTGTTTGTGAAACAGAGAAAGATAGGCGGCCATGGTCCAACCTTGAAGGCTTAT
CAGGAGGGCAGACTTCAAAAGCTACTAAAAATGAACGGCCCTGAAGATCTTCCCAAGTCC
TATGACTATGACCTTATCATCATTGGAGGTGGCTCAGGAGGTCTGGCAGCTGCTAAGGAG
GCAGCCCAATATGGCAAGAAGGTGATGGTCCTGGACTTTGTCACTCCCACCCCTCTTGGA
ACTAGATGGGGTCTCGGAGGAACATGTGTGAATGTGGGTTGCATACCTAAAAAACTGATG
CATCAAGCAGCTTTGTTAGGACAAGCCCTGCAAGACTCTCGAAATTATGGATGGAAAGTC
GAGGAGACAGTTAAGCATGATTGGGACAGAATGATAGAAGCTGTACAGAATCACATTGGC
TCTTTGAATTGGGGCTACCGAGTAGCTCTGCGGGAGAAAAAAGTCGTCTATGAGAATGCT
TATGGGCAATTTATTGGTCCTCACAGGATTAAGGCAACAAATAATAAAGGCAAAGAAAAA
ATTTATTCAGCAGAGAGATTTCTCATTGCCACTGGTGAAAGACCACGTTACTTGGGCATC
CCTGGTGACAAAGAATACTGCATCAGCAGTGATGATCTTTTCTCCTTGCCTTACTGCCCG
GGTAAGACCCTGGTTGTTGGAGCATCCTATGTCGCTTTGGAGTGCGCTGGATTTCTTGCT
GGTATTGGTTTAGACGTCACTGTTATGGTTAGGTCCATTCTTCTTAGAGGATTTGACCAG
GACATGGCCAACAAAATTGGTGAACACATGGAAGAACATGGCATCAAGTTTATAAGACAG
TTCGTACCAATTAAAGTTGAACAAATTGAAGCAGGGACACCAGGCCGACTCAGAGTAGTA
GCTCAGTCCACCAATAGTGAGGAAATCATTGAAGGAGAATATAATACGGTGATGCTGGCA
ATAGGAAGAGATGCTTGCACAAGAAAAATTGGCTTAGAAACCGTAGGGGTGAAGATAAAT
GAAAAGACTGGAAAAATACCTGTCACAGATGAAGAACAGACCAATGTGCCTTACATCTAT
GCCATTGGCGATATATTGGAGGATAAGGTGGAGCTCACCCCAGTTGCAATCCAGGCAGGA
AGATTGCTGGCTCAGAGGCTCTATGCAGGTTCCACTGTCAAGTGTGACTATGAAAATGTT
CCAACCACTGTATTTACTCCTTTGGAATATGGTGCTTGTGGCCTTTCTGAGGAGAAAGCT
GTGGAGAAGTTTGGGGAAGAAAATATTGAGGTTTACCATAGTTACTTTTGGCCATTGGAA
TGGACGATTCCGTCAAGAGATAACAACAAATGTTATGCAAAAATAATCTGTAATACTAAA
GACAATGAACGTGTTGTGGGCTTTCACGTACTGGGTCCAAATGCTGGAGAAGTTACACAA
GGCTTTGCAGCTGCGCTCAAATGTGGACTGACCAAAAAGCAGCTGGACAGCACAATTGGA
ATCCACCCTGTCTGTGCAGAGGTATTCACAACATTGTCTGTGACCAAGCGCTCTGGGGCA
AGCATCCTCCAGGCTGGCTGCTGAGGTTAA
Enzyme 7 GenBank Gene ID NM_001093771.1 Link Image
Enzyme 7 GeneCard ID TXNRD1 Link Image
Enzyme 7 GenAtlas ID TXNRD1 Link Image
Enzyme 7 HGNC ID HGNC:12437 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 12q23-q24.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Gasdaska PY, Gasdaska JR, Cochran S, Powis G: Cloning and sequencing of a human thioredoxin reductase. FEBS Lett. 1995 Oct 2;373(1):5-9. [PubMed Link Image]
  2. Koishi R, Kawashima I, Yoshimura C, Sugawara M, Serizawa N: Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102. J Biol Chem. 1997 Jan 24;272(4):2570-7. [PubMed Link Image]
  3. Hofmann ER, Boyanapalli M, Lindner DJ, Weihua X, Hassel BA, Jagus R, Gutierrez PL, Kalvakolanu DV: Thioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid. Mol Cell Biol. 1998 Nov;18(11):6493-504. [PubMed Link Image]
  4. Rundlof AK, Janard M, Miranda-Vizuete A, Arner ES: Evidence for intriguingly complex transcription of human thioredoxin reductase 1. Free Radic Biol Med. 2004 Mar 1;36(5):641-56. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gladyshev VN, Jeang KT, Stadtman TC: Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):6146-51. [PubMed Link Image]
  7. Tamura T, Stadtman TC: A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1006-11. [PubMed Link Image]
  8. Su D, Gladyshev VN: Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1. Biochemistry. 2004 Sep 28;43(38):12177-88. [PubMed Link Image]
  9. Damdimopoulos AE, Miranda-Vizuete A, Treuter E, Gustafsson JA, Spyrou G: An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling. J Biol Chem. 2004 Sep 10;279(37):38721-9. Epub 2004 Jun 14. [PubMed Link Image]
  10. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  11. Wong JJ, Pung YF, Sze NS, Chin KC: HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets. Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10735-40. Epub 2006 Jun 30. [PubMed Link Image]
  12. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  13. Dammeyer P, Damdimopoulos AE, Nordman T, Jimenez A, Miranda-Vizuete A, Arner ES: Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1. J Biol Chem. 2008 Feb 1;283(5):2814-21. Epub 2007 Nov 27. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  15. Fritz-Wolf K, Urig S, Becker K: The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis. J Mol Biol. 2007 Jun 29;370(1):116-27. Epub 2007 Apr 24. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5367
Enzyme 8 Name Lathosterol oxidase
Enzyme 8 Synonyms
  1. C-5 sterol desaturase
  2. Delta(7)-sterol 5-desaturase
  3. Lathosterol 5-desaturase
  4. Sterol-C5-desaturase
Enzyme 8 Gene Name SC5DL
Enzyme 8 Protein Sequence >Lathosterol oxidase 
MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE
Enzyme 8 Number of Residues 299
Enzyme 8 Molecular Weight 35300.6
Enzyme 8 Theoretical pI 8.24
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid biosynthetic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • organelle
Enzyme 8 General Function Involved in iron ion binding
Enzyme 8 Specific Function Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • 5alpha-cholest-7-en-3beta-ol + NAD(P)H + H+ + O2 = cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O [RN:R03310 R07215]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 32-52 79-99 117-137 186-206
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3721882 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O75845 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name SC5D_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >900 bp 
ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTCCCCCAAATCTTACAG
CCATTTATTAATGGCTCAGCTCATCATACAGACCACCATATGTTCTTTGACTATAATTAT
GGACAATATTTCACTTTGTGGGATAGGATTGGCGGCTCATTCAAAAATCCTTCATCCTTT
GAGGGGAAGGGACCGCTCAGTTATGTGAAGGAGATGACAGAGGGAAAGCGCAGCAGCCCT
TCAGGAAATGGCTGTAAGAATGAAAAATTATTCAATGGAGAGTTTACAAAGACTGAATAG
Enzyme 8 GenBank Gene ID AB016247 Link Image
Enzyme 8 GeneCard ID SC5DL Link Image
Enzyme 8 GenAtlas ID SC5DL Link Image
Enzyme 8 HGNC ID HGNC:10547 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 11q23.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed Link Image]
  2. Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed Link Image]
  3. Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed Link Image]
  6. Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5375
Enzyme 9 Name Dimethylaniline monooxygenase [N-oxide-forming] 5
Enzyme 9 Synonyms
  1. Dimethylaniline oxidase 5
  2. Hepatic flavin-containing monooxygenase 5
  3. FMO 5
Enzyme 9 Gene Name FMO5
Enzyme 9 Protein Sequence >Dimethylaniline monooxygenase [N-oxide-forming] 5 
MTKKRIAVIGGGVSGLSSIKCCVEEGLEPVCFERTDDIGGLWRFQENPEEGRASIYKSVI
INTSKEMMCFSDYPIPDHYPNFMHNAQVLEYFRMYAKEFDLLKYIRFKTTVCSVKKQPDF
ATSGQWEVVTESEGKKEMNVFDGVMVCTGHHTNAHLPLESFPGIEKFKGQYFHSRDYKNP
EGFTGKRVIIIGIGNSGGDLAVEISQTAKQVFLSTRRGAWILNRVGDYGYPADVLFSSRL
THFIWKICGQSLANKYLEKKINQRFDHEMFGLKPKHRALSQHPTLNDDLPNRIISGLVKV
KGNVKEFTETAAIFEDGSREDDIDAVIFATGYSFDFPFLEDSVKVVKNKISLYKKVFPPN
LERPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKTLPSQSEMMAEISKAQEEIDKRY
VESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLLLGPCTPIHYRVQGPGK
WDGARKAILTTDDRIRKPLMTRVVERSSSMTSTMTIGKFMLALAFFAIIIAYF
Enzyme 9 Number of Residues 533
Enzyme 9 Molecular Weight 60220.0
Enzyme 9 Theoretical pI 8.36
Enzyme 9 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • flavin-containing monooxygenase activity
  • monooxygenase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 9 General Function Involved in flavin-containing monooxygenase activity
Enzyme 9 Specific Function In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 189054435 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P49326 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name FMO5_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1602 bp 
ATGACTAAGAAAAGAATTGCTGTGATTGGGGGAGGAGTGAGCGGGCTCTCTTCCATCAAG
TGCTGCGTAGAAGAAGGCTTGGAACCTGTCTGCTTTGAAAGGACTGATGACATCGGAGGG
CTCTGGAGGTTCCAGGAAAATCCTGAAGAAGGAAGGGCCAGTATTTACAAATCAGTGATC
ATCAATACTTCTAAAGAGATGATGTGCTTCAGTGACTATCCAATCCCAGATCATTATCCC
AACTTCATGCATAATGCCCAGGTCCTGGAGTATTTCAGGATGTATGCCAAAGAATTTGAC
CTTCTAAAGTATATTCGATTTAAGACCACTGTGTGCAGTGTGAAGAAGCAGCCTGATTTT
GCCACTTCAGGCCAATGGGAAGTGGTCACTGAATCTGAAGGGAAAAAGGAGATGAATGTC
TTTGATGGAGTCATGGTTTGCACTGGCCATCACACCAATGCTCATCTACCTCTGGAAAGC
TTCCCTGGAATTGAGAAGTTCAAAGGGCAGTACTTCCACAGTCGAGACTATAAGAACCCA
GAGGGATTCACTGGAAAGAGAGTCATTATAATTGGCATTGGGAATTCTGGAGGGGATCTG
GCTGTAGAGATTAGCCAAACAGCCAAGCAGGTTTTCCTCAGCACCAGGAGAGGGGCTTGG
ATCCTGAATCGTGTAGGGGACTACGGATATCCTGCTGATGTGTTGTTCTCTTCTCGACTT
ACACATTTTATATGGAAGATCTGTGGCCAATCATTAGCAAACAAATATTTGGAAAAAAAG
ATAAACCAAAGGTTTGACCATGAAATGTTTGGCCTGAAGCCTAAACACAGAGCTCTGAGT
CAGCATCCAACCTTAAATGATGACCTGCCAAATCGTATCATTTCTGGCTTGGTGAAAGTG
AAAGGAAATGTGAAGGAATTCACGGAGACAGCTGCCATATTTGAGGATGGCTCCAGGGAG
GATGACATTGATGCTGTTATCTTTGCCACAGGCTATAGCTTTGACTTTCCATTTCTGGAA
GATTCCGTCAAAGTGGTCAAAAACAAGATATCCCTGTATAAAAAGGTCTTCCCTCCTAAC
CTGGAAAGGCCAACTCTTGCAATCATAGGCTTGATTCAGCCCTTAGGAGCCATTATGCCC
ATTTCAGAGCTCCAAGGACGCTGGGCCACTCAGGTATTTAAAGGTCTAAAGACATTGCCC
TCACAGAGTGAAATGATGGCAGAAATATCTAAAGCTCAAGAGGAAATTGACAAAAGGTAT
GTGGAGAGCCAACGCCATACCATTCAGGGAGACTACATAGATACCATGGAAGAGCTTGCT
GATTTGGTGGGGGTCAGGCCCAATCTGCTGTCTCTGGCCTTCACTGACCCCAAGCTGGCA
TTACACTTATTACTGGGACCCTGCACTCCAATCCACTATCGTGTACAGGGCCCTGGAAAG
TGGGATGGGGCTCGAAAAGCTATCCTCACCACAGATGATCGCATCAGGAAGCCTCTGATG
ACAAGAGTAGTTGAAAGGAGTAGTTCTATGACTTCAACAATGACAATAGGCAAGTTTATG
CTAGCTCTTGCCTTCTTTGCTATAATTATAGCTTACTTCTAG
Enzyme 9 GenBank Gene ID AK314647 Link Image
Enzyme 9 GeneCard ID FMO5 Link Image
Enzyme 9 GenAtlas ID FMO5 Link Image
Enzyme 9 HGNC ID HGNC:3773 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1q21.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Overby LH, Buckpitt AR, Lawton MP, Atta-Asafo-Adjei E, Schulze J, Philpot RM: Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Arch Biochem Biophys. 1995 Feb 20;317(1):275-84. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5383
Enzyme 10 Name Heme oxygenase 2
Enzyme 10 Synonyms
  1. HO-2
Enzyme 10 Gene Name HMOX2
Enzyme 10 Protein Sequence >Heme oxygenase 2 
MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKG
NIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGEN
WEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQA
GSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFIL
AAGVALAAGLLAWYYM
Enzyme 10 Number of Residues 316
Enzyme 10 Molecular Weight 36032.6
Enzyme 10 Theoretical pI 5.09
Enzyme 10 GO Classification
Function
  • catalytic activity
  • heme oxygenase (decyclizing) activity
  • heme oxygenase (decyclizing) activity
  • heme oxygenase (decyclizing) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Process
  • heme metabolic process
  • heme oxidation
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin metabolic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 10 General Function Involved in heme oxygenase (decyclizing) activity
Enzyme 10 Specific Function Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter
Enzyme 10 Pathways
Enzyme 10 Reactions
  • heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O [RN:R00311]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 187761307 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P30519 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name HMOX2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >951 bp 
ATGTCAGCGGAAGTGGAAACCTCAGAGGGGGTAGACGAGTCAGAAAAAAAGAACTCTGGG
GCCCTAGAAAAGGAGAACCAAATGAGAATGGCTGACCTCTCGGAGCTCCTGAAGGAAGGG
ACCAAGGAAGCACACGACCGGGCAGAAAACACCCAGTTTGTCAAGGACTTCTTGAAAGGC
AACATTAAGAAGGAGCTGTTTAAGCTGGCCACCACGGCACTTTACTTCACATACTCAGCC
CTCGAGGAGGAAATGGAGCGCAACAAGGACCATCCAGCCTTTGCCCCTTTGTACTTCCCC
ATGGAGCTGCACCGGAAGGAGGCGCTGACCAAGGACATGGAGTATTTCTTTGGTGAAAAC
TGGGAGGAGCAGGTGCAGTGCCCCAAGGCTGCCCAGAAGTACGTGGAGCGGATCCACTAC
ATAGGGCAGAACGAGCCGGAGCTACTGGTGGCCCATGCATACACCCGCTACATGGGGGAT
CTCTCGGGGGGCCAGGTGCTGAAGAAGGTGGCCCAGCGAGCACTGAAACTCCCCAGCACA
GGGGAAGGGACCCAGTTCTACCTGTTTGAGAATGTGGACAATGCCCAGCAGTTCAAGCAG
CTCTACCGGGCCAGGATGAACGCCCTGGACCTGAACATGAAGACCAAAGAGAGGATCGTG
GAGGAGGCCAACAAGGCTTTTGAGTATAACATGCAGATATTCAATGAACTGGACCAGGCC
GGCTCCACACTGGCCAGAGAGACCTTGGAGGATGGGTTCCCTGTACACGATGGGAAAGGA
GACATGCGTAAATGCCCTTTCTACGCTGCTGAACAAGACAAAGGTGCCCTGGAGGGCAGC
AGCTGTCCCTTCCGAACAGCTATGGCTGTGCTGAGGAAGCCCAGCCTCCAGTTCATCCTG
GCCGCTGGTGTGGCCCTAGCTGCTGGACTCTTGGCCTGGTACTACATGTGA
Enzyme 10 GenBank Gene ID NM_001127204.1 Link Image
Enzyme 10 GeneCard ID HMOX2 Link Image
Enzyme 10 GenAtlas ID HMOX2 Link Image
Enzyme 10 HGNC ID HGNC:5014 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 16p13.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T: Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. J Biol Chem. 1995 Mar 17;270(11):6345-50. [PubMed Link Image]
  2. McCoubrey WK Jr, Ewing JF, Maines MD: Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys. 1992 May 15;295(1):13-20. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr: Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5387
Enzyme 11 Name Dimethylaniline monooxygenase [N-oxide-forming] 2
Enzyme 11 Synonyms
  1. Dimethylaniline oxidase 2
  2. FMO 1B1
  3. Pulmonary flavin-containing monooxygenase 2
  4. FMO 2
Enzyme 11 Gene Name FMO2
Enzyme 11 Protein Sequence >Dimethylaniline monooxygenase [N-oxide-forming] 2 
MAKKVAVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGVWRFKENVEDGRASIYQSVVT
NTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVLSVRKCPDFS
SSGQWKVVTQSNGKEQSAVFDAVMVCSGHHILPHIPLKSFPGMERFKGQYFHSRQYKHPD
GFEGKRILVIGMGNSGSDIAVELSKNAAQVFISTRHGTWVMSRISEDGYPWDSVFHTRFR
SMLRNVLPRTAVKWMIEQQMNRWFNHENYGLEPQNKYIMKEPVLNDDVPSRLLCGAIKVK
STVKELTETSAIFEDGTVEENIDVIIFATGYSFSFPFLEDSLVKVENNMVSLYKYIFPAH
LDKSTLACIGLIQPLGSIFPTAELQARWVTRVFKGLCSLPSERTMMMDIIKRNEKRIDLF
GESQSQTLQTNYVDYLDELALEIGAKPDFCSLLFKDPKLAVRLYFGPCNSYQYRLVGPGQ
WEGARNAIFTQKQRILKPLKTRALKDSSNFSVSFLLKILGLLAVVVAFFCQLQWS
Enzyme 11 Number of Residues 535
Enzyme 11 Molecular Weight 60906.8
Enzyme 11 Theoretical pI 8.40
Enzyme 11 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • flavin-containing monooxygenase activity
  • monooxygenase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 11 General Function Involved in flavin-containing monooxygenase activity
Enzyme 11 Specific Function Catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. Inactive toward certain tertiary amines, such as imipramine or chloropromazine. Can catalyze the S-oxidation of methimazole. The truncated form is catalytically inactive
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 4503757 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q99518 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name FMO2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID Not Available
Enzyme 11 GeneCard ID FMO2 Link Image
Enzyme 11 GenAtlas ID FMO2 Link Image
Enzyme 11 HGNC ID HGNC:3770 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1q24.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, Phillips IR: The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein. J Biol Chem. 1998 Nov 13;273(46):30599-607. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Blomster HA, Imanishi SY, Siimes J, Kastu J, Morrice NA, Eriksson JE, Sistonen L: In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification. J Biol Chem. 2010 Jun 18;285(25):19324-9. Epub 2010 Apr 13. [PubMed Link Image]
  5. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5388
Enzyme 12 Name Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Enzyme 12 Synonyms
  1. P5C dehydrogenase
  2. Aldehyde dehydrogenase family 4 member A1
Enzyme 12 Gene Name ALDH4A1
Enzyme 12 Protein Sequence >Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial 
MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGR
MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKP
IADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL
EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAML
ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ
NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSL
WPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK
CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTG
AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR
WTSPQVIKETHKPLGDWSYAYMQ
Enzyme 12 Number of Residues 563
Enzyme 12 Molecular Weight 61718.9
Enzyme 12 Theoretical pI 8.20
Enzyme 12 GO Classification
Function
  • 1-pyrroline-5-carboxylate dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline biosynthetic process
  • proline metabolic process
Component
  • cell part
  • cytoplasmic part
  • intracellular part
  • mitochondrial matrix
  • mitochondrial part
Enzyme 12 General Function Involved in oxidoreductase activity
Enzyme 12 Specific Function Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes
Enzyme 12 Pathways
Enzyme 12 Reactions
  • (S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H + H+ [RN:R00707 R00708]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 62896531 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P30038 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name AL4A1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1692 bp 
ATGCTGCTGCCGGCGCCCGCGCTCCGCCGCGCCCTGCTGTCCCGCCCCTGGACCGGGGCC
GGCCTGCGGTGGAAGCACACCTCCTCCCTGAAGGTGGCCAACGAGCCCGTCTTAGCCTTC
ACGCAGGGCAGCCCTGAGCGAGATGCCCTGCAAAAGGCCTTGAAGGACCTGAAGGGCCGG
ATGGAAGCCATCCCATGCGTGGTGGGGGATGAGGAGGTGTGGACGTCGGACGTGCAGTAC
CAAGTGTCGCCTTTTAACCATGGACATAAGGTGGCCAAGTTCTGTTATGCAGACAAGAGC
CTGCTCAACAAAGCCATTGAGGCTGCCCTGGCTGCCCGGAAAGAGTGGGACCTGAAGCCT
ATTGCAGACCGGGCCCAGATCTTCCTGAAGGCGGCAGACATGCTGAGTGGGCCGCGCAGG
GCTGAGATCCTCGCCAAGACCATGGTGGGACAGGGTAAGACCGTGATCCAAGCGGAGATT
GACGCTGCAGCGGAACTCATCGACTTCTTCCGGTTCAATGCCAAGTATGCGGTGGAGCTG
GAGGGGCAGCAGCCCATCAGCGTGCCCCCGAGCACCAACAGCACGGTGTACCGGGGTCTG
GAGGGCTTCGTGGCGGCCATCTCGCCCTTTAACTTCACTGCAATCGGCGGCAACCTGGCG
GGGGCACCGGCCCTGATAGGCAACGTGGTCCTATGGAAGCCCAGTGACACTGCCATGCTG
GCCAGCTATGCTGTCTACCGCATCCTTCGGGAGGCTGGCCTGCCCCCCAACATCATCCAG
TTTGTGCCAGCTGATGGGCCCCTATTTGGGGACACTGTCACCAGCTCAGAGCACCTCTGT
GGCATCAACTTCACAGGCAGTGTGCCCACCTTCAAACACCTGTGGAAGCAGGTGGCCCAG
AACCTGGACCGGTTCCACACCTTCCCACGCCTGGCTGGAGAGTGCGGCGGAAAGAACTTC
CACTTCGTGCACCGCTCGGCCGACGTGGAGAGCGTGGTGAGCGGGACCCTCCGCTCAGCC
TTCGAGTACGGTGGCCAGAAGTGTTCCGCCTGCTCGCGTCTCTACGTGCCGCACTCGCTG
TGGCCGCAGATCAAAGGGCGGCTGCTGGAGGAGCACAGTCGGATCAGAGTGGGCGACCCT
GCAGAGGATTTTGGGACCTTCTTCTCTGCAGTGATTGATGCCAAGTCCTTTGCCCGTATC
AAGAAGTGGCTGGAGCACGCACGCTCCTCACCCAGCCTCACCATCCTGGCCGGGGGCAAG
TGTGATGACTCCGTGGGCTACTTTGTGGAGCCCTGCATCGTGGAGAGCAAGGACCCTCAG
GAGCCCATCATGAAGGAGGAGATCTTCGGGCCTGTACTGTCTGTGTACGTCTACCCGGAT
GACAAGTACAAGGAGACGCTGCAGCTGGTTGACAGCACCACCAGCTATGGCCTCACGGGG
GCAGTGTTCTCCCAGGATAAGGACGTCGTGCAGGAGGCCACAAAGGTGCTGAGGAATGCT
GCCGGCAACTTCTACATCAACGACAAGTCCACTGGCTCGATAGTGGGCCAGCAGCCCTTT
GGGGGGGCCCGAGCCTCTGGAACCAATGACAAGCCAGGGGGCCCACACTACATCCTGCGC
TGGACGTCGCCGCAGGTCATCAAGGAGACACATAAGCCCCTGGGGGACTGGAGCTACGCG
TACATGCAGTGA
Enzyme 12 GenBank Gene ID AK222486 Link Image
Enzyme 12 GeneCard ID ALDH4A1 Link Image
Enzyme 12 GenAtlas ID ALDH4A1 Link Image
Enzyme 12 HGNC ID HGNC:406 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1p36
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Hu CA, Lin WW, Valle D: Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J Biol Chem. 1996 Apr 19;271(16):9795-800. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW: Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme. Comp Biochem Physiol B. 1992 Aug;102(4):791-93. [PubMed Link Image]
  6. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  7. Agarwal DP, Eckey R, Hempel J, Goedde HW: Human liver high Km aldehyde dehydrogenase (ALDH4): properties and structural relationship to the glutamic gamma-semialdehyde dehydrogenase. Adv Exp Med Biol. 1993;328:191-7. [PubMed Link Image]
  8. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  9. Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA: Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5390
Enzyme 13 Name Thioredoxin reductase 2, mitochondrial
Enzyme 13 Synonyms
  1. Selenoprotein Z
  2. SelZ
  3. TR-beta
  4. Thioredoxin reductase TR3
Enzyme 13 Gene Name TXNRD2
Enzyme 13 Protein Sequence >Thioredoxin reductase 2, mitochondrial 
MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQ
LGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQP
VPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLS
ADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI
GLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDST
TGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDV
VEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHG
QEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALG
IKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG
Enzyme 13 Number of Residues 524
Enzyme 13 Molecular Weight 56506.3
Enzyme 13 Theoretical pI 7.55
Enzyme 13 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • antioxidant activity
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
  • purine nucleoside binding
  • thioredoxin-disulfide reductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 13 General Function Involved in oxidoreductase activity
Enzyme 13 Specific Function Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox- regulated cell signaling
Enzyme 13 Pathways
Enzyme 13 Reactions
  • thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+ [RN:R02016]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID Q9NNW7 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name TRXR2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1575 bp 
ATGGCGGCAATGGCGGTGGCGCTGCGGGGATTAGGAGGGCGCTTCCGGTGGCGGACGCAG
GCCGTGGCGGGCGGGGTGCGGGGCGCGGCGCGGGGCGCAGCAGCAGGTCAGCGGGACTAT
GATCTCCTGGTGGTCGGCGGGGGATCTGGTGGCCTGGCTTGTGCCAAGGAGGCCGCCCAG
CTGGGAAGGAAGGTGGCCGTGGTGGACTACGTGGAACCTTCTCCCCAAGGCACCCGGTGG
GGCCTCGGCGGCACCTGCGTCAACGTGGGCTGCATCCCCAAGAAGCTGATGCACCAGGCG
GCACTGCTGGGAGGCCTGATCCAAGATGCCCCCAACTATGGCTGGGAGGTGGCCCAGCCC
GTGCCGCATGACTGGAGGAAGATGGCAGAAGCTGTTCAAAATCACGTGAAATCCTTGAAC
TGGGGCCACCGTGTCCAGCTTCAGGACAGAAAAGTCAAGTACTTTAACATCAAAGCCAGC
TTTGTTGACGAGCACACGGTTTGCGGCGTTGCCAAAGGTGGGAAAGAGATTCTGCTGTCA
GCCGATCACATCATCATTGCTACTGGAGGGCGGCCGAGATACCCCACGCACATCGAAGGT
GCCTTGGAATATGGAATCACAAGTGATGACATCTTCTGGCTGAAGGAATCCCCTGGAAAA
ACGTTGGTGGTCGGGGCCAGCTATGTGGCCCTGGAGTGTGCTGGCTTCCTCACCGGGATT
GGGCTGGACACCACCATCATGATGCGCAGCATCCCCCTCCGCGGCTTCGACCAGCAAATG
TCCTCCATGGTCATAGAGCACATGGCATCTCATGGCACCCGGTTCCTGAGGGGCTGTGCC
CCCTCGCGGGTCAGGAGGCTCCCTGATGGCCAGCTGCAGGTCACCTGGGAGGACAGCACC
ACCGGCAAGGAGGACACGGGCACCTTTGACACCGTCCTGTGGGCCATAGGTCGAGTCCCA
GACACCAGAAGTCTGAATTTGGAGAAGGCTGGGGTAGATACTAGCCCCGACACTCAGAAG
ATCCTGGTGGACTCCCGGGAAGCCACCTCTGTGCCCCACATCTACGCCATTGGTGACGTG
GTGGAGGGGCGGCCTGAGCTGACACCCATAGCGATCATGGCCGGGAGGCTCCTGGTGCAG
CGGCTCTTCGGCGGGTCCTCAGATCTGATGGACTACGACAATGTTCCCACGACCGTCTTC
ACCCCGCTGGAGTATGGCTGTGTGGGGCTGTCCGAGGAGGAGGCAGTGGCTCGCCACGGG
CAGGAGCATGTTGAGGTCTATCACGCCCATTATAAACCACTGGAGTTCACGGTGGCTGGA
CGAGATGCATCCCAGTGTTATGTAAAGATGGTGTGCCTGAGGGAGCCCCCACAGCTGGTG
CTGGGCCTGCATTTCCTTGGCCCCAACGCAGGCGAAGTTACTCAAGGATTTGCTCTGGGG
ATCAAGTGTGGGGCTTCCTATGCGCAGGTGATGCGGACCGTGGGTATCCATCCCACATGC
TCTGAGGAGGTAGTCAAGCTGCGCATCTCCAAGCGCTCAGGCCTGGACCCCACGGTGACA
GGCTGCTGAGGGTAA
Enzyme 13 GenBank Gene ID AF171054 Link Image
Enzyme 13 GeneCard ID TXNRD2 Link Image
Enzyme 13 GenAtlas ID TXNRD2 Link Image
Enzyme 13 HGNC ID HGNC:18155 Link Image
Enzyme 13 Chromosome Location 2
Enzyme 13 Locus 22q11.21
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Sun QA, Wu Y, Zappacosta F, Jeang KT, Lee BJ, Hatfield DL, Gladyshev VN: Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases. J Biol Chem. 1999 Aug 27;274(35):24522-30. [PubMed Link Image]
  2. Gasdaska PY, Berggren MM, Berry MJ, Powis G: Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett. 1999 Jan 8;442(1):105-11. [PubMed Link Image]
  3. Miranda-Vizuete A, Damdimopoulos AE, Pedrajas JR, Gustafsson JA, Spyrou G: Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization. Eur J Biochem. 1999 Apr;261(2):405-12. [PubMed Link Image]
  4. Lescure A, Gautheret D, Carbon P, Krol A: Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. [PubMed Link Image]
  5. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Sun QA, Zappacosta F, Factor VM, Wirth PJ, Hatfield DL, Gladyshev VN: Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicing. J Biol Chem. 2001 Feb 2;276(5):3106-14. Epub 2000 Nov 1. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5397
Enzyme 14 Name Dimethylaniline monooxygenase [N-oxide-forming] 4
Enzyme 14 Synonyms
  1. Dimethylaniline oxidase 4
  2. Hepatic flavin-containing monooxygenase 4
  3. FMO 4
Enzyme 14 Gene Name FMO4
Enzyme 14 Protein Sequence >Dimethylaniline monooxygenase [N-oxide-forming] 4 
MAKKVAVIGAGVSGLSSIKCCVDEDLEPTCFERSDDIGGLWKFTESSKDGMTRVYKSLVT
NVCKEMSCYSDFPFHEDYPNFMNHEKFWDYLQEFAEHFDLLKYIQFKTTVCSITKRPDFS
ETGQWDVVTETEGKQNRAVFDAVMVCTGHFLNPHLPLEAFPGIHKFKGQILHSQEYKIPE
GFQGKRVLVIGLGNTGGDIAVELSRTAAQVLLSTRTGTWVLGRSSDWGYPYNMMVTRRCC
SFIAQVLPSRFLNWIQERKLNKRFNHEDYGLSITKGKKAKFIVNDELPNCILCGAITMKT
SVIEFTETSAVFEDGTVEENIDVVIFTTGYTFSFPFFEEPLKSLCTKKIFLYKQVFPLNL
ERATLAIIGLIGLKGSILSGTELQARWVTRVFKGLCKIPPSQKLMMEATEKEQLIKRGVF
KDTSKDKFDYIAYMDDIAACIGTKPSIPLLFLKDPRLAWEVFFGPCTPYQYRLMGPGKWD
GARNAILTQWDRTLKPLKTRIVPDSSKPASMSHYLKAWGAPVLLASLLLICKSSLFLKLV
RDKLQDRMSPYLVSLWRG
Enzyme 14 Number of Residues 558
Enzyme 14 Molecular Weight 63342.1
Enzyme 14 Theoretical pI 8.59
Enzyme 14 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • flavin-containing monooxygenase activity
  • monooxygenase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 14 General Function Involved in flavin-containing monooxygenase activity
Enzyme 14 Specific Function This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 517-531
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 4753758 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P31512 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name FMO4_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1677 bp 
ATGGCCAAGAAAGTTGCAGTGATTGGAGCTGGTGTGAGTGGCCTCTCCTCCATCAAATGC
TGTGTGGATGAGGACCTGGAGCCCACCTGCTTTGAGAGAAGTGATGACATTGGGGGATTA
TGGAAGTTTACTGAATCTTCCAAAGATGGGATGACCAGGGTCTATAAGTCATTAGTGACA
AATGTCTGTAAGGAAATGTCATGTTACAGTGACTTCCCTTTCCACGAAGATTATCCTAAT
TTCATGAACCATGAAAAATTTTGGGACTATCTCCAAGAATTTGCTGAGCACTTTGACCTC
CTGAAATACATTCAGTTTAAGACCACTGTGTGCAGCATAACGAAGCGTCCAGACTTCTCC
GAAACTGGTCAGTGGGATGTTGTCACAGAGACAGAGGGCAAGCAAAATAGAGCTGTCTTT
GATGCTGTTATGGTTTGCACTGGACATTTCCTGAATCCCCATTTACCTTTGGAAGCCTTT
CCTGGAATTCATAAGTTTAAAGGTCAGATCCTGCATAGTCAAGAGTACAAGATCCCAGAA
GGCTTTCAGGGCAAACGCGTCTTGGTGATTGGTCTTGGGAACACTGGAGGAGACATTGCT
GTGGAACTCAGTCGAACGGCAGCTCAGGTACTTCTCAGTACTAGAACTGGTACCTGGGTT
CTTGGGCGCTCTTCAGATTGGGGCTATCCTTATAATATGATGGTTACAAGAAGATGCTGT
AGTTTTATTGCACAAGTTCTGCCTTCACGTTTTCTAAACTGGATTCAAGAAAGGAAGTTG
AATAAGAGATTTAATCATGAGGATTATGGATTAAGTATTACCAAAGGGAAAAAAGCAAAA
TTCATTGTGAATGATGAGCTGCCAAACTGTATCCTCTGTGGGGCAATCACTATGAAAACC
AGCGTGATTGAATTTACAGAAACCTCTGCTGTCTTTGAAGATGGGACAGTGGAAGAAAAC
ATTGATGTTGTGATCTTCACTACAGGATATACATTTTCTTTTCCATTTTTTGAAGAACCT
CTTAAAAGCCTCTGTACAAAGAAGATATTTCTATACAAGCAAGTCTTTCCCTTAAACCTA
GAGAGAGCGACATTAGCCATCATCGGCCTTATCGGCCTTAAAGGATCCATCTTATCAGGC
ACAGAGCTCCAAGCACGATGGGTCACAAGAGTATTCAAAGGACTCTGTAAGATACCTCCA
TCCCAAAAATTGATGATGGAGGCTACTGAAAAGGAACAGCTCATTAAAAGGGGAGTGTTT
AAAGACACCAGCAAAGACAAATTTGACTACATTGCCTACATGGATGATATCGCTGCCTGC
ATAGGCACAAAGCCCAGCATCCCACTTCTGTTCCTCAAGGATCCCAGACTAGCTTGGGAA
GTTTTCTTTGGACCATGTACTCCTTATCAGTACCGCCTCATGGGCCCTGGAAAATGGGAT
GGAGCCAGAAATGCCATCCTGACCCAGTGGGACAGAACATTGAAACCTTTAAAAACTCGA
ATTGTCCCTGATTCCTCCAAGCCTGCCTCCATGTCACATTATTTAAAAGCCTGGGGGGCA
CCTGTCCTACTTGCCTCTCTTCTACTTATCTGTAAATCTTCACTTTTCTTGAAATTGGTG
AGAGATAAACTACAGGACAGAATGTCCCCTTACCTAGTAAGTCTTTGGCGAGGATGA
Enzyme 14 GenBank Gene ID AL031274 Link Image
Enzyme 14 GeneCard ID FMO4 Link Image
Enzyme 14 GenAtlas ID FMO4 Link Image
Enzyme 14 HGNC ID HGNC:3772 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1q24.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR: Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family. Biochem J. 1992 Oct 1;287 ( Pt 1):261-7. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5403
Enzyme 15 Name Dimethylaniline monooxygenase [N-oxide-forming] 3
Enzyme 15 Synonyms
  1. Dimethylaniline oxidase 3
  2. FMO II
  3. FMO form 2
  4. Hepatic flavin-containing monooxygenase 3
  5. FMO 3
Enzyme 15 Gene Name FMO3
Enzyme 15 Protein Sequence >Dimethylaniline monooxygenase [N-oxide-forming] 3 
MGKKVAIIGAGVSGLASIRSCLEEGLEPTCFEKSNDIGGLWKFSDHAEEGRASIYKSVFS
NSSKEMMCFPDFPFPDDFPNFMHNSKIQEYIIAFAKEKNLLKYIQFKTFVSSVNKHPDFA
TTGQWDVTTERDGKKESAVFDAVMVCSGHHVYPNLPKESFPGLNHFKGKCFHSRDYKEPG
VFNGKRVLVVGLGNSGCDIATELSRTAEQVMISSRSGSWVMSRVWDNGYPWDMLLVTRFG
TFLKNNLPTAISDWLYVKQMNARFKHENYGLMPLNGVLRKEPVFNDELPASILCGIVSVK
PNVKEFTETSAIFEDGTIFEGIDCVIFATGYSFAYPFLDESIIKSRNNEIILFKGVFPPL
LEKSTIAVIGFVQSLGAAIPTVDLQSRWAAQVIKGTCTLPSMEDMMNDINEKMEKKRKWF
GKSETIQTDYIVYMDELSSFIGAKPNIPWLFLTDPKLAMEVYFGPCSPYQFRLVGPGQWP
GARNAILTQWDRSLKPMQTRVVGRLQKPCFFFHWLKLFAIPILLIAVFLVLT
Enzyme 15 Number of Residues 532
Enzyme 15 Molecular Weight 60033.0
Enzyme 15 Theoretical pI 7.87
Enzyme 15 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • flavin-containing monooxygenase activity
  • monooxygenase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 15 General Function Involved in flavin-containing monooxygenase activity
Enzyme 15 Specific Function Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Plays an important role in the metabolism of trimethylamine (TMA), via the production of TMA N-oxide (TMAO). Is also able to perform S-oxidation when acting on sulfide compounds
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 189053761 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P31513 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name FMO3_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1599 bp 
ATGGGGAAGAAAGTGGCCATCATTGGAGCTGGTGTGAGTGGCTTGGCCTCCATCAGGAGC
TGTCTGGAAGAGGGGCTGGAGCCCACCTGCTTTGAGAAGAGCAATGACATTGGGGGCCTG
TGGAAATTTTCAGACCATGCAGAGGAGGGCAGGGCTAGCATTTACAAATCAGTCTTTTCC
AACTCTTCCAAAGAGATGATGTGTTTCCCAGACTTCCCATTTCCCGATGACTTCCCCAAC
TTTATGCACAACAGCAAGATCCAGGAATATATCATTGCATTTGCCAAAGAAAAGAACCTC
CTGAAGTACATACAATTTAAGACATTTGTATCCAGTGTAAATAAACATCCTGATTTTGCA
ACTACTGGCCAGTGGGATGTTACCACTGAAAGGGATGGTAAAAAAGAATCGGCTGTCTTT
GATGCTGTAATGGTTTGTTCCGGACATCATGTGTATCCCAACCTACCAAAAGAGTCCTTT
CCAGGACTAAACCACTTTAAAGGCAAATGCTTCCACAGCAGGGACTATAAAGAACCAGGT
GTATTCAATGGAAAGCGTGTCCTGGTGGTTGGCCTGGGGAATTCGGGCTGTGATATTGCC
ACAGAACTCAGCCGCACAGCAGAACAGGTCATGATCAGTTCCAGAAGTGGCTCCTGGGTG
ATGAGCCGGGTCTGGGACAATGGTTATCCTTGGGACATGCTGCTCGTCACTCGATTTGGA
ACCTTCCTCAAGAACAATTTACCGACAGCCATCTCTGACTGGTTGTACGTGAAGCAGATG
AATGCAAGATTCAAGCATGAAAACTATGGCTTGATGCCTTTAAATGGAGTCCTGAGGAAA
GAGCCTGTATTTAACGATGAGCTCCCAGCAAGCATTCTGTGTGGCATTGTGTCCGTAAAG
CCTAACGTGAAGGAATTCACAGAGACCTCGGCCATTTTTGAGGATGGGACCATATTTGAG
GGCATTGACTGTGTAATCTTTGCAACAGGGTATAGTTTTGCCTACCCCTTCCTTGATGAG
TCTATCATCAAAAGCAGAAACAATGAGATCATTTTATTTAAAGGAGTATTTCCTCCTCTA
CTTGAGAAGTCAACCATAGCAGTGATTGGCTTTGTCCAGTCCCTTGGGGCTGCCATTCCC
ACAGTTGACCTCCAGTCCCGCTGGGCAGCACAAGTAATAAAGGGAACTTGTACTTTGCCT
TCTATGGAAGACATGATGAATGATATTAATGAGAAAATGGAGAAAAAGCGCAAATGGTTT
GGCAAAAGCGAGACCATACAGACAGATTACATTGTTTATATGGATGAACTCTCCTCCTTC
ATTGGGGCAAAGCCCAACATCCCATGGCTGTTTCTCACAGATCCCAAATTGGCCATGGAA
GTTTATTTTGGCCCTTGTAGTCCCTACCAGTTTAGGCTGGTGGGCCCAGGGCAGTGGCCA
GGAGCCAGAAATGCCATACTGACCCAGTGGGACCGGTCGTTGAAACCCATGCAGACACGA
GTGGTCGGGAGACTTCAGAAGCCTTGCTTCTTTTTCCATTGGCTGAAGCTCTTTGCAATT
CCTATTCTGTTAATCGCTGTTTTCCTTGTGTTGACCTAA
Enzyme 15 GenBank Gene ID AK313197 Link Image
Enzyme 15 GeneCard ID FMO3 Link Image
Enzyme 15 GenAtlas ID FMO3 Link Image
Enzyme 15 HGNC ID HGNC:3771 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1q24.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Lomri N, Gu Q, Cashman JR: Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1685-9. [PubMed Link Image]
  2. Dolphin CT, Cullingford TE, Shephard EA, Smith RL, Phillips IR: Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04. Eur J Biochem. 1996 Feb 1;235(3):683-9. [PubMed Link Image]
  3. Dolphin CT, Riley JH, Smith RL, Shephard EA, Phillips IR: Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA. Genomics. 1997 Dec 1;46(2):260-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Treacy EP, Akerman BR, Chow LM, Youil R, Bibeau C, Lin J, Bruce AG, Knight M, Danks DM, Cashman JR, Forrest SM: Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication. Hum Mol Genet. 1998 May;7(5):839-45. [PubMed Link Image]
  8. Akerman BR, Forrest S, Chow L, Youil R, Knight M, Treacy EP: Two novel mutations of the FMO3 gene in a proband with trimethylaminuria. Hum Mutat. 1999;13(5):376-9. [PubMed Link Image]
  9. Akerman BR, Lemass H, Chow LM, Lambert DM, Greenberg C, Bibeau C, Mamer OA, Treacy EP: Trimethylaminuria is caused by mutations of the FMO3 gene in a North American cohort. Mol Genet Metab. 1999 Sep;68(1):24-31. [PubMed Link Image]
  10. Dolphin CT, Janmohamed A, Smith RL, Shephard EA, Phillips IR: Compound heterozygosity for missense mutations in the flavin-containing monooxygenase 3 (FM03) gene in patients with fish-odour syndrome. Pharmacogenetics. 2000 Dec;10(9):799-807. [PubMed Link Image]
  11. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
  12. Fujieda M, Yamazaki H, Togashi M, Saito T, Kamataki T: Two novel single nucleotide polymorphisms (SNPs) of the FMO3 gene in Japanese. Drug Metab Pharmacokinet. 2003;18(5):333-5. [PubMed Link Image]
  13. Zhang J, Tran Q, Lattard V, Cashman JR: Deleterious mutations in the flavin-containing monooxygenase 3 (FMO3) gene causing trimethylaminuria. Pharmacogenetics. 2003 Aug;13(8):495-500. [PubMed Link Image]
  14. Yeung CK, Adman ET, Rettie AE: Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria. Arch Biochem Biophys. 2007 Aug 15;464(2):251-9. Epub 2007 May 2. [PubMed Link Image]
  15. Koukouritaki SB, Poch MT, Henderson MC, Siddens LK, Krueger SK, VanDyke JE, Williams DE, Pajewski NM, Wang T, Hines RN: Identification and functional analysis of common human flavin-containing monooxygenase 3 genetic variants. J Pharmacol Exp Ther. 2007 Jan;320(1):266-73. Epub 2006 Oct 18. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5415
Enzyme 16 Name NADPH--cytochrome P450 reductase
Enzyme 16 Synonyms
  1. CPR
  2. P450R
Enzyme 16 Gene Name POR
Enzyme 16 Protein Sequence >NADPH--cytochrome P450 reductase 
MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTL
TSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLA
DLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEH
FNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEES
SIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHL
MHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHP
FPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWV
VEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYET
KAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPF
IGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQS
HKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVD
YIKKLMTKGRYSLDVWS
Enzyme 16 Number of Residues 677
Enzyme 16 Molecular Weight 76689.1
Enzyme 16 Theoretical pI 5.28
Enzyme 16 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 16 General Function Involved in oxidoreductase activity
Enzyme 16 Specific Function This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 11414998 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P16435 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name NCPR_HUMAN Link Image
Enzyme 16 PDB ID 1AMO Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2034 bp 
ATGGGAGACTCCCACGTGGACACCAGCTCCACCGTGTCCGAGGCGGTGGCCGAAGAAGTA
TCTCTTTTCAGCATGACGGACATGATTCTGTTTTCGCTCATCGTGGGTCTCCTAACCTAC
TGGTTCCTCTTCAGAAAGAAAAAAGAAGAAGTCCCCGAGTTCACCAAAATTCAGACATTG
ACCTCCTCTGTCAGAGAGAGCAGCTTTGTGGAAAAGATGAAGAAAACGGGGAGGAACATC
ATCGTGTTCTACGGCTCCCAGACGGGGACTGCAGAGGAGTTTGCCAACCGCCTGTCCAAG
GACGCCCACCGCTACGGGATGCGAGGCATGTCAGCGGACCCTGAGGAGTATGACCTGGCC
GACCTGAGCAGCCTGCCAGAGATCGACAACGCCCTGGTGGTTTTCTGCATGGCCACCTAC
GGTGAGGGAGACCCCACCGACAATGCCCAGGACTTCTACGACTGGCTGCAGGAGACAGAC
GTGGATCTCTCTGGGGTCAAGTTCGCGGTGTTTGGTCTTGGGAACAAGACCTACGAGCAC
TTCAATGCCATGGGCAAGTACGTGGACAAGCGGCTGGAGCAGCTCGGCGCCCAGCGCATC
TTTGAGCTGGGGTTGGGCGACGACGATGGGAACTTGGAGGAGGACTTCATCACCTGGCGA
GAGCAGTTCTGGCCGGCCGTGTGTGAACACTTTGGGGTGGAAGCCACTGGCGAGGAGTCC
AGCATTCGCCAGTACGAGCTTGTGGTCCACACCGACATAGATGCGGCCAAGGTGTACATG
GGGGAGATGGGCCGGCTGAAGAGCTACGAGAACCAGAAGCCCCCCTTTGATGCCAAGAAT
CCGTTCCTGGCTGCAGTCACCACCAACCGGAAGCTGAACCAGGGAACCGAGCGCCACCTC
ATGCACCTGGAATTGGACATCTCGGACTCCAAAATCAGGTATGAATCTGGGGACCACGTG
GCTGTGTACCCAGCCAACGACTCTGCTCTCGTCAACCAGCTGGGCAAAATCCTGGGTGCC
GACCTGGACGTCGTCATGTCCCTGAACAACCTGGATGAGGAGTCCAACAAGAAGCACCCA
TTCCCGTGCCCTACGTCCTACCGCACGGCCCTCACCTACTACCTGGACATCACCAACCCG
CCGCGTACCAACGTGCTGTACGAGCTGGCGCAGTACGCCTCGGAGCCCTCGGAGCAGGAG
CTGCTGCGCAAGCTGGCCTCCTCCTCCGGCGAGGGCAAGGAGCTGTACCTGAGCTGGGTG
GTGGAGGCCCGGAGGCACATCCTGGCCATCCTGCAGGACTGCCCGTCCCTGCGGCCCCCC
ATCGACCACCTGTGTGAGCTGCTGCCGCGCCTGCAGGCCCGCTACTACTCCATCGCCTCA
TCCTCCAAGGTCCACCCCAACTCTGTGCACATCTGTGCGGTGGTTGTGGAGTACGAGACC
AAGGCCGGCCGCATCAACAAGGGCGTGGCCACCAACTGGCTGCGGGCCAAGGAGCCTGCC
GGGGAGAACGGCGGCCGTGCGCTGGTGCCCATGTTCGTGCGCAAGTCCCAGTTACGCCTG
CCCTTCAAGGCCACCACGCCTGTCATCATGGTGGGCCCCGGCACCGGGGTGGCACCCTTC
ATAGGCTTCATCCAGGAGCGGGCCTGGCTGCGACAGCAGGGCAAGGAGGTGGGGGAGACG
CTGCTGTACTACGGCTGCCGCCGCTCAGATGAGGACTACCTGTACCGGGAGGAGCTGGCG
CAGTTCCACAGGGACGGTGCGCTCACCCAGCTCAACGTGGCCTTCTCCCGGGAGCAGTCC
CACAAGGTCTACGTCCAGCACCTGCTAAAGCAAGACCGAGAGCACCTGTGGAAGTTGATC
GAAGGCGGTGCCCACATCTACGTCTGTGGGGATGCACGGAACATGGCCAGGGATGTGCAG
AACACCTTCTACGACATCGTGGCTGAGCTCGGGGCCATGGAGCACGCGCAGGCGGTGGAC
TACATCAAGAAACTGATGACCAAGGGCCGCTACTCCCTGGACGTGTGGAGCTAG
Enzyme 16 GenBank Gene ID AB051763 Link Image
Enzyme 16 GeneCard ID POR Link Image
Enzyme 16 GenAtlas ID POR Link Image
Enzyme 16 HGNC ID HGNC:9208 Link Image
Enzyme 16 Chromosome Location 7
Enzyme 16 Locus 7q11.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Shephard EA, Palmer CN, Segall HJ, Phillips IR: Quantification of cytochrome P450 reductase gene expression in human tissues. Arch Biochem Biophys. 1992 Apr;294(1):168-72. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Haniu M, McManus ME, Birkett DJ, Lee TD, Shively JE: Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. Biochemistry. 1989 Oct 17;28(21):8639-45. [PubMed Link Image]
  5. Zhao Q, Modi S, Smith G, Paine M, McDonagh PD, Wolf CR, Tew D, Lian LY, Roberts GC, Driessen HP: Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Protein Sci. 1999 Feb;8(2):298-306. [PubMed Link Image]
  6. Adachi M, Tachibana K, Asakura Y, Yamamoto T, Hanaki K, Oka A: Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome. Am J Med Genet A. 2004 Aug 1;128A(4):333-9. [PubMed Link Image]
  7. Fukami M, Horikawa R, Nagai T, Tanaka T, Naiki Y, Sato N, Okuyama T, Nakai H, Soneda S, Tachibana K, Matsuo N, Sato S, Homma K, Nishimura G, Hasegawa T, Ogata T: Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: molecular and clinical studies in 10 patients. J Clin Endocrinol Metab. 2005 Jan;90(1):414-26. Epub 2004 Oct 13. [PubMed Link Image]
  8. Arlt W, Walker EA, Draper N, Ivison HE, Ride JP, Hammer F, Chalder SM, Borucka-Mankiewicz M, Hauffa BP, Malunowicz EM, Stewart PM, Shackleton CH: Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: analytical study. Lancet. 2004 Jun 26;363(9427):2128-35. [PubMed Link Image]
  9. Fluck CE, Tajima T, Pandey AV, Arlt W, Okuhara K, Verge CF, Jabs EW, Mendonca BB, Fujieda K, Miller WL: Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome. Nat Genet. 2004 Mar;36(3):228-30. Epub 2004 Feb 1. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5417
Enzyme 17 Name Dimethylaniline monooxygenase [N-oxide-forming] 1
Enzyme 17 Synonyms
  1. Dimethylaniline oxidase 1
  2. Fetal hepatic flavin-containing monooxygenase 1
  3. FMO 1
Enzyme 17 Gene Name FMO1
Enzyme 17 Protein Sequence >Dimethylaniline monooxygenase [N-oxide-forming] 1 
MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVS
NSCKEMSCYSDFPFPEDYPNYVPNSQFLEYLKMYANHFDLLKHIQFKTKVCSVTKCSDSA
VSGQWEVVTMHEEKQESAIFDAVMVCTGFLTNPYLPLDSFPGINAFKGQYFHSRQYKHPD
IFKDKRVLVIGMGNSGTDIAVEASHLAEKVFLSTTGGGWVISRIFDSGYPWDMVFMTRFQ
NMLRNSLPTPIVTWLMERKINNWLNHANYGLIPEDRTQLKEFVLNDELPGRIITGKVFIR
PSIKEVKENSVIFNNTSKEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAH
LQKPTLAIIGLIKPLGSMIPTGETQARWAVRVLKGVNKLPPPSVMIEEINARKENKPSWF
GLCYCKALQSDYITYIDELLTYINAKPNLFSMLLTDPHLALTVFFGPCSPYQFRLTGPGK
WEGARNAIMTQWDRTFKVIKARVVQESPSPFESFLKVFSFLALLVAIFLIFL
Enzyme 17 Number of Residues 532
Enzyme 17 Molecular Weight 60310.3
Enzyme 17 Theoretical pI 7.22
Enzyme 17 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • flavin-containing monooxygenase activity
  • monooxygenase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 17 General Function Involved in flavin-containing monooxygenase activity
Enzyme 17 Specific Function This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 182671 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q01740 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name FMO1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1599 bp 
ATGGCCAAGCGAGTTGCCATTGTGGGAGCTGGGGTCAGCGGCCTGGCCTCCATCAAGTGC
TGTCTGGAAGAAGGACTGGAGCCCACCTGCTTTGAGAGGAGCGATGACCTTGGGGGGCTG
TGGAGATTCACCGAACATGTTGAAGAAGGCAGAGCCAGTCTCTACAAGTCTGTGGTTTCC
AACAGCTGCAAGGAGATGTCTTGTTACTCAGACTTTCCATTCCCAGAAGATTATCCAAAC
TATGTGCCAAATTCTCAATTCCTGGAATATCTCAAAATGTATGCAAACCACTTTGACCTT
CTGAAACACATTCAATTCAAGACCAAAGTCTGCAGTGTAACAAAATGCTCAGATTCTGCT
GTCTCTGGCCAATGGGAGGTGGTCACTATGCATGAAGAGAAGCAAGAGTCAGCCATCTTT
GATGCTGTCATGGTCTGCACTGGCTTTCTTACTAATCCTTATTTGCCACTGGATTCCTTT
CCAGGTATTAATGCCTTTAAAGGCCAGTACTTTCATAGCCGGCAATATAAGCATCCAGAT
ATATTTAAGGACAAGAGAGTCCTTGTGATTGGAATGGGAAATTCTGGCACAGACATTGCT
GTGGAGGCCAGCCACCTGGCGGAAAAGGTGTTCCTCAGCACCACCGGAGGGGGATGGGTG
ATCAGCCGAATCTTTGACTCGGGCTACCCATGGGACATGGTGTTCATGACACGCTTTCAG
AACATGTTGAGAAATTCCCTCCCAACCCCAATTGTGACTTGGTTGATGGAGCGAAAGATA
AACAACTGGCTCAATCATGCAAATTACGGCTTAATACCAGAAGACAGGACTCAGCTGAAA
GAGTTTGTGCTAAATGATGAGCTCCCAGGACGCATCATCACTGGGAAAGTGTTCATCAGG
CCAAGCATAAAAGAGGTAAAGGAAAACTCTGTCATATTTAACAATACTTCAAAGGAAGAG
CCTATTGACATCATTGTCTTTGCCACTGGATACACATTTGCTTTCCCCTTCCTTGATGAG
TCTGTAGTGAAAGTTGAAGATGGCCAGGCCTCACTGTACAAGTATATCTTCCCTGCACAT
CTGCAAAAGCCAACCCTGGCCATTATTGGCCTCATCAAACCCTTGGGCTCCATGATACCT
ACAGGAGAAACACAAGCTCGGTGGGCTGTTCGAGTCCTGAAAGGTGTAAATAAGTTACCA
CCACCAAGTGTCATGATAGAGGAAATTAATGCAAGGAAAGAAAACAAGCCCAGTTGGTTT
GGCTTGTGCTACTGCAAGGCTTTACAATCAGATTATATCACATACATAGATGAACTCCTG
ACCTATATCAATGCAAAACCCAACCTGTTCTCTATGCTCCTAACGGATCCACATCTGGCT
CTGACCGTCTTCTTTGGCCCATGCTCACCATACCAGTTCCGCTTGACTGGCCCAGGAAAA
TGGGAAGGAGCCAGAAATGCCATCATGACCCAGTGGGACCGAACATTCAAGGTCATCAAA
GCTCGAGTTGTACAAGAGTCTCCATCTCCCTTTGAAAGTTTTCTTAAAGTCTTTAGCTTT
CTGGCTTTGCTTGTGGCTATTTTTCTGATTTTCCTATAA
Enzyme 17 GenBank Gene ID M64082 Link Image
Enzyme 17 GeneCard ID FMO1 Link Image
Enzyme 17 GenAtlas ID FMO1 Link Image
Enzyme 17 HGNC ID HGNC:3769 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 1q24.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Dolphin C, Shephard EA, Povey S, Palmer CN, Ziegler DM, Ayesh R, Smith RL, Phillips IR: Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1). J Biol Chem. 1991 Jul 5;266(19):12379-85. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5420
Enzyme 18 Name Methylenetetrahydrofolate reductase
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name MTHFR
Enzyme 18 Protein Sequence >Methylenetetrahydrofolate reductase 
MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVK
HIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFV
KACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIE
LAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREE
DVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKM
WGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGIL
TINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHL
VNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYE
EESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP
Enzyme 18 Number of Residues 656
Enzyme 18 Molecular Weight 74595.9
Enzyme 18 Theoretical pI 5.00
Enzyme 18 GO Classification
Function
  • catalytic activity
  • methylenetetrahydrofolate reductase (NADPH) activity
  • methylenetetrahydrofolate reductase (NADPH) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine metabolic process
  • oxidation reduction
  • sulfur amino acid metabolic process
Component
—
Enzyme 18 General Function Involved in methylenetetrahydrofolate reductase (NADPH) activity
Enzyme 18 Specific Function Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine
Enzyme 18 Pathways
Enzyme 18 Reactions
  • 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+ [RN:R01224 R07168]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 6139053 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P42898 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name MTHR_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1971 bp 
ATGGTGAACGAAGCCAGAGGAAACAGCAGCCTCAACCCCTGCTTGGAGGGCAGTGCCAGC
AGTGGCAGTGAGAGCTCCAAAGATAGTTCGAGATGTTCCACCCCGGGCCTGGACCCTGAG
CGGCATGAGAGACTCCGGGAGAAGATGAGGCGGCGATTGGAATCTGGTGACAAGTGGTTC
TCCCTGGAATTCTTCCCTCCTCGAACTGCTGAGGGAGCTGTCAATCTCATCTCAAGGTTT
GACCGGATGGCAGCAGGTGGCCCCCTCTACATAGACGTGACCTGGCACCCAGCAGGTGAC
CCTGGCTCAGACAAGGAGACCTCCTCCATGATGATCGCCAGCACCGCCGTGAACTACTGT
GGCCTGGAGACCATCCTGCACATGACCTGCTGCCGTCAGCGCCTGGAGGAGATCACGGGC
CATCTGCACAAAGCTAAGCAGCTGGGCCTGAAGAACATCATGGCGCTGCGGGGAGACCCA
ATAGGTGACCAGTGGGAAGAGGAGGAGGGAGGCTTCAACTACGCAGTGGACCTGGTGAAG
CACATCCGAAGTGAGTTTGGTGACTACTTTGACATCTGTGTGGCAGGTTACCCCAAAGGC
CACCCCGAAGCAGGGAGCTTTGAGGCTGACCTGAAGCACTTGAAGGAGAAGGTGTCTGCG
GGAGCCGATTTCATCATCACGCAGCTTTTCTTTGAGGCTGACACATTCTTCCGCTTTGTG
AAGGCATGCACCGACATGGGCATCACTTGCCCCATCGTCCCCGGGATCTTTCCCATCCAG
GGCTACCACTCCCTTCGGCAGCTTGTGAAGCTGTCCAAGCTGGAGGTGCCACAGGAGATC
AAGGACGTGATTGAGCCAATCAAAGACAACGATGCTGCCATCCGCAACTATGGCATCGAG
CTGGCCGTGAGCCTGTGCCAGGAGCTTCTGGCCAGTGGCTTGGTGCCAGGCCTCCACTTC
TACACCCTCAACCGCGAGATGGCTACCACAGAGGTGCTGAAGCGCCTGGGGATGTGGACT
GAGGACCCCAGGCGTCCCCTACCCTGGGCTCTCAGTGCCCACCCCAAGCGCCGAGAGGAA
GATGTACGTCCCATCTTCTGGGCCTCCAGACCAAAGAGTTACATCTACCGTACCCAGGAG
TGGGACGAGTTCCCTAACGGCCGCTGGGGCAATTCCTCTTCCCCTGCCTTTGGGGAGCTG
AAGGACTACTACCTCTTCTACCTGAAGAGCAAGTCCCCCAAGGAGGAGCTGCTGAAGATG
TGGGGGGAGGAGCTGACCAGTGAAGCAAGTGTCTTTGAAGTCTTTGTTCTTTACCTCTCG
GGAGAACCAAACCGGAATGGTCACAAAGTGACTTGCCTGCCCTGGAACGATGAGCCCCTG
GCGGCTGAGACCAGCCTGCTGAAGGAGGAGCTGCTGCGGGTGAACCGCCAGGGCATCCTC
ACCATCAACTCACAGCCCAACATCAACGGGAAGCCGTCCTCCGACCCCATCGTGGGCTGG
GGCCCCAGCGGGGGCTATGTCTTCCAGAAGGCCTACTTAGAGTTTTTCACTTCCCGCGAG
ACAGCGGAAGCACTTCTGCAAGTGCTGAAGAAGTACGAGCTCCGGGTTAATTACCACCTT
GTCAATGTGAAGGGTGAAAACATCACCAATGCCCCTGAACTGCAGCCGAATGCTGTCACT
TGGGGCATCTTCCCTGGGCGAGAGATCATCCAGCCCACCGTAGTGGATCCCGTCAGCTTC
ATGTTCTGGAAGGACGAGGCCTTTGCCCTGTGGATTGAGCGGTGGGGAAAGCTGTATGAG
GAGGAGTCCCCGTCCCGCACCATCATCCAGTACATCCACGACAACTACTTCCTGGTCAAC
CTGGTGGACAATGACTTCCCACTGGACAACTGCCTCTGGCAGGTGGTGGAAGACACATTG
GAGCTTCTCAACAGGCCCACCCAGAATGCGAGAGAAACGGAGGCTCCATGA
Enzyme 18 GenBank Gene ID U09806 Link Image
Enzyme 18 GeneCard ID MTHFR Link Image
Enzyme 18 GenAtlas ID MTHFR Link Image
Enzyme 18 HGNC ID HGNC:7436 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1p36.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Goyette P, Pai A, Milos R, Frosst P, Tran P, Chen Z, Chan M, Rozen R: Gene structure of human and mouse methylenetetrahydrofolate reductase (MTHFR) Mamm Genome. 1998 Aug;9(8):652-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Nat Genet. 1994 Jun;7(2):195-200. [PubMed Link Image]
  6. Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA mapping and mutation identification. Nat Genet. 1994 Aug;7(4):551. [PubMed Link Image]
  7. Goyette P, Frosst P, Rosenblatt DS, Rozen R: Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency. Am J Hum Genet. 1995 May;56(5):1052-9. [PubMed Link Image]
  8. van der Put NM, Steegers-Theunissen RP, Frosst P, Trijbels FJ, Eskes TK, van den Heuvel LP, Mariman EC, den Heyer M, Rozen R, Blom HJ: Mutated methylenetetrahydrofolate reductase as a risk factor for spina bifida. Lancet. 1995 Oct 21;346(8982):1070-1. [PubMed Link Image]
  9. Frosst P, Blom HJ, Milos R, Goyette P, Sheppard CA, Matthews RG, Boers GJ, den Heijer M, Kluijtmans LA, van den Heuvel LP, et al.: A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nat Genet. 1995 May;10(1):111-3. [PubMed Link Image]
  10. Ou CY, Stevenson RE, Brown VK, Schwartz CE, Allen WP, Khoury MJ, Rozen R, Oakley GP Jr, Adams MJ Jr: 5,10 Methylenetetrahydrofolate reductase genetic polymorphism as a risk factor for neural tube defects. Am J Med Genet. 1996 Jun 28;63(4):610-4. [PubMed Link Image]
  11. Goyette P, Christensen B, Rosenblatt DS, Rozen R: Severe and mild mutations in cis for the methylenetetrahydrofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR. Am J Hum Genet. 1996 Dec;59(6):1268-75. [PubMed Link Image]
  12. Chen J, Giovannucci E, Kelsey K, Rimm EB, Stampfer MJ, Colditz GA, Spiegelman D, Willett WC, Hunter DJ: A methylenetetrahydrofolate reductase polymorphism and the risk of colorectal cancer. Cancer Res. 1996 Nov 1;56(21):4862-4. [PubMed Link Image]
  13. Schneider JA, Rees DC, Liu YT, Clegg JB: Worldwide distribution of a common methylenetetrahydrofolate reductase mutation. Am J Hum Genet. 1998 May;62(5):1258-60. [PubMed Link Image]
  14. van der Put NM, Gabreels F, Stevens EM, Smeitink JA, Trijbels FJ, Eskes TK, van den Heuvel LP, Blom HJ: A second common mutation in the methylenetetrahydrofolate reductase gene: an additional risk factor for neural-tube defects? Am J Hum Genet. 1998 May;62(5):1044-51. [PubMed Link Image]
  15. Kluijtmans LA, Wendel U, Stevens EM, van den Heuvel LP, Trijbels FJ, Blom HJ: Identification of four novel mutations in severe methylenetetrahydrofolate reductase deficiency. Eur J Hum Genet. 1998 May-Jun;6(3):257-65. [PubMed Link Image]
  16. Weisberg I, Tran P, Christensen B, Sibani S, Rozen R: A second genetic polymorphism in methylenetetrahydrofolate reductase (MTHFR) associated with decreased enzyme activity. Mol Genet Metab. 1998 Jul;64(3):169-72. [PubMed Link Image]
  17. Christensen B, Arbour L, Tran P, Leclerc D, Sabbaghian N, Platt R, Gilfix BM, Rosenblatt DS, Gravel RA, Forbes P, Rozen R: Genetic polymorphisms in methylenetetrahydrofolate reductase and methionine synthase, folate levels in red blood cells, and risk of neural tube defects. Am J Med Genet. 1999 May 21;84(2):151-7. [PubMed Link Image]
  18. Skibola CF, Smith MT, Kane E, Roman E, Rollinson S, Cartwright RA, Morgan G: Polymorphisms in the methylenetetrahydrofolate reductase gene are associated with susceptibility to acute leukemia in adults. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12810-5. [PubMed Link Image]
  19. Sibani S, Christensen B, O'Ferrall E, Saadi I, Hiou-Tim F, Rosenblatt DS, Rozen R: Characterization of six novel mutations in the methylenetetrahydrofolate reductase (MTHFR) gene in patients with homocystinuria. Hum Mutat. 2000;15(3):280-7. [PubMed Link Image]
  20. Casas JP, Hingorani AD, Bautista LE, Sharma P: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. Arch Neurol. 2004 Nov;61(11):1652-61. [PubMed Link Image]
  21. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5428
Enzyme 19 Name Glutathione reductase, mitochondrial
Enzyme 19 Synonyms
  1. GR
  2. GRase
Enzyme 19 Gene Name GSR
Enzyme 19 Protein Sequence >Glutathione reductase, mitochondrial 
MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAG
AVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHS
EFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDP
KPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAG
YIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK
TLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD
EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPP
IGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQ
GLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
Enzyme 19 Number of Residues 522
Enzyme 19 Molecular Weight 56256.6
Enzyme 19 Theoretical pI 8.66
Enzyme 19 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • glutathione disulfide oxidoreductase activity
  • glutathione-disulfide reductase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • peptide disulfide oxidoreductase activity
  • purine nucleoside binding
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular metabolic process
  • cellular process
  • glutathione metabolic process
  • metabolic process
  • oxidation reduction
  • peptide metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 19 General Function Involved in oxidoreductase activity
Enzyme 19 Specific Function Maintains high levels of reduced glutathione in the cytosol
Enzyme 19 Pathways
Enzyme 19 Reactions
  • 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ [RN:R00115]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 50301238 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P00390 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name GSHR_HUMAN Link Image
Enzyme 19 PDB ID 1BWC Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1569 bp 
ATGGCCCTGCTGCCCCGAGCCCTGAGCGCCGGCGCGGGACCGAGCTGGCGGCGGGCGGCG
CGCGCCTTCCGAGGCTTCCTGCTGCTTCTGCCCGAGCCCGCGGCCCTCACGCGCGCCCTC
TCCCGTGCCATGGCCTGCAGGCAGGAGCCGCAGCCGCAGGGCCCGCCGCCCGCTGCTGGC
GCCGTGGCCTCCTATGACTACCTGGTGATCGGGGGCGGCTCGGGCGGGCTGGCCAGCGCG
CGCAGGGCGGCCGAGCTGGGTGCCAGGGCCGCCGTGGTGGAGAGCCACAAGCTGGGTGGC
ACTTGCGTGAATGTTGGATGTGTACCCAAAAAGGTAATGTGGAACACAGCTGTCCACTCT
GAATTCATGCATGATCATGCTGATTATGGCTTTCCAAGTTGTGAGGGTAAATTCAATTGG
CGTGTTATTAAGGAAAAGCGGGATGCCTATGTGAGCCGCCTGAATGCCATCTATCAAAAC
AATCTCACCAAGTCCCATATAGAAATCATCCGTGGCCATGCAGCCTTCACGAGTGATCCC
AAGCCCACAATAGAGGTCAGTGGGAAAAAGTACACCGCCCCACACATCCTGATCGCCACA
GGTGGTATGCCCTCCACCCCTCATGAGAGCCAGATCCCCGGTGCCAGCTTAGGAATAACC
AGCGATGGATTTTTTCAGCTGGAAGAATTGCCCGGCCGCAGCGTCATTGTTGGTGCAGGT
TACATTGCTGTGGAGATGGCAGGGATCCTGTCAGCCCTGGGTTCTAAGACATCACTGATG
ATACGGCATGATAAGGTACTTAGAAGTTTTGATTCAATGATCAGCACCAACTGCACGGAG
GAGCTGGAGAACGCTGGCGTGGAGGTGCTGAAGTTCTCCCAGGTCAAGGAGGTTAAAAAG
ACTTTGTCGGGCTTGGAAGTCAGCATGGTTACTGCAGTTCCCGGTAGGCTACCAGTCATG
ACCATGATTCCAGATGTTGACTGCCTGCTCTGGGCCATTGGGCGGGTCCCGAATACCAAG
GACCTGAGTTTAAACAAACTGGGGATTCAAACCGATGACAAGGGTCATATCATCGTAGAC
GAATTCCAGAATACCAACGTCAAAGGCATCTATGCAGTTGGGGATGTATGTGGAAAAGCT
CTTCTTACTCCAGTTGCAATAGCTGCTGGCCGAAAACTTGCCCATCGACTTTTTGAATAT
AAGGAAGATTCCAAATTAGATTATAACAACATCCCAACTGTGGTCTTCAGCCACCCCCCT
ATTGGGACAGTGGGACTCACGGAAGATGAAGCCATTCATAAATATGGAATAGAAAATGTG
AAGACCTATTCAACGAGCTTTACCCCGATGTATCACGCAGTTACCAAAAGGAAAACAAAA
TGTGTGATGAAAATGGTCTGTGCTAACAAGGAAGAAAAGGTGGTTGGGATCCATATGCAG
GGACTTGGGTGTGATGAAATGCTGCAGGGTTTTGCTGTTGCAGTGAAGATGGGAGCAACG
AAGGCAGACTTTGACAACACAGTCGCCATTCACCCTACCTCTTCAGAAGAGCTGGTCACA
CTTCGTTGA
Enzyme 19 GenBank Gene ID NM_000637.3 Link Image
Enzyme 19 GeneCard ID GSR Link Image
Enzyme 19 GenAtlas ID GSR Link Image
Enzyme 19 HGNC ID HGNC:4623 Link Image
Enzyme 19 Chromosome Location 8
Enzyme 19 Locus 8p21.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Tutic M, Lu XA, Schirmer RH, Werner D: Cloning and sequencing of mammalian glutathione reductase cDNA. Eur J Biochem. 1990 Mar 30;188(3):523-8. [PubMed Link Image]
  2. Kelner MJ, Montoya MA: Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun. 2000 Mar 16;269(2):366-8. [PubMed Link Image]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259-67. [PubMed Link Image]
  6. Krohne-Ehrich G, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. Eur J Biochem. 1977 Oct 17;80(1):65-71. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Thieme R, Pai EF, Schirmer RH, Schulz GE: Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol. 1981 Nov 15;152(4):763-82. [PubMed Link Image]
  9. Karplus PA, Schulz GE: Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. [PubMed Link Image]
  10. Savvides SN, Karplus PA: Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. [PubMed Link Image]
  11. Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. [PubMed Link Image]
  12. Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5430
Enzyme 20 Name Heme oxygenase 1
Enzyme 20 Synonyms
  1. HO-1
Enzyme 20 Gene Name HMOX1
Enzyme 20 Protein Sequence >Heme oxygenase 1 
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVA
LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHE
VGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ
LYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA
SNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Enzyme 20 Number of Residues 288
Enzyme 20 Molecular Weight 32818.3
Enzyme 20 Theoretical pI 8.68
Enzyme 20 GO Classification
Function
  • catalytic activity
  • heme oxygenase (decyclizing) activity
  • heme oxygenase (decyclizing) activity
  • heme oxygenase (decyclizing) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Process
  • heme metabolic process
  • heme oxidation
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin metabolic process
  • tetrapyrrole metabolic process
Component
—
Enzyme 20 General Function Involved in heme oxygenase (decyclizing) activity
Enzyme 20 Specific Function Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed
Enzyme 20 Pathways
Enzyme 20 Reactions
  • heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O [RN:R00311]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 35173 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P09601 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name HMOX1_HUMAN Link Image
Enzyme 20 PDB ID 1T5P Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >867 bp 
ATGGAGCGTCCGCAACCCGACAGCATGCCCCAGGATTTGTCAGAGGCCCTGAAGGAGGCC
ACCAAGGAGGTGCACACCCAGGCAGAGAATGCTGAGTTCATGAGGAACTTTCAGAAGGGC
CAGGTGACCCGAGACGGCTTCAAGCTGGTGATGGCCTCCCTGTACCACATCTATGTGGCC
CTGGAGGAGGAGATTGAGCGCAACAAGGAGAGCCCAGTCTTCGCCCCTGTCTACTTCCCA
GAAGAGCTGCACCGCAAGGCTGCCCTGGAGCAGGACCTGGCCTTCTGGTACGGGCCCCGC
TGGCAGGAGGTCATCCCCTACACACCAGCCATGCAGCGCTATGTGAAGCGGCTCCACGAG
GTGGGGCGCACAGAGCCCGAGCTGCTGGTGGCCCACGCCTACACCCGCTACCTGGGTGAC
CTGTCTGGGGGCCAGGTGCTCAAAAAGATTGCCCAGAAAGCCCTGGACCTGCCCAGCTCT
GGCGAGGGCCTGGCCTTCTTCACCTTCCCCAACATTGCCAGTGCCACCAAGTTCAAGCAG
CTCTACCGCTCCCGCATGAACTCCCTGGAGATGACTCCCGCAGTCAGGCAGAGGGTGATA
GAAGAGGCCAAGACTGCGTTCCTGCTCAACATCCAGCTCTTTGAGGAGTTGCAGGAGCTG
CTGACCCATGACACCAAGGACCAGAGCCCCTCACGGGCACCAGGGCTTCGCCAGCGGGCC
AGCAACAAAGTGCAAGATTCTGCCCCCGTGGAGACTCCCAGAGGGAAGCCCCCACTCAAC
ACCCGCTCCCAGGCTCCGCTTCTCCGATGGGTCCTTACACTCAGCTTTCTGGTGGCGACA
GTTGCTGTAGGGCTTTATGCCATGTGA
Enzyme 20 GenBank Gene ID X06985 Link Image
Enzyme 20 GeneCard ID HMOX1 Link Image
Enzyme 20 GenAtlas ID HMOX1 Link Image
Enzyme 20 HGNC ID HGNC:5013 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 22q12|22q13.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Yoshida T, Biro P, Cohen T, Muller RM, Shibahara S: Human heme oxygenase cDNA and induction of its mRNA by hemin. Eur J Biochem. 1988 Feb 1;171(3):457-61. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  4. Keyse SM, Tyrrell RM: Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci U S A. 1989 Jan;86(1):99-103. [PubMed Link Image]
  5. Shibahara S, Sato M, Muller RM, Yoshida T: Structural organization of the human heme oxygenase gene and the function of its promoter. Eur J Biochem. 1989 Feb 15;179(3):557-63. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  9. Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL: Crystal structure of human heme oxygenase-1. Nat Struct Biol. 1999 Sep;6(9):860-7. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5436
Enzyme 21 Name NADPH:adrenodoxin oxidoreductase, mitochondrial
Enzyme 21 Synonyms
  1. AR
  2. Adrenodoxin reductase
  3. Ferredoxin--NADP(+) reductase
  4. Ferredoxin reductase
Enzyme 21 Gene Name FDXR
Enzyme 21 Protein Sequence >NADPH:adrenodoxin oxidoreductase, mitochondrial 
MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLKH
PQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVP
ELREAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAV
ILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKE
LREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASAS
RAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSI
GYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQM
LLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLV
DPQEMLRLLGH
Enzyme 21 Number of Residues 491
Enzyme 21 Molecular Weight 53836.4
Enzyme 21 Theoretical pI 8.56
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Involved in catalytic activity
Enzyme 21 Specific Function Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver
Enzyme 21 Pathways
Enzyme 21 Reactions
  • 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH [RN:R01195]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 12804205 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P22570 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name ADRO_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1476 bp 
ATGGCTTCGCGCTGCTGGCGCTGGTGGGGCTGGTCGGCGTGGCCTCGGACCCGGCTGCCT
CCCGCCGGGAGCACCCCGAGCTTCTGCCACCATTTCTCCACACAGGAGAAGACCCCCCAG
ATCTGTGTGGTGGGCAGTGGCCCAGCTGGCTTCTACACGGCCCAACACCTGCTAAAGCAC
CCCCAGGCCCACGTGGACATCTACGAGAAACAGCCTGTGCCCTTTGGCCTGGTGCGCTTT
GGTGTGGCGCCTGATCACCCCGAGGTGAAGAATGTCATCAACACATTTACCCAGACGGCC
CATTCTGGCCGCTGTGCCTTCTGGGGCAACGTGGAGGTGGGCAGGGACGTGACGGTGCCG
GAGCTGCGGGAGGCCTACCACGCTGTGGTGCTGAGCTACGGGGCAGAGGACCATCGGGCC
CTGGAAATTCCTGGTGAGGAGCTGCCAGGTGTGTGCTCCGCCCGGGCCTTCGTGGGCTGG
TACAACGGGCTTCCTGAGAACCAGGAGCTGGAGCCAGACCTGAGCTGTGACACAGCCGTG
ATTCTGGGGCAGGGGAACGTGGCTCTGGACGTGGCCCGCATCCTACTGACCCCACCTGAG
CACCTGGAGAGAACGGACATCACGAAGGCAGCCCTGGGTGTACTGAGGCAGAGTCGAGTG
AAGACAGTGTGGCTAGTGGGCCGGCGTGGACCCCTGCAAGTGGCCTTCACCATTAAGGAG
CTTCGGGAGATGATTCAGTTACCGGGAGCCCGGCCCATTTTGGATCCTGTGGATTTCTTG
GGTCTCCAGGACAAGATCAAGGAGGTCCCCCGCCCGAGGAAGCGGCTGACGGAACTGCTG
CTTCGAACGGCCACAGAGAAGCCAGGGCCGGCGGAAGCTGCCCGCCAGGCATCGGCCTCC
CGTGCCTGGGGCCTCCGCTTTTTCCGAAGCCCCCAGCAGGTGCTGCCCTCACCAGATGGG
CGGCGGGCAGCAGGTGTCCGCCTAGCAGTCACTAGACTGGAGGGTGTCGATGAGGCCACC
CGTGCAGTGCCCACGGGAGACATGGAAGACCTCCCTTGTGGGCTGGTGCTCAGCAGCATT
GGGTATAAGAGCCGCCCTGTCGACCCAAGCGTGCCCTTTGACTCCAAGCTTGGGGTCATC
CCCAATGTGGAGGGCCGGGTTATGGATGTGCCAGGCCTCTACTGCAGCGGCTGGGTGAAG
AGAGGACCTACAGGTGTCATAGCCACAACCATGACTGACAGCTTCCTCACCGGCCAGATG
CTGCTGCAGGACCTGAAGGCTGGGTTGCTCCCCTCTGGCCCCAGGCCTGGCTACGCAGCC
ATCCAGGCCCTGCTCAGCAGCCGAGGGGTCCGGCCAGTCTCTTTCTCAGACTGGGAGAAG
CTGGATGCCGAGGAGGTGGCCCGGGGCCAGGGCACGGGGAAGCCCAGGGAGAAGCTGGTG
GATCCTCAGGAGATGCTGCGCCTCCTGGGCCACTGA
Enzyme 21 GenBank Gene ID BC002960 Link Image
Enzyme 21 GeneCard ID FDXR Link Image
Enzyme 21 GenAtlas ID FDXR Link Image
Enzyme 21 HGNC ID HGNC:3642 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 17q24-q25
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Solish SB, Picado-Leonard J, Morel Y, Kuhn RW, Mohandas TK, Hanukoglu I, Miller WL: Human adrenodoxin reductase: two mRNAs encoded by a single gene on chromosome 17cen----q25 are expressed in steroidogenic tissues. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7104-8. [PubMed Link Image]
  2. Lin D, Shi YF, Miller WL: Cloning and sequence of the human adrenodoxin reductase gene. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8516-20. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5492
Enzyme 22 Name Squalene synthase
Enzyme 22 Synonyms
  1. SQS
  2. SS
  3. FPP:FPP farnesyltransferase
  4. Farnesyl-diphosphate farnesyltransferase
Enzyme 22 Gene Name FDFT1
Enzyme 22 Protein Sequence >Squalene synthase 
MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQA
LDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQ
VLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVG
IGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYV
KKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATL
AACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTR
QIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
Enzyme 22 Number of Residues 417
Enzyme 22 Molecular Weight 48114.9
Enzyme 22 Theoretical pI 6.51
Enzyme 22 GO Classification
Function
  • catalytic activity
  • farnesyl-diphosphate farnesyltransferase activity
  • farnesyltranstransferase activity
  • prenyltransferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • biosynthetic process
  • lipid biosynthetic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 22 General Function Involved in transferase activity
Enzyme 22 Specific Function 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Enzyme 22 Pathways
Enzyme 22 Reactions
  • (1) (1a) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate [RN:R00702]
  • (2) (1b) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+ [RN:R02872]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 284-304 384-404
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID P37268 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name FDFT_HUMAN Link Image
Enzyme 22 PDB ID 1EZF Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1254 bp 
ATGGAGTTCGTGAAATGCCTTGGCCACCCCGAAGAGTTCTACAACCTGGTGCGCTTCCGG
ATCGGGGGCAAGCGGAAGGTGATGCCCAAGATGGACCAGGACTCGCTCAGCAGCAGCCTG
AAAACTTGCTACAAGTATCTCAATCAGACCAGTCGCAGTTTCGCAGCTGTTATCCAGGCG
CTGGATGGGGAAATGCGCAACGCAGTGTGCATATTTTATCTGGTTCTCCGAGCTCTGGAC
ACACTGGAAGATGACATGACCATCAGTGTGGAAAAGAAGGTCCCGCTGTTACACAACTTT
CACTCTTTCCTTTACCAACCAGACTGGCGGTTCATGGAGAGCAAGGAGAAGGATCGCCAG
GTGCTGGAGGACTTCCCAACGATCTCCCTTGAGTTTAGAAATCTGGCTGAGAAATACCAA
ACAGTGATTGCCGACATTTGCCGGAGAATGGGCATTGGGATGGCAGAGTTTTTGGATAAG
CATGTGACCTCTGAACAGGAGTGGGACAAGTACTGCCACTATGTTGCTGGGCTGGTCGGA
ATTGGCCTTTCCCGTCTTTTCTCAGCCTCAGAGTTTGAAGACCCCTTAGTTGGTGAAGAT
ACAGAACGTGCCAACTCTATGGGCCTGTTTCTGCAGAAAACAAACATCATCCGTGACTAT
CTGGAAGACCAGCAAGGAGGAAGAGAGTTCTGGCCTCAAGAGGTTTGGAGCAGGTATGTT
AAGAAGTTAGGGGATTTTGCTAAGCCGGAGAATATTGACTTGGCCGTGCAGTGCCTGAAT
GAACTTATAACCAATGCACTGCACCACATCCCAGATGTCATCACCTACCTTTCGAGACTC
AGAAACCAGAGTGTGTTTAACTTCTGCGCTATTCCACAGGTGATGGCCATTGCCACTTTG
GCTGCCTGTTATAATAACCAGCAGGTGTTCAAAGGGGCAGTGAAGATTCGGAAAGGGCAA
GCAGTGACCCTGATGATGGATGCCACCAATATGCCAGCTGTCAAAGCCATCATATATCAG
TATATGGAAGAGATTTATCATAGAATCCCCGACTCAGACCCATCTTCTAGCAAAACAAGG
CAGATCATCTCCACCATCCGGACGCAGAATCTTCCCAACTGTCAGCTGATTTCCCGAAGC
CACTACTCCCCCATCTACCTGTCGTTTGTCATGCTTTTGGCTGCCCTGAGCTGGCAGTAC
CTGACCACTCTCTCCCAGGTAACAGAAGACTATGTTCAGACTGGAGAACACTGA
Enzyme 22 GenBank Gene ID L06070 Link Image
Enzyme 22 GeneCard ID FDFT1 Link Image
Enzyme 22 GenAtlas ID FDFT1 Link Image
Enzyme 22 HGNC ID HGNC:3629 Link Image
Enzyme 22 Chromosome Location 8
Enzyme 22 Locus 8p23.1-p22
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Robinson GW, Tsay YH, Kienzle BK, Smith-Monroy CA, Bishop RW: Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation. Mol Cell Biol. 1993 May;13(5):2706-17. [PubMed Link Image]
  2. Jiang G, McKenzie TL, Conrad DG, Shechter I: Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase. J Biol Chem. 1993 Jun 15;268(17):12818-24. [PubMed Link Image]
  3. Summers C, Karst F, Charles AD: Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase. Gene. 1993 Dec 22;136(1-2Che):185-92. [PubMed Link Image]
  4. Soltis DA, McMahon G, Caplan SL, Dudas DA, Chamberlin HA, Vattay A, Dottavio D, Rucker ML, Engstrom RG, Cornell-Kennon SA, et al.: Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems. Arch Biochem Biophys. 1995 Feb 1;316(2):713-23. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM, Hamanaka ES, Thompson JF, Harwood HJ Jr: Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J Biol Chem. 2000 Sep 29;275(39):30610-7. [PubMed Link Image]
  7. Do R, Pare G, Montpetit A, Hudson TJ, Gaudet D, Engert JC: K45R variant of squalene synthase increases total cholesterol levels in two study samples from a French Canadian population. Hum Mutat. 2008 May;29(5):689-94. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5494
Enzyme 23 Name Delta(14)-sterol reductase
Enzyme 23 Synonyms
  1. Delta-14-SR
  2. Another new gene 1 protein
  3. C-14 sterol reductase
  4. Putative sterol reductase SR-1
  5. Sterol C14-reductase
  6. Transmembrane 7 superfamily member 2
Enzyme 23 Gene Name TM7SF2
Enzyme 23 Protein Sequence >Delta(14)-sterol reductase 
MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSP
RALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAG
LPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELN
PRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWH
EEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATG
YYIFRGANSQKNTFRKNPSDPRVAGLETISTATGRKLLVSGWWGMVRHPNYLGDLIMALA
WSLPCGVSHLLPYFYLLYFTALLVHREARDERQCLQKYGLAWQEYCRRVPYRIMPYIY
Enzyme 23 Number of Residues 418
Enzyme 23 Molecular Weight 46405.3
Enzyme 23 Theoretical pI 9.04
Enzyme 23 GO Classification
Function
—
Process
—
Component
  • cell part
  • membrane
Enzyme 23 General Function Involved in delta14-sterol reductase activity
Enzyme 23 Specific Function Involved in the conversion of lanosterol to cholesterol
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+ [RN:R05639]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 13-35 62-81 102-124 129-148 255-277 287-304 355-377
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 117414150 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O76062 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name ERG24_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1257 bp 
ATGGCCCCCACTCAGGGCCCCCGGGCCCCGCTGGAATTCGGAGGGCCCCTGGGCGCCGCG
GCTCTGCTACTGCTGCTGCCCGCCACCATGTTCCACCTGCTCCTGGCGGCCCGTTCGGGC
CCCGCGCGCCTGCTGGGTCCACCCGCGTCCCTGCCCGGGCTGGAGGTGCTGTGGAGCCCA
CGGGCGCTGCTGCTGTGGCTCGCCTGGCTCGGCCTGCAGGCGGCGCTCTACCTACTGCCG
GCGCGCAAGGTGGCCGAGGGGCAGGAATTGAAGGACAAGAGTCGCCTGCGCTATCCTATT
AACGGCTTCCAGGCCCTGGTGCTGACAGCCCTGTTGGTGGGGCTGGGGATGTCAGCGGGG
CTGCCTCTGGGGGCGCTCCCGGAAATGCTCCTGCCCTTGGCGTTTGTCGCCACCCTCACC
GCTTTCATCTTCAGCCTCTTTCTCTACATGAAGGCGCAGGTAGCCCCAGTTTCGGCCCTG
GCACCTGGGGGGAACTCAGGCAATCCGATTTACGACTTTTTTCTGGGACGAGAGCTCAAC
CCTCGTATCTGTTTCTTCGACTTCAAATATTTCTGTGAACTGCGACCCGGCCTCATCGGC
TGGGTCCTCATCAACCTGGCCCTGTTGATGAAGGAGGCAGAGCTTCGAGGCAGTCCCTCA
CTGGCCATGTGGCTGGTCAATGGCTTCCAGTTGCTCTACGTGGGTGATGCCCTCTGGCAC
GAGGAGGCCGTCCTCACCACCATGGATATCACACATGACGGGTTTGGCTTCATGCTGGCG
TTTGGGGACATGGCCTGGGTGCCCTTCACCTACAGCCTGCAGGCCCAGTTCCTGCTGCAC
CACCCGCAGCCCCTGGGGTTGCCCATGGCCTCTGTCATCTGCCTCATCAATGCTACTGGT
TACTACATCTTCCGTGGGGCGAATTCCCAGAAAAACACTTTCCGAAAGAATCCTTCTGAC
CCCAGAGTGGCTGGGCTTGAGACCATCTCTACAGCCACAGGGCGGAAACTGCTGGTGTCT
GGGTGGTGGGGTATGGTCCGCCATCCCAACTATCTTGGAGACCTCATCATGGCTCTGGCT
TGGTCCTTGCCCTGCGGGGTGTCACACCTGCTGCCCTACTTCTACCTCCTCTACTTCACC
GCGCTGCTGGTGCACCGTGAGGCCCGGGATGAGCGGCAGTGCCTGCAGAAGTACGGCCTG
GCCTGGCAGGAGTACTGCCGGCGTGTGCCTTACCGCATCATGCCCTACATCTACTGA
Enzyme 23 GenBank Gene ID NM_003273.2 Link Image
Enzyme 23 GeneCard ID TM7SF2 Link Image
Enzyme 23 GenAtlas ID TM7SF2 Link Image
Enzyme 23 HGNC ID HGNC:11863 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 11q13
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Lemmens IH, Kas K, Merregaert J, Van de Ven WJ: Identification and molecular characterization of TM7SF2 in the FAUNA gene cluster on human chromosome 11q13. Genomics. 1998 May 1;49(3):437-42. [PubMed Link Image]
  2. Holmer L, Pezhman A, Worman HJ: The human lamin B receptor/sterol reductase multigene family. Genomics. 1998 Dec 15;54(3):469-76. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Roberti R, Bennati AM, Galli G, Caruso D, Maras B, Aisa C, Beccari T, Della Fazia MA, Servillo G: Cloning and expression of sterol Delta 14-reductase from bovine liver. Eur J Biochem. 2002 Jan;269(1):283-90. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5496
Enzyme 24 Name Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
Enzyme 24 Synonyms
  1. Protein H105e3
Enzyme 24 Gene Name NSDHL
Enzyme 24 Protein Sequence >Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating 
MEPAVSEPMRDQVARTHLTEDTPKVNADIEKVNQNQAKRCTVIGGSGFLGQHMVEQLLAR
GYAVNVFDIQQGFDNPQVRFFLGDLCSRQDLYPALKGVNTVFHCASPPPSSNNKELFYRV
NYIGTKNVIETCKEAGVQKLILTSSASVIFEGVDIKNGTEDLPYAMKPIDYYTETKILQE
RAVLGANDPEKNFLTTAIRPHGIFGPRDPQLVPILIEAARNGKMKFVIGNGKNLVDFTFV
ENVVHGHILAAEQLSRDSTLGGKAFHITNDEPIPFWTFLSRILTGLNYEAPKYHIPYWVA
YYLALLLSLLVMVISPVIQLQPTFTPMRVALAGTFHYYSCERAKKAMGYQPLVTMDDAME
RTVQSFRHLRRVK
Enzyme 24 Number of Residues 373
Enzyme 24 Molecular Weight 41900.0
Enzyme 24 Theoretical pI 8.20
Enzyme 24 GO Classification
Function
  • 3-beta-hydroxy-delta5-steroid dehydrogenase activity
  • binding
  • catalytic activity
  • oxidoreductase activity
  • steroid dehydrogenase activity
  • steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • steroid biosynthetic process
  • steroid metabolic process
Component
—
Enzyme 24 General Function Involved in 3-beta-hydroxy-delta5-steroid dehydrogenase activity
Enzyme 24 Specific Function 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest- 7-ene-4-alpha-carboxylate + NAD(P)(+) = 4-alpha-methyl-5-alpha- cholest-7-en-3-one + CO(2) + NAD(P)H
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + NAD(P)+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NAD(P)H [RN:R04483 R07149]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 298-318
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID Q15738 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name NSDHL_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1122 bp 
ATGGAACCAGCAGTTAGCGAGCCAATGAGAGACCAAGTCGCACGGACTCATTTGACAGAG
GACACTCCCAAAGTGAATGCTGACATAGAAAAGGTTAACCAGAATCAGGCCAAGAGATGC
ACAGTGATCGGTGGCTCTGGATTCCTGGGGCAGCACATGGTGGAGCAGTTGCTGGCAAGA
GGATATGCTGTCAATGTATTTGATATCCAGCAAGGGTTTGATAATCCCCAGGTGCGGTTC
TTTCTGGGTGACCTCTGCAGCCGACAGGATCTGTACCCAGCTCTGAAAGGTGTAAACACA
GTTTTCCACTGTGCGTCACCCCCACCATCCAGTAACAACAAGGAGCTCTTTTATAGAGTG
AATTACATTGGCACCAAGAATGTCATTGAAACTTGCAAAGAGGCTGGGGTTCAGAAACTC
ATTTTAACCAGCAGTGCCAGTGTCATCTTTGAGGGCGTCGATATCAAGAATGGAACTGAA
GACCTTCCCTATGCCATGAAACCCATTGACTACTACACAGAGACTAAGATCTTACAGGAG
AGGGCAGTTCTGGGCGCCAACGATCCTGAGAAGAATTTCTTAACCACAGCCATCCGCCCT
CATGGCATTTTCGGCCCAAGGGACCCGCAGTTGGTACCCATCCTCATCGAGGCAGCCAGG
AACGGCAAGATGAAGTTCGTGATTGGAAATGGGAAGAACTTGGTGGACTTCACCTTTGTG
GAGAACGTGGTCCATGGACACATCCTGGCGGCAGAGCAGCTCTCCCGAGACTCGACACTG
GGTGGGAAGGCATTTCACATCACCAATGATGAGCCCATCCCTTTCTGGACATTCCTGTCT
CGCATCCTGACAGGCCTCAATTATGAGGCCCCCAAGTACCACATCCCCTACTGGGTGGCC
TACTACCTGGCCCTCCTGCTATCCCTGCTGGTGATGGTGATCAGTCCTGTCATCCAGCTG
CAGCCCACCTTCACACCCATGCGGGTCGCACTGGCTGGCACATTCCACTACTACAGCTGC
GAGAGAGCCAAAAAGGCCATGGGCTACCAGCCACTAGTGACCATGGATGATGCTATGGAG
AGGACCGTGCAGAGCTTTCGCCACCTGCGGAGGGTCAAGTGA
Enzyme 24 GenBank Gene ID U47105 Link Image
Enzyme 24 GeneCard ID NSDHL Link Image
Enzyme 24 GenAtlas ID NSDHL Link Image
Enzyme 24 HGNC ID HGNC:13398 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Mallon AM, Platzer M, Bate R, Gloeckner G, Botcherby MR, Nordsiek G, Strivens MA, Kioschis P, Dangel A, Cunningham D, Straw RN, Weston P, Gilbert M, Fernando S, Goodall K, Hunter G, Greystrong JS, Clarke D, Kimberley C, Goerdes M, Blechschmidt K, Rump A, Hinzmann B, Mundy CR, Miller W, Poustka A, Herman GE, Rhodes M, Denny P, Rosenthal A, Brown SD: Comparative genome sequence analysis of the Bpa/Str region in mouse and Man. Genome Res. 2000 Jun;10(6):758-75. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Levin ML, Chatterjee A, Pragliola A, Worley KC, Wehnert M, Zhuchenko O, Smith RF, Lee CC, Herman GE: A comparative transcription map of the murine bare patches (Bpa) and striated (Str) critical regions and human Xq28. Genome Res. 1996 Jun;6(6):465-77. [PubMed Link Image]
  4. Konig A, Happle R, Bornholdt D, Engel H, Grzeschik KH: Mutations in the NSDHL gene, encoding a 3beta-hydroxysteroid dehydrogenase, cause CHILD syndrome. Am J Med Genet. 2000 Feb 14;90(4):339-46. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5497
Enzyme 25 Name Lanosterol 14-alpha demethylase
Enzyme 25 Synonyms
  1. LDM
  2. CYPLI
  3. Cytochrome P450 51A1
  4. Cytochrome P450-14DM
  5. Cytochrome P45014DM
  6. Cytochrome P450LI
  7. Sterol 14-alpha demethylase
Enzyme 25 Gene Name CYP51A1
Enzyme 25 Protein Sequence >Lanosterol 14-alpha demethylase 
MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKS
PPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNS
KNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETK
EYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWL
LPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDE
VAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDL
NLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLD
FNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFP
TVNYTTMIHTPENPVIRYKRRSK
Enzyme 25 Number of Residues 503
Enzyme 25 Molecular Weight 56805.3
Enzyme 25 Theoretical pI 8.72
Enzyme 25 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
—
Component
—
Enzyme 25 General Function Involved in monooxygenase activity
Enzyme 25 Specific Function Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions
  • obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 4 H2O [RN:R05731]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 24-44
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 4503243 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q16850 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name CP51A_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1530 bp 
ATGGCGGCGGCGGCTGGGATGCTGCTGCTGGGCTTGCTGCAGGCGGGTGGGTCGGTGCTG
GGCCAGGCGATGGAGAAGGTGACAGGCGGCAACCTCTTGTCCATGCTGCTGATCGCCTGC
GCCTTCACCCTCAGCCTGGTCTACCTGATCCGTCTGGCCGCCGGCCACCTGGTCCAGCTG
CCCGCAGGGGTGAAAAGTCCTCCATACATTTTCTCCCCAATTCCATTCCTTGGGCATGCC
ATAGCATTTGGGAAAAGTCCAATTGAATTTCTAGAAAATGCATATGAGAAGTATGGACCT
GTATTTAGTTTTACCATGGTAGGCAAGACATTTACTTACCTTCTGGGGAGTGATGCTGCT
GCACTGCTTTTTAATAGTAAAAATGAAGACCTGAATGCAGAAGATGTCTACAGTCGCCTG
ACAACACCTGTGTTTGGGAAGGGAGTTGCATACGATGTGCCTAATCCAGTTTTCTTGGAG
CAGAAGAAAATGTTAAAAAGTGGCCTTAACATAGCCCACTTTAAACAGCATGTTTCTATA
ATTGAAAAAGAAACAAAGGAATACTTTGAGAGTTGGGGAGAAAGTGGAGAAAAAAATGTG
TTTGAAGCTCTTTCTGAGCTCATAATTTTAACAGCTAGCCATTGTTTGCATGGAAAGGAA
ATCAGAAGTCAACTCAATGAAAAGGTAGCACAGCTGTATGCAGATTTGGATGGAGGTTTC
AGCCATGCAGCCTGGCTCTTACCAGGTTGGCTGCCTTTGCCTAGTTTCAGACGCAGGGAC
AGAGCTCATCGGGAAATCAAGGATATTTTCTATAAGGCAATCCAGAAACGCAGACAGTCT
CAAGAAAAAATTGATGACATTCTCCAAACTTTACTAGATGCTACATACAAGGATGGGCGT
CCTTTGACTGATGATGAAGTAGCAGGGATGCTTATTGGATTACTCTTGGCAGGGCAGCAT
ACATCCTCAACTACTAGTGCTTGGATGGGCTTCTTTTTGGCCAGAGACAAAACACTTCAA
AAAAAATGTTATTTAGAACAGAAAACAGTCTGTGGAGAGAATCTGCCTCCTTTAACTTAT
GACCAGCTCAAGGATCTAAATTTACTTGATCGCTGTATAAAAGAAACATTAAGACTTAGA
CCTCCTATAATGATCATGATGAGAATGGCCAGAACTCCTCAGACTGTGGCAGGGTATACC
ATTCCTCCAGGACATCAGGTGTGTGTTTCTCCCACTGTCAATCAAAGACTTAAAGACTCA
TGGGTAGAACGCCTGGACTTTAATCCTGATCGCTACTTACAGGATAACCCAGCATCAGGG
GAAAAGTTTGCCTATGTGCCATTTGGAGCTGGGCGTCATCGTTGTATTGGGGAAAATTTT
GCCTATGTTCAAATTAAGACAATTTGGTCCACTATGCTTCGTTTATATGAATTTGATCTC
ATTGATGGATACTTTCCCACTGTGAATTATACAACTATGATTCACACCCCTGAAAACCCA
GTTATCCGTTACAAACGAAGATCAAAATGA
Enzyme 25 GenBank Gene ID NM_000786 Link Image
Enzyme 25 GeneCard ID CYP51A1 Link Image
Enzyme 25 GenAtlas ID CYP51A1 Link Image
Enzyme 25 HGNC ID HGNC:2649 Link Image
Enzyme 25 Chromosome Location 7
Enzyme 25 Locus 7q21.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Stromstedt M, Rozman D, Waterman MR: The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch Biochem Biophys. 1996 May 1;329(1):73-81. [PubMed Link Image]
  2. Aoyama Y, Noshiro M, Gotoh O, Imaoka S, Funae Y, Kurosawa N, Horiuchi T, Yoshida Y: Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient and conserved P450 species. J Biochem. 1996 May;119(5):926-33. [PubMed Link Image]
  3. Rozman D, Stromstedt M, Waterman MR: The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family. Arch Biochem Biophys. 1996 Sep 15;333(2):466-74. [PubMed Link Image]
  4. Rozman D, Stromstedt M, Tsui LC, Scherer SW, Waterman MR: Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. Genomics. 1996 Dec 15;38(3):371-81. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  7. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5526
Enzyme 26 Name 4-trimethylaminobutyraldehyde dehydrogenase
Enzyme 26 Synonyms
  1. TMABADH
  2. Aldehyde dehydrogenase E3 isozyme
  3. Aldehyde dehydrogenase family 9 member A1
  4. Gamma-aminobutyraldehyde dehydrogenase
  5. R-aminobutyraldehyde dehydrogenase
Enzyme 26 Gene Name ALDH9A1
Enzyme 26 Protein Sequence >4-trimethylaminobutyraldehyde dehydrogenase 
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
Enzyme 26 Number of Residues 494
Enzyme 26 Molecular Weight 53801.5
Enzyme 26 Theoretical pI 5.61
Enzyme 26 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 26 General Function Involved in oxidoreductase activity
Enzyme 26 Specific Function Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction
Enzyme 26 Pathways
Enzyme 26 Reactions
  • 4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+ [RN:R03283]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 7248636 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P49189 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name AL9A1_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1485 bp 
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCCGCGTG
GAGCCGGCGGACGCCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATA
GCTACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCT
GCTTTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCT
GCCAGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGC
AAGTCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTAT
GCGGGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGT
TATACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTT
CAGATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAA
CCTTCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGT
GTACCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGT
CAGCATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATC
ATGGAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCA
CTCATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAAC
TTCCTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATT
CTTGATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCC
CTTCTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTT
GGGTTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATAT
GTACCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAAT
TGCAGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTA
TCATTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCA
GCTGGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCT
GGGACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATAT
AAGAAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTG
AAGACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
Enzyme 26 GenBank Gene ID AF172093 Link Image
Enzyme 26 GeneCard ID ALDH9A1 Link Image
Enzyme 26 GenAtlas ID ALDH9A1 Link Image
Enzyme 26 HGNC ID HGNC:412 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 1q23.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed Link Image]
  2. Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed Link Image]
  6. Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed Link Image]
  7. Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5528
Enzyme 27 Name Alpha-aminoadipic semialdehyde dehydrogenase
Enzyme 27 Synonyms
  1. Alpha-AASA dehydrogenase
  2. Aldehyde dehydrogenase family 7 member A1
  3. Antiquitin-1
  4. Betaine aldehyde dehydrogenase
  5. Delta1-piperideine-6-carboxylate dehydrogenase
  6. P6c dehydrogenase
Enzyme 27 Gene Name ALDH7A1
Enzyme 27 Protein Sequence >Alpha-aminoadipic semialdehyde dehydrogenase 
MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWG
GRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDA
LREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIE
QWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLED
NKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN
NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVG
NPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHD
ASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGI
VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
Enzyme 27 Number of Residues 539
Enzyme 27 Molecular Weight 58486.7
Enzyme 27 Theoretical pI 8.09
Enzyme 27 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 27 General Function Involved in oxidoreductase activity
Enzyme 27 Specific Function Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism
Enzyme 27 Pathways
Enzyme 27 Reactions
  • L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+ [RN:R03102 R03103]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 188035924 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P49419 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name AL7A1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1620 bp 
ATGTGGCGCCTTCCTCGCGCGCTGTGTGTGCACGCTGCAAAGACCAGCAAGCTCTCTGGA
CCTTGGAGCAGGCCTGCCGCCTTCATGTCCACTCTCCTCATCAATCAGCCCCAGTATGCG
TGGCTGAAAGAGCTGGGGCTCCGCGAGGAAAACGAGGGCGTGTATAATGGAAGCTGGGGA
GGCCGGGGAGAGGTTATTACGACCTATTGCCCTGCTAACAACGAGCCAATAGCAAGAGTC
CGACAGGCCAGTGTGGCAGACTATGAAGAAACTGTAAAGAAAGCAAGAGAAGCATGGAAA
ATCTGGGCAGATATTCCTGCTCCAAAACGAGGAGAAATAGTAAGACAGATTGGCGATGCC
TTGCGGGAGAAGATCCAAGTACTAGGAAGCTTGGTGTCTTTGGAGATGGGGAAAATCTTA
GTGGAAGGTGTGGGTGAAGTTCAGGAGTATGTGGATATCTGTGACTATGCTGTTGGTTTA
TCAAGGATGATTGGAGGACCTATCTTGCCTTCTGAAAGATCTGGCCATGCACTGATTGAG
CAGTGGAATCCCGTAGGCCTGGTTGGAATCATCACGGCATTCAATTTCCCTGTGGCAGTG
TATGGTTGGAACAACGCCATCGCCATGATCTGTGGAAATGTCTGCCTCTGGAAAGGAGCT
CCAACCACTTCCCTCATTAGTGTGGCTGTCACAAAGATAATAGCCAAGGTTCTGGAGGAC
AACAAGCTGCCTGGTGCAATTTGTTCCTTGACTTGTGGTGGAGCAGATATTGGCACAGCA
ATGGCCAAAGATGAACGAGTGAACCTGCTGTCCTTCACTGGGAGCACTCAGGTGGGAAAA
CAGGTGGGCCTGATGGTGCAGGAGAGGTTTGGGAGAAGTCTGTTGGAACTTGGAGGAAAC
AATGCCATTATTGCCTTTGAAGATGCAGACCTCAGCTTAGTTGTTCCATCAGCTCTCTTC
GCTGCTGTGGGAACAGCTGGCCAGAGGTGTACCACTGCGAGGCGACTGTTTATACATGAA
AGCATCCATGATGAGGTTGTAAACAGACTTAAAAAGGCCTATGCACAGATCCGAGTTGGG
AACCCATGGGACCCTAATGTTCTCTATGGGCCACTCCACACCAAGCAGGCAGTGAGCATG
TTTCTTGGAGCAGTGGAAGAAGCAAAGAAAGAAGGTGGCACAGTGGTCTATGGGGGCAAG
GTTATGGATCGCCCTGGAAATTATGTAGAACCGACAATTGTGACAGGTCTTGGCCACGAT
GCGTCCATTGCACACACAGAGACTTTTGCTCCGATTCTCTATGTCTTTAAATTCAAGAAT
GAAGAAGAGGTCTTTGCATGGAATAATGAAGTAAAACAGGGACTTTCAAGTAGCATCTTT
ACCAAAGATCTGGGCAGAATCTTTCGCTGGCTTGGACCTAAAGGATCAGACTGTGGCATT
GTAAATGTCAACATTCCAACAAGTGGGGCTGAGATTGGAGGTGCCTTTGGAGGAGAAAAG
CACACTGGTGGTGGCAGGGAGTCTGGCAGTGATGCCTGGAAACAGTACATGAGAAGGTCT
ACTTGTACTATCAACTACAGTAAAGACCTTCCTCTGGCCCAAGGAATCAAGTTTCAGTAA
Enzyme 27 GenBank Gene ID NM_001182.3 Link Image
Enzyme 27 GeneCard ID ALDH7A1 Link Image
Enzyme 27 GenAtlas ID ALDH7A1 Link Image
Enzyme 27 HGNC ID HGNC:877 Link Image
Enzyme 27 Chromosome Location 5
Enzyme 27 Locus 5q31
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Lee P, Kuhl W, Gelbart T, Kamimura T, West C, Beutler E: Homology between a human protein and a protein of the green garden pea. Genomics. 1994 May 15;21(2):371-8. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Skvorak AB, Robertson NG, Yin Y, Weremowicz S, Her H, Bieber FR, Beisel KW, Lynch ED, Beier DR, Morton CC: An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics. 1997 Dec 1;46(2):191-9. [PubMed Link Image]
  6. Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V: Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. J Biol Chem. 2010 Jun 11;285(24):18452-63. Epub 2010 Mar 5. [PubMed Link Image]
  7. Mills PB, Struys E, Jakobs C, Plecko B, Baxter P, Baumgartner M, Willemsen MA, Omran H, Tacke U, Uhlenberg B, Weschke B, Clayton PT: Mutations in antiquitin in individuals with pyridoxine-dependent seizures. Nat Med. 2006 Mar;12(3):307-9. Epub 2006 Feb 19. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5529
Enzyme 28 Name Aldehyde dehydrogenase family 1 member A3
Enzyme 28 Synonyms
  1. Aldehyde dehydrogenase 6
  2. Retinaldehyde dehydrogenase 3
  3. RALDH-3
  4. RalDH3
Enzyme 28 Gene Name ALDH1A3
Enzyme 28 Protein Sequence >Aldehyde dehydrogenase family 1 member A3 
MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
Enzyme 28 Number of Residues 512
Enzyme 28 Molecular Weight 56108.0
Enzyme 28 Theoretical pI 7.29
Enzyme 28 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 28 General Function Involved in oxidoreductase activity
Enzyme 28 Specific Function Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system
Enzyme 28 Pathways
Enzyme 28 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+ [RN:R00538 R00634]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 46621670 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P47895 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name AL1A3_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1539 bp 
ATGGCCACCGCTAACGGGGCCGTGGAAAACGGGCAGCCGGACAGGAAGCCGCCGGCCCTG
CCGCGCCCCATCCGCAACCTGGAGGTCAAGTTCACCAAGATATTTATCAACAATGAATGG
CACGAATCCAAGAGTGGGAAAAAGTTTGCTACATGTAACCCTTCAACTCGGGAGCAAATA
TGTGAAGTGGAAGAAGGAGATAAGCCCGACGTGGACAAGGCTGTGGAGGCTGCACAGGTT
GCCTTCCAGAGGGGCTCGCCATGGCGCCGGCTGGATGCCCTGAGTCGTGGGCGGCTGCTG
CACCAGCTGGCTGACCTGGTGGAGAGGGACCGCGCCACCTTGGCCGCCCTGGAGACGATG
GATACAGGGAAGCCATTTCTTCATGCTTTTTTCATCGACCTGGAGGGCTGTATTAGAACC
CTCAGATACTTTGCAGGGTGGGCAGACAAAATCCAGGGCAAGACCATCCCCACAGATGAC
AACGTCGTGTGCTTCACCAGGCATGAGCCCATTGGTGTCTGTGGGGCCATCACTCCATGG
AACTTCCCCCTGCTGATGCTGGTGTGGAAGCTGGCACCCGCCCTCTGCTGTGGGAACACC
ATGGTCCTGAAGCCTGCGGAGCAGACACCTCTCACCGCCCTTTATCTCGGCTCTCTGATC
AAAGAGGCCGGGTTCCCTCCAGGAGTGGTGAACATTGTGCCAGGATTCGGGCCCACAGTG
GGAGCAGCAATTTCTTCTCACCCTCAGATCAACAAGATCGCCTTCACCGGCTCCACAGAG
GTTGGAAAACTGGTTAAAGAAGCTGCGTCCCGGAGCAATCTGAAGCGGGTGACGCTGGAG
CTGGGGGGGAAGAACCCCTGCATCGTGTGTGCGGACGCTGACTTGGACTTGGCAGTGGAG
TGTGCCCATCAGGGAGTGTTCTTCAACCAAGGCCAGTGTTGCACGGCAGCCTCCAGGGTG
TTCGTGGAGGAGCAGGTCTACTCTGAGTTTGTCAGGCGGAGCGTGGAGTATGCCAAGAAA
CGGCCCGTGGGAGACCCCTTCGATGTCAAAACAGAACAGGGGCCTCAGATTGATCAAAAG
CAGTTCGACAAAATCTTAGAGCTGATCGAGAGTGGGAAGAAGGAAGGGGCCAAGCTGGAA
TGCGGGGGCTCAGCCATGGAAGACAAGGGGCTCTTCATCAAACCCACTGTCTTCTCAGAA
GTCACAGACAACATGCGGATTGCCAAAGAGGAGATTTTCGGGCCAGTGCAACCAATACTG
AAGTTCAAAAGTATCGAAGAAGTGATAAAAAGAGCGAATAGCACCGACTATGGACTCACA
GCAGCCGTGTTCACAAAAAATCTCGACAAAGCCCTGAAGTTGGCTTCTGCCTTAGAGTCT
GGAACGGTCTGGATCAACTGCTACAACGCCCTCTATGCACAGGCTCCATTTGGTGGCTTT
AAAATGTCAGGAAATGGCAGAGAACTAGGTGAATACGCTTTGGCCGAATACACAGAAGTG
AAAACTGTCACCATCAAACTTGGCGACAAGAACCCCTGA
Enzyme 28 GenBank Gene ID BC069274 Link Image
Enzyme 28 GeneCard ID ALDH1A3 Link Image
Enzyme 28 GenAtlas ID ALDH1A3 Link Image
Enzyme 28 HGNC ID HGNC:409 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 15q26.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Hsu LC, Chang WC, Hiraoka L, Hsieh CL: Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6. Genomics. 1994 Nov 15;24(2):333-41. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5530
Enzyme 29 Name Aldehyde dehydrogenase, mitochondrial
Enzyme 29 Synonyms
  1. ALDH class 2
  2. ALDH-E2
  3. ALDHI
Enzyme 29 Gene Name ALDH2
Enzyme 29 Protein Sequence >Aldehyde dehydrogenase, mitochondrial 
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Enzyme 29 Number of Residues 517
Enzyme 29 Molecular Weight 56380.9
Enzyme 29 Theoretical pI 7.05
Enzyme 29 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 29 General Function Involved in oxidoreductase activity
Enzyme 29 Specific Function An aldehyde + NAD(+) + H(2)O = an acid + NADH
Enzyme 29 Pathways
Enzyme 29 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 28606 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P05091 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Enzyme 29 PDB ID 1OF7 Link Image
Enzyme 29 PDB File Show
Enzyme 29 3D Structure
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1551 bp 
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
Enzyme 29 GenBank Gene ID X05409 Link Image
Enzyme 29 GeneCard ID ALDH2 Link Image
Enzyme 29 GenAtlas ID ALDH2 Link Image
Enzyme 29 HGNC ID HGNC:404 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 12q24.2
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed Link Image]
  2. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed Link Image]
  3. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed Link Image]
  6. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed Link Image]
  7. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed Link Image]
  8. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  9. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  10. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed Link Image]
  11. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed Link Image]
  12. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed Link Image]
  13. Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5531
Enzyme 30 Name Fatty aldehyde dehydrogenase
Enzyme 30 Synonyms
  1. Aldehyde dehydrogenase 10
  2. Aldehyde dehydrogenase family 3 member A2
  3. Microsomal aldehyde dehydrogenase
Enzyme 30 Gene Name ALDH3A2
Enzyme 30 Protein Sequence >Fatty aldehyde dehydrogenase 
MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQE
VITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQ
PLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDH
IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT
CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKI
AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLA
LYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS
HQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLV
KAEYY
Enzyme 30 Number of Residues 485
Enzyme 30 Molecular Weight 54847.4
Enzyme 30 Theoretical pI 7.99
Enzyme 30 GO Classification
Function
  • aldehyde dehydrogenase [NAD(P)+] activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • cellular aldehyde metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 30 General Function Involved in oxidoreductase activity
Enzyme 30 Specific Function Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length
Enzyme 30 Pathways
Enzyme 30 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 464-480
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID P51648 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name AL3A2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1458 bp 
ATGGAGCTCGAAGTCCGGCGGGTCCGACAGGCGTTCCTGTCCGGCCGGTCGCGACCTCTG
CGGTTTCGGCTGCAGCAGCTGGAGGCCCTGCGGAGGATGGTGCAGGAGCGCGAGAAGGAT
ATCCTGACGGCCATCGCCGCCGACCTGTGCAAGAGTGAATTCAATGTGTACAGTCAGGAA
GTCATTACTGTCCTTGGGGAAATTGATTTTATGCTTGAGAATCTTCCTGAATGGGTTACT
GCTAAACCAGTTAAGAAGAACGTGCTCACCATGCTGGATGAGGCCTATATTCAGCCACAG
CCTCTGGGAGTGGTGCTGATAATCGGAGCTTGGAATTACCCCTTCGTTCTCACCATTCAG
CCACTGATAGGAGCCATCGCTGCAGGAAATGCTGTGATTATAAAGCCTTCTGAACTGAGT
GAAAATACAGCCAAGATCTTGGCAAAGCTTCTCCCTCAGTATTTAGACCAGGATCTCTAT
ATTGTTATTAATGGTGGTGTTGAGGAAACCACGGAGCTCCTGAAGCAGCGATTTGACCAC
ATTTTCTATACGGGAAACACTGCGGTTGGCAAAATTGTCATGGAAGCTGCTGCCAAGCAT
CTGACCCCTGTGACTCTTGAACTGGGAGGGAAAAGTCCATGTTATATTGATAAAGATTGT
GACCTGGACATTGTTTGCAGACGCATAACCTGGGGAAAATACATGAATTGTGGCCAAACC
TGCATTGCACCCGACTATATTCTCTGTGAAGCATCCCTCCAAAATCAAATTGTATGGAAG
ATTAAGGAAACAGTGAAGGAATTTTATGGAGAAAATATAAAAGAGTCTCCTGATTATGAA
AGGATCATCAATCTTCGTCATTTTAAGAGGATACTAAGTTTGCTTGAAGGACAAAAGATA
GCTTTTGGTGGGGAGACTGATGAGGCCACACGCTACATAGCCCCAACAGTACTTACCGAT
GTTGATCCTAAAACCAAGGTGATGCAAGAAGAAATTTTTGGACCAATTCTTCCAATAGTG
CCTGTGAAAAATGTAGATGAGGCCATAAATTTCATAAATGAACGTGAAAAGCCTCTGGCT
CTTTATGTATTTTCGCATAACCATAAGCTCATCAAACGGATGATTGATGAGACATCCAGT
GGAGGTGTCACAGGCAATGACGTCATTATGCACTTCACGCTCAACTCTTTCCCATTTGGA
GGAGTGGGTTCCAGTGGGATGGGAGCTTATCACGGAAAACATAGTTTTGATACTTTTTCT
CATCAGCGTCCCTGTTTATTAAAAAGTTTAAAGAGAGAAGGTGCTAACAAACTCAGATAT
CCTCCCAACAGCCAGTCAAAGGTGGATTGGGGGAAATTTTTTCTCTTGAAACGGTTCAAC
AAAGAAAAACTCGGTCTCCTGTTGCTCACTTTCCTGGGTATTGTAGCCGCTGTGCTTGTC
AAGGCAGAATATTACTGA
Enzyme 30 GenBank Gene ID L47162 Link Image
Enzyme 30 GeneCard ID ALDH3A2 Link Image
Enzyme 30 GenAtlas ID ALDH3A2 Link Image
Enzyme 30 HGNC ID HGNC:403 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 17p11.2
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. De Laurenzi V, Rogers GR, Hamrock DJ, Marekov LN, Steinert PM, Compton JG, Markova N, Rizzo WB: Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. Nat Genet. 1996 Jan;12(1):52-7. [PubMed Link Image]
  2. Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG: Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Genomics. 1997 Jan 15;39(2):127-35. [PubMed Link Image]
  3. Chang C, Yoshida A: Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression. Genomics. 1997 Feb 15;40(1):80-5. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Sillen A, Jagell S, Wadelius C: A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden. Hum Genet. 1997 Aug;100(2):201-3. [PubMed Link Image]
  6. Sillen A, Anton-Lamprecht I, Braun-Quentin C, Kraus CS, Sayli BS, Ayuso C, Jagell S, Kuster W, Wadelius C: Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome. Hum Mutat. 1998;12(6):377-84. [PubMed Link Image]
  7. Rizzo WB, Carney G, Lin Z: The molecular basis of Sjogren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene. Am J Hum Genet. 1999 Dec;65(6):1547-60. [PubMed Link Image]
  8. Aoki N, Suzuki H, Ito K, Ito M: A novel point mutation of the FALDH gene in a Japanese family with Sjogren-Larsson syndrome. J Invest Dermatol. 2000 May;114(5):1065-6. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5532
Enzyme 31 Name Aldehyde dehydrogenase X, mitochondrial
Enzyme 31 Synonyms
  1. Aldehyde dehydrogenase 5
  2. Aldehyde dehydrogenase family 1 member B1
Enzyme 31 Gene Name ALDH1B1
Enzyme 31 Protein Sequence >Aldehyde dehydrogenase X, mitochondrial 
MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
Enzyme 31 Number of Residues 517
Enzyme 31 Molecular Weight 57238.0
Enzyme 31 Theoretical pI 6.79
Enzyme 31 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 31 General Function Involved in oxidoreductase activity
Enzyme 31 Specific Function ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation
Enzyme 31 Pathways
Enzyme 31 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID P30837 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name AL1B1_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1554 bp 
ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCGCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGGATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAG
Enzyme 31 GenBank Gene ID BT007418 Link Image
Enzyme 31 GeneCard ID ALDH1B1 Link Image
Enzyme 31 GenAtlas ID ALDH1B1 Link Image
Enzyme 31 HGNC ID HGNC:407 Link Image
Enzyme 31 Chromosome Location 9
Enzyme 31 Locus 9p11.1
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5538
Enzyme 32 Name Pyrroline-5-carboxylate reductase 1, mitochondrial
Enzyme 32 Synonyms
  1. P5C reductase 1
  2. P5CR 1
Enzyme 32 Gene Name PYCR1
Enzyme 32 Protein Sequence >Pyrroline-5-carboxylate reductase 1, mitochondrial 
MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETV
QHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPAPRVIRC
MTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH
ALHVLESGGFRSLLINAVEASCIRTRELQSMADQEQVSPAAIKKTILDKVKLDSPAGTAL
SPSGHTKLLPRSLAPAGKD
Enzyme 32 Number of Residues 319
Enzyme 32 Molecular Weight 33360.3
Enzyme 32 Theoretical pI 7.69
Enzyme 32 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
  • pyrroline-5-carboxylate reductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline biosynthetic process
  • proline metabolic process
Component
—
Enzyme 32 General Function Involved in oxidoreductase activity
Enzyme 32 Specific Function Involved in the cellular response to oxidative stress
Enzyme 32 Pathways
Enzyme 32 Reactions
  • L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+ [RN:R01248 R01251]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 16306658 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P32322 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name P5CR1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >960 bp 
ATGAGCGTGGGCTTCATCGGCGCTGGCCAGCTGGCTTTTGCCCTGGCCAAGGGCTTCACA
GCAGCAGGCGTCTTGGCTGCCCACAAGATAATGGCTAGCTCCCCAGACATGGACCTGGCC
ACAGTTTCTGCTCTCAGGAAGATGGGGGTGAAGTTGACACCCCACAACAAGGAGACGGTG
CAGCACAGTGATGTGCTCTTCCTGGCTGTGAAGCCACACATCATCCCCTTCATCCTGGAT
GAAATAGGCGCCGACATTGAGGACAGACACATTGTGGTGTCCTGCGCGGCCGGCGTCACC
ATCAGCTCCATTGAGAAGAAGCTGTCAGCGTTTCGGCCAGCCCCCAGGGTCATCCGCTGC
ATGACCAACACTCCAGTCGTGGTGCGGGAGGGGGCCACCGTGTATGCCACAGGCACGCAC
GCCCAGGTGGAGGACGGGAGGCTCATGGAGCAGCTGCTGAGCAGCGTGGGCTTCTGCACG
GAGGTGGAAGAGGACCTGATTGATGCCGTCACGGGGCTCAGTGGCAGCGGCCCCGCCTAC
GCATTCACAGCCCTGGATGCCCTGGCTGATGGGGGCGTGAAGATGGGACTTCCAAGGCGC
CTGGCAGTCCGCCTCGGGGCCCAGGCCCTCCTGGGGGCTGCCAAGATGCTGCTGCACTCA
GAACAGCACCCAGGCCAGCTCAAGGACAACGTCAGCTCTCCTGGTGGGGCCACCATCCAT
GCCTTGCATGTGCTGGAGAGTGGGGGCTTCCGCTCCCTGCTCATCAACGCTGTGGAGGCC
TCCTGCATCCGCACACGGGAGCTGCAGTCCATGGCTGACCAGGAGCAGGTGTCACCAGCC
GCCATCAAGAAGACCATCCTGGACAAGGTGAAGCTGGACTCCCCTGCAGGGACCGCTCTG
TCGCCTTCTGGCCACACCAAGCTGCTCCCCCGCAGCCTGGCCCCAGCGGGCAAGGATTGA
Enzyme 32 GenBank Gene ID BC001504 Link Image
Enzyme 32 GeneCard ID PYCR1 Link Image
Enzyme 32 GenAtlas ID PYCR1 Link Image
Enzyme 32 HGNC ID HGNC:9721 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 17q25.3
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Dougherty KM, Brandriss MC, Valle D: Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae. J Biol Chem. 1992 Jan 15;267(2):871-5. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Reversade B, Escande-Beillard N, Dimopoulou A, Fischer B, Chng SC, Li Y, Shboul M, Tham PY, Kayserili H, Al-Gazali L, Shahwan M, Brancati F, Lee H, O'Connor BD, Schmidt-von Kegler M, Merriman B, Nelson SF, Masri A, Alkazaleh F, Guerra D, Ferrari P, Nanda A, Rajab A, Markie D, Gray M, Nelson J, Grix A, Sommer A, Savarirayan R, Janecke AR, Steichen E, Sillence D, Hausser I, Budde B, Nurnberg G, Nurnberg P, Seemann P, Kunkel D, Zambruno G, Dallapiccola B, Schuelke M, Robertson S, Hamamy H, Wollnik B, Van Maldergem L, Mundlos S, Kornak U: Mutations in PYCR1 cause cutis laxa with progeroid features. Nat Genet. 2009 Sep;41(9):1016-21. Epub 2009 Aug 2. [PubMed Link Image]
  4. Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z: Crystal structure of human pyrroline-5-carboxylate reductase. J Mol Biol. 2006 Jun 23;359(5):1364-77. Epub 2006 May 11. [PubMed Link Image]
  5. Guernsey DL, Jiang H, Evans SC, Ferguson M, Matsuoka M, Nightingale M, Rideout AL, Provost S, Bedard K, Orr A, Dube MP, Ludman M, Samuels ME: Mutation in pyrroline-5-carboxylate reductase 1 gene in families with cutis laxa type 2. Am J Hum Genet. 2009 Jul;85(1):120-9. Epub 2009 Jul 2. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5540
Enzyme 33 Name Pyrroline-5-carboxylate reductase 2
Enzyme 33 Synonyms
  1. P5C reductase 2
  2. P5CR 2
Enzyme 33 Gene Name PYCR2
Enzyme 33 Protein Sequence >Pyrroline-5-carboxylate reductase 2 
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
Enzyme 33 Number of Residues 320
Enzyme 33 Molecular Weight 33636.8
Enzyme 33 Theoretical pI 7.87
Enzyme 33 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
  • pyrroline-5-carboxylate reductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline biosynthetic process
  • proline metabolic process
Component
—
Enzyme 33 General Function Involved in oxidoreductase activity
Enzyme 33 Specific Function L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H
Enzyme 33 Pathways
Enzyme 33 Reactions
  • L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+ [RN:R01248 R01251]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 33150582 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q96C36 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name P5CR2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >963 bp 
ATGAGCGTGGGCTTCATCGGGGCCGGCCAGCTGGCTAATGCTCTGGCGCGGGGCTTCACG
GCCGCAGCATTCCTGTCGGCTCACAAGATAATAGCCAGCTCCCCAGAAATGAACCTGCCC
ACGGTGTCCGCGCTCAGGAAGATGGGTGTGAACCTGACACGCAGCAACAAGGAGACGGTG
AAGCACAGCGACGTCCTGTTTCTGGCTGTGAAGCACATTATCATCCCCTTCATCCTGGAT
GAGATTGGGGCCGACGTGCAAGCCAGACACATCGTGGTCTCCTGTGCGGCTGGTGTCACC
ATCAGCTCTGTGGAGAAGAAGCTGATGGCATTCCAGCCAGCCCCCAAAGTGATTCGCTGC
ATGACCAACACACCTGTGGTAGTGCAGGAAGGCGCTACAGTGTACGCCACGGGCACCCAT
GCCCTGGTGGAGGATGGGCAGCTCCTGGAGCAGCTCATGAGCAGCGTGGGCTTCTGCACT
GAGGTGGAAGAGGACCTCATCGATGCCGTCACGGGGCTCAGTGGCAGCGGGCCTGCCTAT
GCATTCATGGCTCTGGACGCATTGGCTGATGGTGGGGTGAAGATGGGTTTGCCACGGCGC
CTGGCAATCCAACTCGGGGCCCAGGCTTTGCTGGGAGCTGCCAAGATGCTGCTGGACTCG
GAGCAGCATCCATGCCAGCTTAAGGACAATGTCTGCTCCCCTGGGGGAGCCACCATCCAC
GCCCTGCACTTTCTAGAGAGTGGGGGCTTCCGCTCTCTGCTCATCAATGCAGTTGAGGCC
TCCTGTATCCGAACACGAGAGCTACAGTCCATGGCCGACCAAGAAAAGATCTCCCCAGCT
GCCCTTAAGAAGACCCTCTTAGACAGAGTGAAGCTGGAATCCCCCACAGTCTCCACACTG
ACCCCCTCCAGCCCAGGGAAGCTCCTCACAAGAAGCCTGGCCCTGGGAGGCAAGAAGGAC
TAA
Enzyme 33 GenBank Gene ID AF087859 Link Image
Enzyme 33 GeneCard ID PYCR2 Link Image
Enzyme 33 GenAtlas ID PYCR2 Link Image
Enzyme 33 HGNC ID HGNC:30262 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 1q42.12
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5541
Enzyme 34 Name L-xylulose reductase
Enzyme 34 Synonyms
  1. XR
  2. Carbonyl reductase II
  3. Dicarbonyl/L-xylulose reductase
  4. Kidney dicarbonyl reductase
  5. kiDCR
  6. Sperm surface protein P34H
Enzyme 34 Gene Name DCXR
Enzyme 34 Protein Sequence >L-xylulose reductase 
MELFLAGRRVLVTGAGKGIGRGTVQALHATGARVVAVSRTQADLDSLVRECPGIEPVCVD
LGDWEATERALGSVGPVDLLVNNAAVALLQPFLEVTKEAFDRSFEVNLRAVIQVSQIVAR
GLIARGVPGAIVNVSSQCSQRAVTNHSVYCSTKGALDMLTKVMALELGPHKIRVNAVNPT
VVMTSMGQATWSDPHKAKTMLNRIPLGKFAEVEHVVNAILFLLSDRSGMTTGSTLPVEGG
FWAC
Enzyme 34 Number of Residues 244
Enzyme 34 Molecular Weight 25912.9
Enzyme 34 Theoretical pI 8.23
Enzyme 34 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 34 General Function Involved in oxidoreductase activity
Enzyme 34 Specific Function Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L- xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions
  • xylitol + NADP+ = L-xylulose + NADPH + H+ [RN:R01904]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID Q7Z4W1 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name DCXR_HUMAN Link Image
Enzyme 34 PDB ID 1PR9 Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >735 bp 
ATGGAGCTGTTCCTCGCGGGCCGCCGGGTGCTGGTCACCGGGGCAGGCAAAGGTATAGGG
CGCGGCACGGTCCAGGCGCTGCACGCGACGGGCGCGCGGGTGGTGGCTGTGAGCCGGACT
CAGGCGGATCTTGACAGCCTTGTCCGCGAGTGCCCGGGGATAGAACCCGTGTGCGTGGAC
CTGGGTGACTGGGAGGCCACCGAGCGGGCGCTGGGCAGCGTGGGCCCCGTGGACCTGCTG
GTGAACAACGCCGCTGTCGCCCTGCTGCAGCCCTTCCTGGAGGTCACCAAGGAGGCCTTT
GACAGATCCTTTGAGGTGAACCTGCGTGCGGTCATCCAGGTGTCGCAGATTGTGGCCAGG
GGCTTAATAGCCCGGGGAGTCCCAGGGGCCATCGTGAATGTCTCCAGCCAGTGCTCCCAG
CGGGCAGTAACTAACCATAGCGTCTACTGCTCCACCAAGGGTGCCCTGGACATGCTGACC
AAGGTGATGGCCCTAGAGCTCGGGCCCCACAAGATCCGAGTGAATGCAGTAAACCCCACA
GTGGTGATGACGTCCATGGGCCAGGCCACCTGGAGTGACCCCCACAAGGCCAAGACTATG
CTGAACCGAATCCCACTTGGCAAGTTTGCTGAGGTAGAGCACGTGGTGAACGCCATCCTC
TTTCTGCTGAGTGACCGAAGTGGCATGACCACGGGTTCCACTTTGCCGGTGGAAGGGGGC
TTCTGGGCCTGCTGA
Enzyme 34 GenBank Gene ID AB013846 Link Image
Enzyme 34 GeneCard ID DCXR Link Image
Enzyme 34 GenAtlas ID DCXR Link Image
Enzyme 34 HGNC ID HGNC:18985 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 17q25.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Legare C, Gaudreault C, St-Jacques S, Sullivan R: P34H sperm protein is preferentially expressed by the human corpus epididymidis. Endocrinology. 1999 Jul;140(7):3318-27. [PubMed Link Image]
  2. Nakagawa J, Ishikura S, Asami J, Isaji T, Usami N, Hara A, Sakurai T, Tsuritani K, Oda K, Takahashi M, Yoshimoto M, Otsuka N, Kitamura K: Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney. J Biol Chem. 2002 May 17;277(20):17883-91. Epub 2002 Mar 6. [PubMed Link Image]
  3. Xia XY, Xu XF, Gao Y, Huang YF: [Molecular cloning of human sperm surface protein P34H gene and semi-quantitative analysis of its expression in testis and epididymidis] Zhonghua Nan Ke Xue. 2003 Feb;9(1):24-7. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  7. El-Kabbani O, Chung RP, Ishikura S, Usami N, Nakagawa J, Hara A: Crystallization and preliminary crystallographic analysis of human L-xylulose reductase. Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1379-80. Epub 2002 Jul 20. [PubMed Link Image]
  8. El-Kabbani O, Ishikura S, Darmanin C, Carbone V, Chung RP, Usami N, Hara A: Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis. Proteins. 2004 May 15;55(3):724-32. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5564
Enzyme 35 Name Glucose-6-phosphate 1-dehydrogenase
Enzyme 35 Synonyms
  1. G6PD
Enzyme 35 Gene Name G6PD
Enzyme 35 Protein Sequence >Glucose-6-phosphate 1-dehydrogenase 
MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGL
LPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQR
LNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSS
DRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEP
FGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQA
NNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGK
ALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESEL
DLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPI
PYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
Enzyme 35 Number of Residues 515
Enzyme 35 Molecular Weight 59256.3
Enzyme 35 Theoretical pI 6.84
Enzyme 35 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • glucose-6-phosphate dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • small molecule metabolic process
Component
—
Enzyme 35 General Function Involved in glucose-6-phosphate dehydrogenase activity
Enzyme 35 Specific Function Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power
Enzyme 35 Pathways
Enzyme 35 Reactions
  • D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+ [RN:R00835]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 31543 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P11413 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name G6PD_HUMAN Link Image
Enzyme 35 PDB ID 1QKI Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1548 bp 
ATGGCAGAGCAGGTGGCCCTGAGCCGGACCCACGTGTGCGGGATCCTGCGGGAAGAGCTT
TTCCAGGGCGATGCCTTCCATCAGTCGGATACACACATATTCATCATCATGGGTGCATCG
GGTGACCTGGCCAAGAAGAAGATCTACCCCACCATCTGGTGGCTGTTCCGGGATGGCCTT
CTGCCCGAAAACACCTTCATCGTGGGCTATGCCCGTTCCCGCCTCACAGTGGCTGACATC
CGCAAACAGAGTGAGCCCTTCTTCAAGGCCACCCCAGAGGAGAAGCTCAAGCTGGAGGAC
TTCTTTGCCCGCAACTCCTATGTGGCTGGCCAGTACGATGATGCAGCCTCCTACCAGCGC
CTCAACAGCCACATGAATGCCCTCCACCTGGGGTCACAGGCCAACCGCCTCTTCTACCTG
GCCTTGCCCCCGACCGTCTACGAGGCCGTCACCAAGAACATTCACGAGTCCTGCATGAGC
CAGATAGGCTGGAACCGCATCATCGTGGAGAAGCCCTTCGGGAGGGACCTGCAGAGCTCT
GACCGGCTGTCCAACCACATCTCCTCCCTGTTCCGTGAGGACCAGATCTACCGCATCGAC
CACTACCTGGGCAAGGAGATGGTGCAGAACCTCATGGTGCTGAGATTTGCCAACAGGATC
TTCGGCCCCATCTGGAACCGGGACAACATCGCCTGCGTTATCCTCACCTTCAAGGAGCCC
TTTGGCACTGAGGGTCGCGGGGGCTATTTCGATGAATTTGGGATCATCCGGGACGTGATG
CAGAACCACCTACTGCAGATGCTGTGTCTGGTGGCCATGGAGAAGCCCGCCTCCACCAAC
TCAGATGACGTCCGTGATGAGAAGGTCAAGGTGTTGAAATGCATCTCAGAGGTGCAGGCC
AACAATGTGGTCCTGGGCCAGTACGTGGGGAACCCCGATGGAGAGGGCGAGGCCACCAAA
GGGTACCTGGACGACCCCACGGTGCCCCGCGGGTCCACCACCGCCACTTTTGCAGCCGTC
GTCCTCTATGTGGAGAATGAGAGGTGGGATGGGGTGCCCTTCATCCTGCGCTGCGGCAAG
GCCCTGAACGAGCGCAAGGCCGAGGTGAGGCTGCAGTTCCATGATGTGGCCGGCGACATC
TTCCACCAGCAGTGCAAGCGCAACGAGCTGGTGATCCGCGTGCAGCCCAACGAGGCCGTG
TACACCAAGATGATGACCAAGAAGCCGGGCATGTTCTTCAACCCCGAGGAGTCGGAGCTG
GACCTGACCTACGGCAACAGATACAAGAACGTGAAGCTCCCTGACGCCTACGAGCGCCTC
ATCCTGGACGTCTTCTGCGGGAGCCAGATGCACTTCGTGCGCAGCGACGAGCTCCGTGAG
GCCTGGCGTATTTTCACCCCACTGCTGCACCAGATTGAGCTGGAGAAGCCCAAGCCCATC
CCCTATATTTATGGCAGCCGAGGCCCCACGGAGGCAGACGAGCTGATGAAGAGAGTGGGT
TTCCAGTATGAGGGCACCTACAAGTGGGTGAACCCCCACAAGCTCTGA
Enzyme 35 GenBank Gene ID X03674 Link Image
Enzyme 35 GeneCard ID G6PD Link Image
Enzyme 35 GenAtlas ID G6PD Link Image
Enzyme 35 HGNC ID HGNC:4057 Link Image
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Persico MG, Viglietto G, Martini G, Toniolo D, Paonessa G, Moscatelli C, Dono R, Vulliamy T, Luzzatto L, D'Urso M: Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones: primary structure of the protein and unusual 5' non-coding region. Nucleic Acids Res. 1986 Mar 25;14(6):2511-22. [PubMed Link Image]
  2. Martini G, Toniolo D, Vulliamy T, Luzzatto L, Dono R, Viglietto G, Paonessa G, D'Urso M, Persico MG: Structural analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase. EMBO J. 1986 Aug;5(8):1849-55. [PubMed Link Image]
  3. Hirono A, Beutler E: Molecular cloning and nucleotide sequence of cDNA for human glucose-6-phosphate dehydrogenase variant A(-). Proc Natl Acad Sci U S A. 1988 Jun;85(11):3951-4. [PubMed Link Image]
  4. Chen EY, Cheng A, Lee A, Kuang WJ, Hillier L, Green P, Schlessinger D, Ciccodicola A, D'Urso M: Sequence of human glucose-6-phosphate dehydrogenase cloned in plasmids and a yeast artificial chromosome. Genomics. 1991 Jul;10(3):792-800. [PubMed Link Image]
  5. Chen EY, Zollo M, Mazzarella R, Ciccodicola A, Chen CN, Zuo L, Heiner C, Burough F, Repetto M, Schlessinger D, D'Urso M: Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci. Hum Mol Genet. 1996 May;5(5):659-68. [PubMed Link Image]
  6. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. [PubMed Link Image]
  9. Kanno H, Kondoh T, Yoshida A: 5' structure and expression of human glucose-6-phosphate dehydrogenase mRNA. DNA Cell Biol. 1993 Apr;12(3):209-15. [PubMed Link Image]
  10. Toniolo D, Filippi M, Dono R, Lettieri T, Martini G: The CpG island in the 5' region of the G6PD gene of man and mouse. Gene. 1991 Jun 30;102(2):197-203. [PubMed Link Image]
  11. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  12. Chao LT, Du CS, Louie E, Zuo L, Chen E, Lubin B, Chiu DT: A to G substitution identified in exon 2 of the G6PD gene among G6PD deficient Chinese. Nucleic Acids Res. 1991 Nov 11;19(21):6056. [PubMed Link Image]
  13. Saunders MA, Hammer MF, Nachman MW: Nucleotide variability at G6pd and the signature of malarial selection in humans. Genetics. 2002 Dec;162(4):1849-61. [PubMed Link Image]
  14. Takizawa T, Huang IY, Ikuta T, Yoshida A: Human glucose-6-phosphate dehydrogenase: primary structure and cDNA cloning. Proc Natl Acad Sci U S A. 1986 Jun;83(12):4157-61. [PubMed Link Image]
  15. Camardella L, Caruso C, Rutigliano B, Romano M, Di Prisco G, Descalzi-Cancedda F: Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate. Eur J Biochem. 1988 Feb 1;171(3):485-9. [PubMed Link Image]
  16. Descalzi-Cancedda F, Caruso C, Romano M, di Prisco G, Camardella L: Amino acid sequence of the carboxy-terminal end of human erythrocyte glucose-6-phosphate dehydrogenase. Biochem Biophys Res Commun. 1984 Jan 13;118(1):332-8. [PubMed Link Image]
  17. Hirono A, Beutler E: Alternative splicing of human glucose-6-phosphate dehydrogenase messenger RNA in different tissues. J Clin Invest. 1989 Jan;83(1):343-6. [PubMed Link Image]
  18. Camardella L, Damonte G, Carratore V, Benatti U, Tonetti M, Moneti G: Glucose 6-phosphate dehydrogenase from human erythrocytes: identification of N-acetyl-alanine at the N-terminus of the mature protein. Biochem Biophys Res Commun. 1995 Feb 6;207(1):331-8. [PubMed Link Image]
  19. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  20. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  21. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  22. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  23. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  24. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  25. Au SW, Gover S, Lam VM, Adams MJ: Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency. Structure. 2000 Mar 15;8(3):293-303. [PubMed Link Image]
  26. Vulliamy T, Beutler E, Luzzatto L: Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene. Hum Mutat. 1993;2(3):159-67. [PubMed Link Image]
  27. Kwok CJ, Martin AC, Au SW, Lam VM: G6PDdb, an integrated database of glucose-6-phosphate dehydrogenase (G6PD) mutations. Hum Mutat. 2002 Mar;19(3):217-24. [PubMed Link Image]
  28. Takizawa T, Yoneyama Y, Miwa S, Yoshida A: A single nucleotide base transition is the basis of the common human glucose-6-phosphate dehydrogenase variant A (+). Genomics. 1987 Nov;1(3):228-31. [PubMed Link Image]
  29. Vulliamy TJ, D'Urso M, Battistuzzi G, Estrada M, Foulkes NS, Martini G, Calabro V, Poggi V, Giordano R, Town M, et al.: Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia. Proc Natl Acad Sci U S A. 1988 Jul;85(14):5171-5. [PubMed Link Image]
  30. De Vita G, Alcalay M, Sampietro M, Cappelini MD, Fiorelli G, Toniolo D: Two point mutations are responsible for G6PD polymorphism in Sardinia. Am J Hum Genet. 1989 Feb;44(2):233-40. [PubMed Link Image]
  31. Beutler E, Westwood B, Prchal JT, Vaca G, Bartsocas CS, Baronciani L: New glucose-6-phosphate dehydrogenase mutations from various ethnic groups. Blood. 1992 Jul 1;80(1):255-6. [PubMed Link Image]
  32. Filosa S, Calabro V, Vallone D, Poggi V, Mason P, Pagnini D, Alfinito F, Rotoli B, Martini G, Luzzatto L, et al.: Molecular basis of chronic non-spherocytic haemolytic anaemia: a new G6PD variant (393 Arg----His) with abnormal KmG6P and marked in vivo instability. Br J Haematol. 1992 Jan;80(1):111-6. [PubMed Link Image]
  33. Perng LI, Chiou SS, Liu TC, Chang JG: A novel C to T substitution at nucleotide 1360 of cDNA which abolishes a natural Hha I site accounts for a new G6PD deficiency gene in Chinese. Hum Mol Genet. 1992 Jun;1(3):205. [PubMed Link Image]
  34. Ahluwalia A, Corcoran CM, Vulliamy TJ, Ishwad CS, Naidu JM, Argusti A, Stevens DJ, Mason PJ, Luzzatto L: G6PD Kalyan and G6PD Kerala; two deficient variants in India caused by the same 317 Glu-->Lys mutation. Hum Mol Genet. 1992 Jun;1(3):209-10. [PubMed Link Image]
  35. Nafa K, Reghis A, Osmani N, Baghli L, Benabadji M, Kaplan JC, Vulliamy TJ, Luzzatto L: G6PD Aures: a new mutation (48 Ile-->Thr) causing mild G6PD deficiency is associated with favism. Hum Mol Genet. 1993 Jan;2(1):81-2. [PubMed Link Image]
  36. Hirono A, Miwa S, Fujii H, Ishida F, Yamada K, Kubota K: Molecular study of eight Japanese cases of glucose-6-phosphate dehydrogenase deficiency by nonradioisotopic single-strand conformation polymorphism analysis. Blood. 1994 Jun 1;83(11):3363-8. [PubMed Link Image]
  37. Filosa S, Cai W, Galanello R, Cao A, de Mattia D, Schettini F, Martini G: A novel single-base mutation in the glucose 6-phosphate dehydrogenase gene is associated with chronic non-spherocytic haemolytic anaemia. Hum Genet. 1994 Nov;94(5):560-2. [PubMed Link Image]
  38. Ganczakowski M, Town M, Bowden DK, Vulliamy TJ, Kaneko A, Clegg JB, Weatherall DJ, Luzzatto L: Multiple glucose 6-phosphate dehydrogenase-deficient variants correlate with malaria endemicity in the Vanuatu archipelago (southwestern Pacific). Am J Hum Genet. 1995 Jan;56(1):294-301. [PubMed Link Image]
  39. Kaeda JS, Chhotray GP, Ranjit MR, Bautista JM, Reddy PH, Stevens D, Naidu JM, Britt RP, Vulliamy TJ, Luzzatto L, et al.: A new glucose-6-phosphate dehydrogenase variant, G6PD Orissa (44 Ala-->Gly), is the major polymorphic variant in tribal populations in India. Am J Hum Genet. 1995 Dec;57(6):1335-41. [PubMed Link Image]
  40. Mason PJ, Sonati MF, MacDonald D, Lanza C, Busutil D, Town M, Corcoran CM, Kaeda JS, Stevens DJ, al-Ismail S, et al.: New glucose-6-phosphate dehydrogenase mutations associated with chronic anemia. Blood. 1995 Mar 1;85(5):1377-80. [PubMed Link Image]
  41. Vlachos A, Westwood B, Lipton JM, Beutler E: G6PD Mount Sinai: a new severe hemolytic variant characterized by dual mutations at nucleotides 376G and 1159T (N126D). Hum Mutat. 1998;Suppl 1:S154-5. [PubMed Link Image]
  42. Galanello R, Loi D, Sollaino C, Dessi S, Cao A, Melis MA: A new glucose 6 phosphate dehydrogenase variant G6PD Sinnai (34 G-->T). Mutations in brief no. 156. Online. Hum Mutat. 1998;12(1):72-3. [PubMed Link Image]
  43. Iancovici-Kidon M, Sthoeger D, Abrahamov A, Wolach B, Beutler E, Gelbart T, Barak Y: A new exon 9 glucose-6-phosphate dehydrogenase mutation (G6PD "Rehovot") in a Jewish Ethiopian family with variable phenotypes. Blood Cells Mol Dis. 2000 Dec;26(6):567-71. [PubMed Link Image]
  44. Louicharoen C, Patin E, Paul R, Nuchprayoon I, Witoonpanich B, Peerapittayamongkol C, Casademont I, Sura T, Laird NM, Singhasivanon P, Quintana-Murci L, Sakuntabhai A: Positively selected G6PD-Mahidol mutation reduces Plasmodium vivax density in Southeast Asians. Science. 2009 Dec 11;326(5959):1546-9. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5565
Enzyme 36 Name GDH/6PGL endoplasmic bifunctional protein
Enzyme 36 Synonyms
  1. Glucose 1-dehydrogenase
  2. Hexose-6-phosphate dehydrogenase
  3. 6-phosphogluconolactonase
  4. 6PGL
Enzyme 36 Gene Name H6PD
Enzyme 36 Protein Sequence >GDH/6PGL endoplasmic bifunctional protein 
MWNMLIVAMCLALLGCLQAQELQGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGRGHSF
SFHGAALTAPKQGQELMAKALESLSCPKDMAPSHCAEHKDQFLQLSQYRQLKTAEDYQAL
NKDIEAQLQHAGLREAGRIFYFSVPPFAYEDIARNINSSCRPGPGAWLRVVLEKPFGHDH
FSAQQLATELGTFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEII
MKETVDAEGRTSFYEEYGVIRDVLQNHLTEVLTLVAMELPHNVSSAEAVLRHKLQVFQAL
RGLQRGSAVVGQYQSYSEQVRRELQKPDSFHSLTPTFAAVLVHIDNLRWEGVPFILMSGK
ALDERVGYARILFKNQACCVQSEKHWAAAQSQCLPRQLVFHIGHGDLGSPAVLVSRNLFR
PSLPSSWKEMEGPPGLRLFGSPLSDYYAYSPVRERDAHSVLLSHIFHGRKNFFITTENLL
ASWNFWTPLLESLAHKAPRLYPGGAENGRLLDFEFSSGRLFFSQQQPEQLVPGPGPAPMP
SDFQVLRAKYRESPLVSAWSEELISKLANDIEATAVRAVRRFGQFHLALSGGSSPVALFQ
QLATAHYGFPWAHTHLWLVDERCVPLSDPESNFQGLQAHLLQHVRIPYYNIHPMPVHLQQ
RLCAEEDQGAQIYAREISALVANSSFDLVLLGMGADGHTASLFPQSPTGLDGEQLVVLTT
SPSQPHRRMSLSLPLINRAKKVAVLVMGRMKREITTLVSRVGHEPKKWPISGVLPHSGQL
VWYMDYDAFLG
Enzyme 36 Number of Residues 791
Enzyme 36 Molecular Weight 88892.0
Enzyme 36 Theoretical pI 7.31
Enzyme 36 GO Classification
Function
  • 6-phosphogluconolactonase activity
  • NADP or NADPH binding
  • binding
  • carboxylesterase activity
  • catalytic activity
  • glucose-6-phosphate dehydrogenase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • carbohydrate metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • pentose-phosphate shunt
  • primary metabolic process
  • small molecule metabolic process
Component
—
Enzyme 36 General Function Involved in 6-phosphogluconolactonase activity
Enzyme 36 Specific Function Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates
Enzyme 36 Pathways
Enzyme 36 Reactions
  • 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate [RN:R02035]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-19
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 4186038 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID O95479 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name G6PE_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2376 bp 
ATGTGGAATATGCTCATAGTGGCGATGTGCTTGGCCCTTCTGGGCTGCCTGCAAGCCCAG
GAGCTCCAGGGACATGTCTCCATAATCCTGCTGGGAGCAACTGGGGACCTGGCTAAGAAG
TACTTATGGCAGGGACTGTTCCAGCTGTACCTGGATGAAGCGGGGAGGGGTCACAGTTTT
AGCTTCCATGGAGCTGCTCTGACAGCCCCCAAGCAGGGTCAAGAGCTCATGGCCAAGGCC
CTGGAATCCCTCTCCTGCCCCAAGGACATGGCACCCAGTCACTGTGCAGAGCACAAGGAT
CAGTTCCTGCAGCTGAGCCAGTACCGCCAACTGAAGACGGCCGAGGACTATCAGGCCCTG
AACAAGGACATCGAGGCACAGCTCCAGCACGCAGGCCTCCGGGAGGCTGGCAGGATCTTC
TACTTCTCAGTGCCACCCTTCGCCTATGAAGACATTGCCCGCAACATCAACAGTAGCTGC
CGGCCAGGCCCGGGCGCCTGGCTGCGGGTTGTCCTTGAGAAACCCTTTGGCCATGACCAC
TTCTCAGCCCAGCAGCTGGCCACAGAACTCGGGACCTTTTTCCAGGAGGAGGAGATGTAC
CGGGTGGACCATTACTTAGGCAAGCAGGCTGTGGCGCAGATCCTGCCTTTCCGAGACCAG
AACCGCAAGGCTTTGGACGGCCTCTGGAACCGGCACCATGTGGAGCGGGTGGAGATCATC
ATGAAAGAGACCGTGGATGCTGAAGGCCGCACCAGCTTCTATGAGGAGTACGGTGTCATT
CGCGACGTCCTCCAGAACCATCTGACGGAGGTCCTCACCCTCGTGGCCATGGAGCTGCCC
CACAATGTCAGCAGTGCGGAGGCTGTGCTGCGGCACAAGCTTCAGGTCTTCCAGGCGCTG
CGGGGCCTGCAGAGGGGCAGTGCCGTCGTGGGCCAGTACCAGTCTTACAGTGAGCAGGTG
CGCAGAGAGCTGCAGAAGCCAGACAGCTTCCACAGCCTGACGCCGACCTTCGCAGGTGTC
CTAGTGCACATTGACAACCTTCGCTGGGAGGGCGTGCCTTTCATCCTGATGTCTGGCAAA
GCCTTGGACGAGAGAGTGGGCTACGCTCGGATCTTGTTCAAGAACCAGGCCTGCTGTGTG
CAGAGCGAAAAGCACTGGGCCGCGGCGCAGAGCCAGTGCCTGCCCCGGCAGCTCGTCTTC
CACATCGGCCATGGCGACCTGGGCAGCCCTGCCGTGCTGGTCAGCAGGAACCTGTTCAGG
CCCTCCCTGCCCTCCAGCTGGAAGGAAATGGAGGGACCACCTGGGCTCCGCCTTTTCGGC
AGCCCTCTGTCCGATTACTACGCCTACAGCCCTGTGCGGGAGCGGGACGCCCACTCCGTC
CTCTTATCCCATATCTTCCATGGCCGGAAGAATTTCTTCATCACCACAGAGAACTTGCTG
GCCTCCTGGAACTTCTGGACCCCTCTGCTGGAGAGCCTGGCCCATAAGGCCCCACGCCTC
TACCCTGGAGGAGCTGAGAATGGCCGTCTGTTGGACTTTGAGTTCAGTAGCGGCCGGTTG
TTCTTTTCCCAGCAGCAGCCGGAGCAGCTGGTGCCAGGGCCAGGGCCGGCCCCAATGCCC
AGTGACTTCCAGGTCCTCAGGGCCAAGTACCGAGAGAGCCCGCTGGTCTCCGCCTGGTCC
GAGGAGCTGATCTCTAAGCTGGCTAATGACATCGAGGCCACCGCTGTGCGAGCCGTGCGG
CGCTTTGGCCAGTTCCACCTGGCACTGTCGGGGGGCTCGAGCCCCGTGGCCCTGTTCCAG
CAGCTGGCCACGGCGCACTATGGCTTCCCCTGGGCCCACACGCACCTGTGGCTGGTTGAC
GAGCGCTGCGTCCCACTCTCAGACCCGGAGTCCAACTTCCAGGGCCTGCAGGCCCACCTG
CTGCAGCACGTCCGGATCCCCTACTACAACATCCACCCCATGCCTGTGCACCTGCAGCAG
CGGCTCTGCGCCGAGGAGGACCAGGGCGCCCAGATCTATGCCAGGGAGATCTCAGCCCTG
GTGGCCAACAGCAGCTTCGACCTGGTGCTGCTGGGCATGGGTGCCGACGGGCACACAGCC
TCCCTCTTCCCACAGTCACCCACTGGCCTGGATGGCGAGCAGCTGGTCGTGCTGACCACG
AGCCCCTCCCAGCCACACCGCCGCATGAGCCTTAGCCTGCCTCTCATCAACCGCGCCAAG
AAGGTGGCAGTCCTGGTCATGGGCAGGATGAAGCGTGAGATCACCACGCTGGTGAGCCGG
GTGGGCCATGAGCCCAAGAAGTGGCCCATCTCGGGTGTCCTGCCGCACTCCGGCCAGCTG
GTGTGGTACATGGACTACGACGCCTTCCTGGGATGA
Enzyme 36 GenBank Gene ID AJ012590 Link Image
Enzyme 36 GeneCard ID H6PD Link Image
Enzyme 36 GenAtlas ID H6PD Link Image
Enzyme 36 HGNC ID HGNC:4795 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1p36
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Mason PJ, Stevens D, Diez A, Knight SW, Scopes DA, Vulliamy TJ: Human hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) encoded at 1p36: coding sequence and expression. Blood Cells Mol Dis. 1999 Feb;25(1):30-7. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. Draper N, Walker EA, Bujalska IJ, Tomlinson JW, Chalder SM, Arlt W, Lavery GG, Bedendo O, Ray DW, Laing I, Malunowicz E, White PC, Hewison M, Mason PJ, Connell JM, Shackleton CH, Stewart PM: Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency. Nat Genet. 2003 Aug;34(4):434-9. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5596
Enzyme 37 Name Aldo-keto reductase family 1 member C3
Enzyme 37 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase type 5
  2. 17-beta-HSD 5
  3. 3-alpha-HSD type II, brain
  4. 3-alpha-hydroxysteroid dehydrogenase type 2
  5. 3-alpha-HSD type 2
  6. Chlordecone reductase homolog HAKRb
  7. Dihydrodiol dehydrogenase 3
  8. DD-3
  9. DD3
  10. Dihydrodiol dehydrogenase type I
  11. HA1753
  12. Indanol dehydrogenase
  13. Prostaglandin F synthase
  14. PGFS
  15. Testosterone 17-beta-dehydrogenase 5
  16. Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Enzyme 37 Gene Name AKR1C3
Enzyme 37 Protein Sequence >Aldo-keto reductase family 1 member C3 
MDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPM
SLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD
RNLHYFNSDSFASHPNYPYSDEY
Enzyme 37 Number of Residues 323
Enzyme 37 Molecular Weight 36852.9
Enzyme 37 Theoretical pI 8.06
Enzyme 37 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 37 General Function Involved in oxidoreductase activity
Enzyme 37 Specific Function Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta- PGF2 to PGD2. Functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone
Enzyme 37 Pathways
Enzyme 37 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+ [RN:R00814]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 6624211 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID P42330 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name AK1C3_HUMAN Link Image
Enzyme 37 PDB ID 1XF0 Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >972 bp 
ATGGATTCCAAACAGCAGTGTGTAAAGCTAAATGATGGCCACTTCATGCCTGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGAAGTAAAGCTTTGGAGGTCACAAAATTA
GCAATAGAAGCTGGGTTCCGCCATATAGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTCCACTTTTCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AACTCACTGAAAAAAGCTCAATTGGACTATGTTGACCTCTATCTTATTCATTCTCCAATG
TCTCTAAAGCCAGGTGAGGAACTTTCACCAACAGATGAAAATGGAAAAGTAATATTTGAC
ATAGTGGATCTCTGTACCACCTGGGAGGCCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATTGGGGTGTCAAACTTCAACCGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCGTATTTCAACCGGAGT
AAATTGCTAGATTTCTGCAAGTCGAAAGATATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCTCAACGAGACAAACGATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTTTTTGAGTTCCAGTTGACTGCAGAGGACATGAAAGCCATAGATGGCCTAGAC
AGAAATCTCCACTATTTTAACAGTGATAGTTTTGCTAGCCACCCTAATTATCCATATTCA
GATGAATATTAA
Enzyme 37 GenBank Gene ID AB018580 Link Image
Enzyme 37 GeneCard ID AKR1C3 Link Image
Enzyme 37 GenAtlas ID AKR1C3 Link Image
Enzyme 37 HGNC ID HGNC:386 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 10p15-p14
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  2. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed Link Image]
  3. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  4. Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM: Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. Mol Endocrinol. 1997 Dec;11(13):1971-84. [PubMed Link Image]
  5. Suzuki-Yamamoto T, Nishizawa M, Fukui M, Okuda-Ashitaka E, Nakajima T, Ito S, Watanabe K: cDNA cloning, expression and characterization of human prostaglandin F synthase. FEBS Lett. 1999 Dec 3;462(3):335-40. [PubMed Link Image]
  6. Griffin LD, Mellon SH: Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13512-7. [PubMed Link Image]
  7. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  8. Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N: Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). Mol Cell Endocrinol. 2001 Jan 22;171(1-2):137-49. [PubMed Link Image]
  9. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed Link Image]
  10. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  11. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  12. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  13. Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V: Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. Endocrinology. 1999 Feb;140(2):568-74. [PubMed Link Image]
  14. Komoto J, Yamada T, Watanabe K, Takusagawa F: Crystal structure of human prostaglandin F synthase (AKR1C3). Biochemistry. 2004 Mar 2;43(8):2188-98. [PubMed Link Image]
  15. Lovering AL, Ride JP, Bunce CM, Desmond JC, Cummings SM, White SA: Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in complex with the nonsteroidal anti-inflammatory drugs flufenamic acid and indomethacin. Cancer Res. 2004 Mar 1;64(5):1802-10. [PubMed Link Image]
  16. Qiu W, Zhou M, Labrie F, Lin SX: Crystal structures of the multispecific 17beta-hydroxysteroid dehydrogenase type 5: critical androgen regulation in human peripheral tissues. Mol Endocrinol. 2004 Jul;18(7):1798-807. Epub 2004 Apr 15. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 5623
Enzyme 38 Name Aldo-keto reductase family 1 member C1
Enzyme 38 Synonyms
  1. 20-alpha-hydroxysteroid dehydrogenase
  2. 20-alpha-HSD
  3. Chlordecone reductase homolog HAKRC
  4. Dihydrodiol dehydrogenase 1/2
  5. DD1/DD2
  6. High-affinity hepatic bile acid-binding protein
  7. HBAB
  8. Indanol dehydrogenase
  9. Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Enzyme 38 Gene Name AKR1C1
Enzyme 38 Protein Sequence >Aldo-keto reductase family 1 member C1 
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
Enzyme 38 Number of Residues 323
Enzyme 38 Molecular Weight 36788.0
Enzyme 38 Theoretical pI 7.99
Enzyme 38 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 38 General Function Involved in oxidoreductase activity
Enzyme 38 Specific Function Converts progesterone to its inactive form, 20-alpha- dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation
Enzyme 38 Pathways
Enzyme 38 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+ [RN:R00814]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein Not Available
Enzyme 38 UniProtKB/Swiss-Prot ID Q04828 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name AK1C1_HUMAN Link Image
Enzyme 38 PDB ID 1MRQ Link Image
Enzyme 38 PDB File Show
Enzyme 38 3D Structure
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >972 bp 
ATGGATTCGAAATATCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTTTAGAGGCCACCAAATTG
GCAATTGAAGCTGGCTTCCGCCATATTGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGATTATGTTGACCTCTACCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCGTGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCACCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTACAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
Enzyme 38 GenBank Gene ID M86609 Link Image
Enzyme 38 GeneCard ID AKR1C1 Link Image
Enzyme 38 GenAtlas ID AKR1C1 Link Image
Enzyme 38 HGNC ID HGNC:384 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 10p15-p14
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE: cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J Biol Chem. 1993 May 15;268(14):10448-57. [PubMed Link Image]
  2. Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A: Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. J Biol Chem. 1994 Mar 18;269(11):8416-22. [PubMed Link Image]
  3. Ciaccio PJ, Jaiswal AK, Tew KD: Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics. J Biol Chem. 1994 Jun 3;269(22):15558-62. [PubMed Link Image]
  4. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  5. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  6. Zhang Y, Dufort I, Rheault P, Luu-The V: Characterization of a human 20alpha-hydroxysteroid dehydrogenase. J Mol Endocrinol. 2000 Oct;25(2):221-8. [PubMed Link Image]
  7. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  10. Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N: Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. Biochem J. 1996 Jan 15;313 ( Pt 2):373-6. [PubMed Link Image]
  11. Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed Link Image]
  12. Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R: Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids. J Mol Biol. 2003 Aug 15;331(3):593-604. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 5624
Enzyme 39 Name Aldo-keto reductase family 1 member C2
Enzyme 39 Synonyms
  1. 3-alpha-HSD3
  2. Chlordecone reductase homolog HAKRD
  3. Dihydrodiol dehydrogenase 2
  4. DD-2
  5. DD2
  6. Dihydrodiol dehydrogenase/bile acid-binding protein
  7. DD/BABP
  8. Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
  9. Type III 3-alpha-hydroxysteroid dehydrogenase
Enzyme 39 Gene Name AKR1C2
Enzyme 39 Protein Sequence >Aldo-keto reductase family 1 member C2 
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
Enzyme 39 Number of Residues 323
Enzyme 39 Molecular Weight 36735.0
Enzyme 39 Theoretical pI 7.55
Enzyme 39 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 39 General Function Involved in oxidoreductase activity
Enzyme 39 Specific Function Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha- DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+ [RN:R00814]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 4062863 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P52895 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name AK1C2_HUMAN Link Image
Enzyme 39 PDB ID 1IHI Link Image
Enzyme 39 PDB File Show
Enzyme 39 3D Structure
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >972 bp 
ATGGATTCGAAATACCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTCTAGAGGCCGTCAAATTG
GCAATAGAAGCCGGGTTCCACCATATTGATTCTGCACATGTTTACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGAGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGACTATGTTGACCTCTATCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACATGGGAGGCCATGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCACAGGCTGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCATCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
Enzyme 39 GenBank Gene ID AB021654 Link Image
Enzyme 39 GeneCard ID AKR1C2 Link Image
Enzyme 39 GenAtlas ID AKR1C2 Link Image
Enzyme 39 HGNC ID HGNC:385 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 10p15-p14
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  2. Ciaccio PJ, Tew KD: cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase. Biochim Biophys Acta. 1994 Jun 28;1186(1-2):129-32. [PubMed Link Image]
  3. Qin KN, Khanna M, Cheng KC: Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein. Gene. 1994 Nov 18;149(2):357-61. [PubMed Link Image]
  4. Dufort I, Soucy P, Labrie F, Luu-The V: Molecular cloning of human type 3 3 alpha-hydroxysteroid dehydrogenase that differs from 20 alpha-hydroxysteroid dehydrogenase by seven amino acids. Biochem Biophys Res Commun. 1996 Nov 12;228(2):474-9. [PubMed Link Image]
  5. Shiraishi H, Ishikura S, Matsuura K, Deyashiki Y, Ninomiya M, Sakai S, Hara A: Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA. Biochem J. 1998 Sep 1;334 ( Pt 2):399-405. [PubMed Link Image]
  6. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N: Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. Biochem J. 1996 Jan 15;313 ( Pt 2):373-6. [PubMed Link Image]
  11. Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE: cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J Biol Chem. 1993 May 15;268(14):10448-57. [PubMed Link Image]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Jin Y, Stayrook SE, Albert RH, Palackal NT, Penning TM, Lewis M: Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate. Biochemistry. 2001 Aug 28;40(34):10161-8. [PubMed Link Image]
  14. Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SX: Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution. J Biol Chem. 2001 Nov 9;276(45):42091-8. Epub 2001 Aug 20. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 5628
Enzyme 40 Name Glyoxylate reductase/hydroxypyruvate reductase
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name GRHPR
Enzyme 40 Protein Sequence >Glyoxylate reductase/hydroxypyruvate reductase 
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLS
DHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLL
TTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRF
LYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVF
INISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHR
TRNTMSLLAANNLLAGLRGEPMPSELKL
Enzyme 40 Number of Residues 328
Enzyme 40 Molecular Weight 35667.9
Enzyme 40 Theoretical pI 7.44
Enzyme 40 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cofactor binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • metabolic process
Component
—
Enzyme 40 General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Enzyme 40 Specific Function Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate
Enzyme 40 Pathways
Enzyme 40 Reactions
  • D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H + H+ [RN:R01388 R01392]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 6002730 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q9UBQ7 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name GRHPR_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >987 bp 
ATGAGACCGGTGCGACTCATGAAGGTGTTCGTCACCCGCAGGATACCCGCCGAGGGTAGG
GTCGCGCTCGCCCGGGCGGCAGACTGTGAGGTGGAGCAGTGGGACTCGGATGAGCCCATC
CCTGCCAAGGAGCTAGAGCGAGGTGTGGCGGGGGCCCACGGCCTGCTCTGCCTCCTCTCC
GACCACGTGGACAAGAGGATCCTGGATGCTGCAGGGGCCAATCTCAAAGTCATCAGCACC
ATGTCTGTGGGCATCGACCACTTGGCTTTGGATGAAATCAAGAAGCGTGGGATCCGAGTT
GGCTACACCCCAGATGTCCTGACAGATACCACCGCCGAACTCGCAGTCTCCCTGCTACTT
ACCACCTGCCGCCGGTTGCCGGAGGCCATCGAGGAAGTGAAGAATGGTGGCTGGACCTCG
TGGAAGCCCCTCTGGCTGTGTGGCTATGGACTCACGCAGAGCACTGTCGGCATCATCGGG
CTGGGGCGCATAGGCCAGGCCATTGCTCGGCGTCTGAAACCATTCGGTGTCCAGAGATTT
CTGTACACAGGGCGCCAGCCCAGGCCTGAGGAAGCAGCAGAATTCCAGGCAGAGTTTGTG
TCTACCCCTGAGCTGGCTGCCCAATCTGATTTCATCGTCGTGGCCTGCTCCTTAACACCT
GCAACCGAGGGACTCTGCAACAAGGACTTCTTCCAGAAGATGAAGGAAACAGCTGTGTTC
ATCAACATCAGCAGGGGCGACGTCGTAAACCAGGACGACCTGTACCAGGCCTTGGCCAGT
GGTAAGATTGCAGCTGCTGGACTGGATGTGACGAGCCCAGAACCACTGCCTACAAACCAC
CCTCTCCTGACCCTGAAGAACTGTGTGATTCTGCCCCACATTGGCAGTGCCACCCACAGA
ACCCGCAACACCATGTCCTTGTTGGCAGCTAACAACTTGCTGGCTGGCCTGAGAGGGGAG
CCGATGCCTAGTGAACTCAAGCTGTAG
Enzyme 40 GenBank Gene ID AF134895 Link Image
Enzyme 40 GeneCard ID GRHPR Link Image
Enzyme 40 GenAtlas ID GRHPR Link Image
Enzyme 40 HGNC ID HGNC:4570 Link Image
Enzyme 40 Chromosome Location 9
Enzyme 40 Locus 9q12
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Rumsby G, Cregeen DP: Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase. Biochim Biophys Acta. 1999 Sep 3;1446(3):383-8. [PubMed Link Image]
  2. Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP: The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II. Hum Mol Genet. 1999 Oct;8(11):2063-9. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Huang T, Yang W, Pereira AC, Craigen WJ, Shih VE: Cloning and characterization of a putative human d-2-hydroxyacid dehydrogenase in chromosome 9q. Biochem Biophys Res Commun. 2000 Feb 16;268(2):298-301. [PubMed Link Image]
  5. Booth MP, Conners R, Rumsby G, Brady RL: Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase. J Mol Biol. 2006 Jun 30;360(1):178-89. Epub 2006 May 22. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 5638
Enzyme 41 Name Cytochrome P450 4A11
Enzyme 41 Synonyms
  1. 20-hydroxyeicosatetraenoic acid synthase
  2. 20-HETE synthase
  3. CYP4AII
  4. CYPIVA11
  5. Cytochrome P-450HK-omega
  6. Cytochrome P450HL-omega
  7. Fatty acid omega-hydroxylase
  8. Lauric acid omega-hydroxylase
Enzyme 41 Gene Name CYP4A11
Enzyme 41 Protein Sequence >Cytochrome P450 4A11 
MSVSVLSPSRLLGDVSGILQAASLLILLLLLIKAVQLYLHRQWLLKALQQFPCPPSHWLF
GHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSY
RFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQD
SPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQND
TIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKM
ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAS
ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHH
NPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL
LPDPTRIPIPIARLVLKSKNGIHLRLRRLPNPCEDKDQL
Enzyme 41 Number of Residues 519
Enzyme 41 Molecular Weight 59347.3
Enzyme 41 Theoretical pI 8.99
Enzyme 41 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 41 General Function Involved in monooxygenase activity
Enzyme 41 Specific Function Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE)
Enzyme 41 Pathways
Enzyme 41 Reactions
  • octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O [RN:R02879]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein Not Available
Enzyme 41 UniProtKB/Swiss-Prot ID Q02928 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name CP4AB_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1560 bp 
ATGAGTGTCTCTGTGCTGAGCCCCAGCAGACTCCTGGGTGATGTCTCTGGAATCCTCCAA
GCGGCCTCCCTGCTCATTCTGCTTCTGCTGCTGATCAAGGCAGTTCAGCTCTACCTGCAC
AGGCAGTGGCTGCTCAAAGCCCTCCAGCAGTTCCCGTGCCCTCCCTCCCACTGGCTCTTC
GGGCACATCCAGGAGCTCCAACAGGACCAGGAGCTACAACGGATTCAGAAATGGGTGGAG
ACATTCCCAAGTGCCTGTCCTCATTGGCTATGGGGAGGCAAAGTTCGTGTCCAGCTCTAT
GACCCTGACTATATGAAGGTGATTCTGGGGAGATCAGACCCGAAATCCCATGGTTCCTAC
AGATTCCTGGCTCCATGGATTGGGTACGGCTTGCTCCTGTTGAATGGGCAGACATGGTTC
CAGCATCGACGGATGCTGACCCCAGCCTTCCACTATGACATCCTGAAGCCCTATGTGGGG
CTCATGGCAGACTCTGTACGAGTGATGCTGGACAAATGGGAAGAGCTCCTTGGCCAGGAT
TCCCCTCTGGAGGTCTTTCAGCACGTCTCCTTGATGACCCTGGACACCATCATGAAGTGT
GCCTTCAGCCATCAGGGCAGCATCCAGGTGGACAGGAATTCTCAGTCCTACATACAGGCC
ATTAGTGACCTGAACAACCTGGTTTTTTCCCGTGTGAGGAATGCCTTTCACCAGAATGAC
ACCATCTACAGCCTGACCTCTGCTGGCCGCTGGACACACCGCGCCTGCCAGCTGGCCCAT
CAGCACACAGACCAAGTGATCCAACTGAGGAAGGCTCAACTACAGAAGGAGGGGGAGCTG
GAGAAGATCAAGAGGAAGAGGCATTTGGATTTTCTGGATATCCTCCTCTTGGCCAAAATG
GAGAATGGGAGCATCTTGTCAGACAAGGACCTCCGTGCTGAGGTGGACACGTTCATGTTT
GAGGGCCACGACACCACAGCCAGTGGGATCTCCTGGATCCTCTATGCTCTGGCCACACAC
CCCAAGCATCAGGAGAGGTGCCGGGAGGAGATCCACAGCCTCCTGGGTGATGGAGCCTCC
ATCACCTGGAACCACCTGGACCAGATGCCCTACACCACCATGTGCATTAAGGAGGCACTG
AGGCTCTACCCACCGGTGCCAGGCATTGGCAGAGAGCTCAGCACTCCCGTCACCTTCCCT
GATGGGCGCTCCTTGCCCAAAGGTATCATGGTCCTCCTCTCCATTTATGGCCTTCACCAC
AACCCAAAAGTGTGGCCCAACCCAGAGGTGTTTGACCCTTTCCGTTTTGCACCGGGTTCT
GCTCAACACAGCCACGCTTTCCTGCCCTTCTCAGGAGGATCAAGGAACTGCATTGGGAAA
CAATTTGCCATGAACGAGCTGAAGGTGGCCACGGCCCTGACCCTGCTCCGCTTTGAGCTG
CTGCCTGATCCCACCAGGATCCCCATCCCCATTGCACGACTTGTGTTGAAATCCAAAAAT
GGAATCCACCTGCGTCTCAGGAGGCTCCCTAACCCTTGTGAAGACAAGGACCAGCTTTGA
Enzyme 41 GenBank Gene ID L04751 Link Image
Enzyme 41 GeneCard ID CYP4A11 Link Image
Enzyme 41 GenAtlas ID CYP4A11 Link Image
Enzyme 41 HGNC ID HGNC:2642 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 1p33
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Palmer CN, Richardson TH, Griffin KJ, Hsu MH, Muerhoff AS, Clark JE, Johnson EF: Characterization of a cDNA encoding a human kidney, cytochrome P-450 4A fatty acid omega-hydroxylase and the cognate enzyme expressed in Escherichia coli. Biochim Biophys Acta. 1993 Feb 20;1172(1-2):161-6. [PubMed Link Image]
  2. Kawashima H, Kusunose E, Kikuta Y, Kinoshita H, Tanaka S, Yamamoto S, Kishimoto T, Kusunose M: Purification and cDNA cloning of human liver CYP4A fatty acid omega-hydroxylase. J Biochem (Tokyo). 1994 Jul;116(1):74-80. [PubMed Link Image]
  3. Imaoka S, Ogawa H, Kimura S, Gonzalez FJ: Complete cDNA sequence and cDNA-directed expression of CYP4A11, a fatty acid omega-hydroxylase expressed in human kidney. DNA Cell Biol. 1993 Dec;12(10):893-9. [PubMed Link Image]
  4. Bellamine A, Wang Y, Waterman MR, Gainer JV 3rd, Dawson EP, Brown NJ, Capdevila JH: Characterization of the CYP4A11 gene, a second CYP4A gene in humans. Arch Biochem Biophys. 2003 Jan 1;409(1):221-7. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Kawashima H, Kusunose E, Kubota I, Maekawa M, Kusunose M: Purification and NH2-terminal amino acid sequences of human and rat kidney fatty acid omega-hydroxylases. Biochim Biophys Acta. 1992 Jan 24;1123(2):156-62. [PubMed Link Image]
  8. Bell DR, Plant NJ, Rider CG, Na L, Brown S, Ateitalla I, Acharya SK, Davies MH, Elias E, Jenkins NA, et al.: Species-specific induction of cytochrome P-450 4A RNAs: PCR cloning of partial guinea-pig, human and mouse CYP4A cDNAs. Biochem J. 1993 Aug 15;294 ( Pt 1):173-80. [PubMed Link Image]
  9. Hoch U, Ortiz De Montellano PR: Covalently linked heme in cytochrome p4504a fatty acid hydroxylases. J Biol Chem. 2001 Apr 6;276(14):11339-46. Epub 2001 Jan 3. [PubMed Link Image]
  10. LeBrun LA, Hoch U, Ortiz de Montellano PR: Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family. J Biol Chem. 2002 Apr 12;277(15):12755-61. Epub 2002 Jan 30. [PubMed Link Image]
  11. Gainer JV, Bellamine A, Dawson EP, Womble KE, Grant SW, Wang Y, Cupples LA, Guo CY, Demissie S, O'Donnell CJ, Brown NJ, Waterman MR, Capdevila JH: Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension. Circulation. 2005 Jan 4;111(1):63-9. Epub 2004 Dec 20. [PubMed Link Image]
  12. Cho BH, Park BL, Kim LH, Chung HS, Shin HD: Highly polymorphic human CYP4A11 gene. J Hum Genet. 2005;50(5):259-63. Epub 2005 May 14. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 5658
Enzyme 42 Name Methionine synthase reductase
Enzyme 42 Synonyms
  1. MSR
Enzyme 42 Gene Name MTRR
Enzyme 42 Protein Sequence >Methionine synthase reductase 
MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS
Enzyme 42 Number of Residues 725
Enzyme 42 Molecular Weight 80409.2
Enzyme 42 Theoretical pI 6.47
Enzyme 42 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 42 General Function Involved in oxidoreductase activity
Enzyme 42 Specific Function Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions
  • 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine [RN:R05182]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 6561339 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q9UBK8 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name MTRR_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >2178 bp 
ATGGGCGCTGCGTCAGTGCGCGCTGGCGCAAGGTTGGTGGAAGTCGCGTTGTGCAGTTTC
ACTGTTACATGCCTTGAAGTGATGAGGAGGTTTCTGTTACTATATGCTACACAGCAGGGA
CAGGCAAAGGCCATCGCAGAAGAAATGTGTGAGCAAGCTGTGGTACATGGATTTTCTGCA
GATCTTCACTGTATTAGTGAATCCGATAAGTATGACCTAAAAACCGAAACAGCTCCTCTT
GTTGTTGTGGTTTCTACCACGGGCACCGGAGACCCACCCGACACAGCCCGCAAGTTTGTT
AAGGAAATACAGAACCAAACACTGCCGGTTGATTTCTTTGCTCACCTGCGGTATGGGTTA
CTGGGTCTCGGTGATTCAGAATACACCTACTTTTGCAATGGGGGGAAGATAATTGATAAA
CGACTTCAAGAGCTTGGAGCCCGGCATTTCTATGACACTGGACATGCAGATGACTGTGTA
GGTTTAGAACTTGTGGTTGAGCCGTGGATTGCTGGACTCTGGCCAGCCCTCAGAAAGCAT
TTTAGGTCAAGCAGAGGACAAGAGGAGATAAGTGGCGCACTCCCGGTGGCATCACCTGCA
TCCTTGAGGACAGACCTTGTGAAGTCAGAGCTGCTACACATTGAATCTCAAGTCGAGCTT
CTGAGATTCGATGATTCAGGAAGAAAGGATTCTGAGGTTTTGAAGCAAAATGCAGTGAAC
AGCAACCAATCCAATGTTGTAATTGAAGACTTTGAGTCCTCACTTACCCGTTCGGTACCC
CCACTCTCACAAGCCTCTCTGAATATTCCTGGTTTACCCCCAGAATATTTACAGGTACAT
CTGCAGGAGTCTCTTGGCCAGGAGGAAAGCCAAGTATCTGTGACTTCAGCAGATCCAGTT
TTTCAAGTGCCAATTTCAAAGGCAGTTCAACTTACTACGAATGATGCCATAAAAACCACT
CTGCTGGTAGAATTGGACATTTCAAATACAGACTTTTCCTATCAGCCTGGAGATGCCTTC
AGCGTGATCTGCCCTAACAGTGATTCTGAGGTACAAAGCCTACTCCAAAGACTGCAGCTT
GAAGATAAAAGAGAGCACTGCGTCCTTTTGAAAATAAAGGCAGACACAAAGAAGAAAGGA
GCTACCTTACCCCAGCATATACCTGCGGGATGTTCTCTCCAGTTCATTTTTACCTGGTGT
CTTGAAATCCGAGCAATTCCTAAAAAGGCATTTTTGCGAGCCCTTGTGGACTATACCAGT
GACAGTGCTGAAAAGCGCAGGCTACAGGAGCTGTGCAGTAAACAAGGGGCAGCCGATTAT
AGCCGCTTTGTACGAGATGCCTGTGCCTGCTTGTTGGATCTCCTCCTCGCTTTCCCTTCT
TGCCAGCCACCACTCAGTCTCCTGCTCGAACATCTTCCTAAACTTCAACCCAGACCATAT
TCGTGTGCAAGCTCAAGTTTATTTCACCCAGGAAAGCTCCATTTTGTCTTCAACATTGTG
GAATTTCTGTCTACTGCCACAACAGAGGTTCTGCGGAAGGGAGTATGTACAGGCTGGCTG
GCCTTGTTGGTTGCTTCAGTTCTTCAGCCAAACATACATGCATCCCATGAAGACAGCGGG
AAAGCCCTGGCTCCTAAGATATCCATCTCTCCTCGAACAACAAATTCTTTCCACTTACCA
GATGACCCCTCAATCCCCATCATAATGGTGGGTCCAGGAACCGGCATAGCCCCGTTTATT
GGGTTCCTACAACATAGAGAGAAACTCCAAGAACAACACCCAGATGGAAATTTTGGAGCA
ATGTGGTTGTTTTTTGGCTGCAGGCATAAGGATAGGGATTATCTATTCAGAAAAGAGCTC
AGACATTTCCTTAAGCATGGGATCTTAACTCATCTAAAGGTTTCCTTCTCAAGAGATGCT
CCTGTTGGGGAGGAGGAAGCCCCAGCAAAGTATGTACAAGACAACATCCAGCTTCATGGC
CAGCAGGTGGCGAGAATCCTCCTCCAGGAGAACGGCCATATTTATGTGTGTGGAGATGCA
AAGAATATGGCCAAGGATGTACATGATGCCCTTGTGCAAATAATAAGCAAAGAGGTTGGA
GTTGAAAAACTAGAAGCAATGAAAACCCTGGCCACTTTAAAAGAAGAAAAACGCTACCTT
CAGGATATTTGGTCATAA
Enzyme 42 GenBank Gene ID AF121214 Link Image
Enzyme 42 GeneCard ID MTRR Link Image
Enzyme 42 GenAtlas ID MTRR Link Image
Enzyme 42 HGNC ID HGNC:7473 Link Image
Enzyme 42 Chromosome Location 5
Enzyme 42 Locus 5p15.31
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Leclerc D, Odievre M, Wu Q, Wilson A, Huizenga JJ, Rozen R, Scherer SW, Gravel RA: Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene. Gene. 1999 Nov 15;240(1):75-88. [PubMed Link Image]
  2. Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA: Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):3059-64. [PubMed Link Image]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Froese DS, Wu X, Zhang J, Dumas R, Schoel WM, Amrein M, Gravel RA: Restricted role for methionine synthase reductase defined by subcellular localization. Mol Genet Metab. 2008 May;94(1):68-77. Epub 2008 Jan 24. [PubMed Link Image]
  6. Wilson A, Leclerc D, Rosenblatt DS, Gravel RA: Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. Hum Mol Genet. 1999 Oct;8(11):2009-16. [PubMed Link Image]
  7. Wilson A, Platt R, Wu Q, Leclerc D, Christensen B, Yang H, Gravel RA, Rozen R: A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida. Mol Genet Metab. 1999 Aug;67(4):317-23. [PubMed Link Image]
  8. Doolin MT, Barbaux S, McDonnell M, Hoess K, Whitehead AS, Mitchell LE: Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. Am J Hum Genet. 2002 Nov;71(5):1222-6. Epub 2002 Oct 9. [PubMed Link Image]
  9. O'Leary VB, Mills JL, Pangilinan F, Kirke PN, Cox C, Conley M, Weiler A, Peng K, Shane B, Scott JM, Parle-McDermott A, Molloy AM, Brody LC: Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association. Mol Genet Metab. 2005 Jul;85(3):220-7. Epub 2005 Mar 17. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 5673
Enzyme 43 Name Sepiapterin reductase
Enzyme 43 Synonyms
  1. SPR
Enzyme 43 Gene Name SPR
Enzyme 43 Protein Sequence >Sepiapterin reductase 
MEGGLGRAVCLLTGASRGFGRTLAPLLASLLSPGSVLVLSARNDEALRQLEAELGAERSG
LRVVRVPADLGAEAGLQQLLGALRELPRPKGLQRLLLINNAGSLGDVSKGFVDLSDSTQV
NNYWALNLTSMLCLTSSVLKAFPDSPGLNRTVVNISSLCALQPFKGWALYCAGKAARDML
FQVLALEEPNVRVLNYAPGPLDTDMQQLARETSVDPDMRKGLQELKAKGKLVDCKVSAQK
LLSLLEKDEFKSGAHVDFYDK
Enzyme 43 Number of Residues 261
Enzyme 43 Molecular Weight 28048.1
Enzyme 43 Theoretical pI 8.19
Enzyme 43 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • sepiapterin reductase activity
Process
  • biosynthetic process
  • cellular biosynthetic process
  • heterocycle biosynthetic process
  • metabolic process
  • oxidation reduction
  • pteridine and derivative biosynthetic process
  • tetrahydrobiopterin biosynthetic process
Component
—
Enzyme 43 General Function Involved in oxidoreductase activity
Enzyme 43 Specific Function Catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin
Enzyme 43 Pathways
Enzyme 43 Reactions
  • (1) 7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+ [RN:R02975]
  • (2) tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+ [RN:R08208]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 338021 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P35270 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name SPRE_HUMAN Link Image
Enzyme 43 PDB ID 1Z6Z Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >786 bp 
ATGGAGGGCGGGCTGGGGCGTGCTGTGTGCTTGCTGACCGGGGCCTCCCGCGGCTTCGGC
CGGACGCTGGCCCCGCTCCTGGCCTCGCTGCTGTCGCCCGGCTCCGTGCTTGTCCTTAGC
GCCCGCAACGACGAGGCACTGCGCCAGCTGGAGGCCGAGCTGGGCGCCGAGCGGTCTGGC
CTGCGCGTGGTGCGGGTGCCCGCCGACCTGGGCGCCGAGGCCGGCTTGCAGCAGCTGCTC
GGCGCCCTGCGCGAGCTCCCCCGGCCCAAGGGGCTGCAGCGACTGCTGCTTATCAACAAC
GCGGGCTCTCTTGGGGATGTGTCCAAAGGCTTCGTGGACCTGAGTGACTCCACTCAAGTG
AACAACTACTGGGCACTGAACTTGACCTCCATGCTCTGCCTGACTTCCAGCGTCCTGAAG
GCCTTCCCGGACAGTCCTGGCCTCAACAGAACCGTGGTTAACATCTCGTCCCTCTGTGCC
CTGCAACCTTTCAAAGGCTGGGCGCTGTACTGTGCAGGAAAGGCTGCTCGTGATATGCTG
TTCCAGGTCCTGGCGCTGGAGGAACCTAATGTGAGGGTGCTGAACTATGCCCCAGGTCCT
CTGGACACAGACATGCAGCAGTTGGCCCGGGAGACCTCCGTGGACCCAGACATGCGAAAA
GGGCTGCAGGAGCTGAAGGCAAAGGGGAAGCTGGTGGATTGCAAGGTGTCAGCCCAGAAA
CTGCTGAGCTTACTGGAAAAGGACGAGTTCAAGTCTGGAGCCCACGTGGACTTCTATGAC
AAATAA
Enzyme 43 GenBank Gene ID M76231 Link Image
Enzyme 43 GeneCard ID SPR Link Image
Enzyme 43 GenAtlas ID SPR Link Image
Enzyme 43 HGNC ID HGNC:11257 Link Image
Enzyme 43 Chromosome Location 2
Enzyme 43 Locus 2p14-p12
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Ichinose H, Katoh S, Sueoka T, Titani K, Fujita K, Nagatsu T: Cloning and sequencing of cDNA encoding human sepiapterin reductase--an enzyme involved in tetrahydrobiopterin biosynthesis. Biochem Biophys Res Commun. 1991 Aug 30;179(1):183-9. [PubMed Link Image]
  2. Maier J, Schott K, Werner T, Bacher A, Ziegler I: Detection of a novel sepiapterin reductase mRNA: assay of mRNA in various cells and tissues of various species. Exp Cell Res. 1993 Feb;204(2):217-22. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Ohye T, Hori TA, Katoh S, Nagatsu T, Ichinose H: Genomic organization and chromosomal localization of the human sepiapterin reductase gene. Biochem Biophys Res Commun. 1998 Oct 20;251(2):597-602. [PubMed Link Image]
  7. Fujimoto K, Takahashi SY, Katoh S: Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II. Biochim Biophys Acta. 2002 Jan 31;1594(1):191-8. [PubMed Link Image]
  8. Bonafe L, Thony B, Penzien JM, Czarnecki B, Blau N: Mutations in the sepiapterin reductase gene cause a novel tetrahydrobiopterin-dependent monoamine-neurotransmitter deficiency without hyperphenylalaninemia. Am J Hum Genet. 2001 Aug;69(2):269-77. Epub 2001 Jul 6. [PubMed Link Image]
  9. Abeling NG, Duran M, Bakker HD, Stroomer L, Thony B, Blau N, Booij J, Poll-The BT: Sepiapterin reductase deficiency an autosomal recessive DOPA-responsive dystonia. Mol Genet Metab. 2006 Sep-Oct;89(1-2):116-20. Epub 2006 May 2. [PubMed Link Image]
  10. Friedman J, Hyland K, Blau N, MacCollin M: Dopa-responsive hypersomnia and mixed movement disorder due to sepiapterin reductase deficiency. Neurology. 2006 Dec 12;67(11):2032-5. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 5685
Enzyme 44 Name Estradiol 17-beta-dehydrogenase 2
Enzyme 44 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase type 2
  2. 17-beta-HSD 2
  3. 20 alpha-hydroxysteroid dehydrogenase
  4. 20-alpha-HSD
  5. E2DH
  6. Microsomal 17-beta-hydroxysteroid dehydrogenase
  7. Testosterone 17-beta-dehydrogenase
Enzyme 44 Gene Name HSD17B2
Enzyme 44 Protein Sequence >Estradiol 17-beta-dehydrogenase 2 
MSTFFSDTAWICLAVPTVLCGTVFCKYKKSSGQLWSWMVCLAGLCAVCLLILSPFWGLIL
FSVSCFLMYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPG
AEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWAVINNAGVLGFPTDGELL
LMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVT
MFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYI
LAQRNFLLLINSLASKDFSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYD
YFAKRHFGQDKPMPRALRMPNYKKKAT
Enzyme 44 Number of Residues 387
Enzyme 44 Molecular Weight 42784.8
Enzyme 44 Theoretical pI 8.62
Enzyme 44 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 44 General Function Involved in oxidoreductase activity
Enzyme 44 Specific Function Capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 uses NADPH
Enzyme 44 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 44 Reactions
  • testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+ [RN:R01836]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • 4-24
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID P37059 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name DHB2_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1164 bp 
ATGAGCACTTTCTTCTCGGACACAGCATGGATCTGCCTGGCTGTCCCCACAGTACTATGT
GGGACAGTATTTTGCAAATACAAGAAGAGCTCAGGGCAGCTGTGGAGCTGGATGGTCTGC
CTGGCAGGCCTCTGTGCAGTCTGCCTGCTCATCCTGTCCCCTTTTTGGGGCTTGATCCTC
TTCTCGGTGTCATGCTTCCTCATGTATACTTACTTATCTGGCCAAGAATTGTTACCTGTG
GATCAGAAGGCAGTCCTGGTGACAGGTGGTGATTGCGGGCTTGGCCATGCTTTGTGCAAG
TATCTGGATGAGCTGGGCTTCACGGTATTTGCCGGAGTTTTGAATGAAAATGGCCCAGGA
GCTGAGGAATTGCGAAGAACCTGCTCTCCGCGCCTCTCGGTGCTCCAAATGGACATCACG
AAGCCAGTGCAGATAAAAGATGCTTACAGCAAGGTTGCAGCAATGCTGCAGGACAGAGGA
CTGTGGGCTGTGATCAACAATGCTGGGGTGCTTGGCTTTCCAACTGATGGGGAGCTTCTT
CTTATGACTGACTACAAACAATGCATGGCCGTGAACTTCTTTGGAACTGTGGAGGTCACA
AAGACGTTTTTGCCTCTTCTTAGAAAATCCAAAGGGAGGCTGGTGAATGTCAGCAGCATG
GGAGGAGGGGCCCCAATGGAAAGGCTGGCATCTTATGGCTCATCAAAGGCGGCTGTGACC
ATGTTCTCATCAGTTATGAGACTGGAGCTTTCCAAGTGGGGAATTAAAGTTGCTTCCATC
CAACCTGGAGGCTTCCTAACAAATATCGCAGGCACCAGTGACAAGTGGGAAAAGCTGGAG
AAGGACATTCTGGACCACCTCCCCGCTGAGGTACAGGAAGACTACGGCCAGGACTACATC
TTAGCACAGCGGAATTTCCTCCTATTGATCAACTCGTTAGCCAGCAAGGACTTCTCTCCG
GTGCTGCGGGACATCCAGCATGCTATCTTGGCGAAGAGCCCTTTTGCCTATTACACGCCA
GGGAAAGGCGCTTACTTGTGGATCTGCCTTGCTCACTATTTGCCTATTGGCATATATGAT
TACTTTGCTAAAAGACATTTTGGCCAAGACAAGCCCATGCCCAGAGCTCTAAGAATGCCT
AACTACAAGAAAAAGGCCACCTAG
Enzyme 44 GenBank Gene ID L11708 Link Image
Enzyme 44 GeneCard ID HSD17B2 Link Image
Enzyme 44 GenAtlas ID HSD17B2 Link Image
Enzyme 44 HGNC ID HGNC:5211 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 16q24.1-q24.2
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Wu L, Einstein M, Geissler WM, Chan HK, Elliston KO, Andersson S: Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity. J Biol Chem. 1993 Jun 15;268(17):12964-9. [PubMed Link Image]
  2. Labrie Y, Durocher F, Lachance Y, Turgeon C, Simard J, Labrie C, Labrie F: The human type II 17 beta-hydroxysteroid dehydrogenase gene encodes two alternatively spliced mRNA species. DNA Cell Biol. 1995 Oct;14(10):849-61. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 5691
Enzyme 45 Name Estradiol 17-beta-dehydrogenase 8
Enzyme 45 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 8
  2. 17-beta-HSD 8
  3. 3-oxoacyl-[acyl-carrier-protein] reductase
  4. Protein Ke6
  5. Ke-6
  6. Really interesting new gene 2 protein
  7. Testosterone 17-beta-dehydrogenase 8
Enzyme 45 Gene Name HSD17B8
Enzyme 45 Protein Sequence >Estradiol 17-beta-dehydrogenase 8 
MASQLQNRLRSALALVTGAGSGIGRAVSVRLAGEGATVAACDLDRAAAQETVRLLGGPGS
KEGPPRGNHAAFQADVSEARAARCLLEQVQACFSRPPSVVVSCAGITQDEFLLHMSEDDW
DKVIAVNLKGTFLVTQAAAQALVSNGCRGSIINISSIVGKVGNVGQTNYAASKAGVIGLT
QTAARELGRHGIRCNSVLPGFIATPMTQKVPQKVVDKITEMIPMGHLGDPEDVADVVAFL
ASEDSGYITGTSVEVTGGLFM
Enzyme 45 Number of Residues 261
Enzyme 45 Molecular Weight 26973.6
Enzyme 45 Theoretical pI 6.50
Enzyme 45 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 45 General Function Involved in oxidoreductase activity
Enzyme 45 Specific Function NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. Has very low activity towards testosterone. The heteroteramer with CBR4 has NADH-dependent 3- ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria
Enzyme 45 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 45 Reactions
  • testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+ [RN:R01836]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein Not Available
Enzyme 45 UniProtKB/Swiss-Prot ID Q92506 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name DHB8_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >786 bp 
ATGGCGTCTCAGCTCCAGAACCGACTCCGCTCCGCACTGGCCTTGGTCACAGGTGCGGGG
AGCGGCATCGGCCGAGCGGTCAGTGTACGCCTGGCCGGAGAGGGGGCCACCGTAGCTGCC
TGCGACCTGGACCGGGCAGCGGCACAGGAGACGGTGCGGCTGCTGGGCGGGCCAGGGAGC
AAGGAGGGGCCGCCCCGAGGGAACCATGCTGCCTTCCAGGCTGACGTGTCTGAGGCCAGG
GCCGCCAGGTGCCTGCTGGAACAAGTGCAGGCCTGCTTTTCTCGCCCACCATCTGTCGTT
GTGTCCTGTGCGGGCATCACCCAGGATGAGTTTCTGCTGCACATGTCTGAGGATGACTGG
GACAAAGTCATAGCTGTCAACCTCAAGGGCACCTTCCTAGTCACTCAGGCTGCAGCACAA
GCCCTGGTGTCCAATGGTTGTCGTGGTTCCATCATCAACATCAGTAGCATCGTAGGAAAG
GTGGGGAACGTGGGGCAGACAAACTATGCAGCATCCAAGGCTGGAGTGATTGGGCTGACC
CAGACCGCAGCCCGGGAGCTTGGACGACATGGGATCCGCTGTAACTCTGTCCTCCCAGGG
TTCATTGCAACACCCATGACACAGAAAGTGCCACAGAAAGTGGTGGACAAGATTACTGAA
ATGATCCCGATGGGACACTTGGGGGACCCTGAGGATGTGGCAGATGTGGTCGCATTCTTG
GCATCTGAAGATAGTGGATACATCACAGGGACCTCAGTGGAAGTCACTGGAGGTCTTTTC
ATGTAG
Enzyme 45 GenBank Gene ID BT007239 Link Image
Enzyme 45 GeneCard ID HSD17B8 Link Image
Enzyme 45 GenAtlas ID HSD17B8 Link Image
Enzyme 45 HGNC ID HGNC:3554 Link Image
Enzyme 45 Chromosome Location 6
Enzyme 45 Locus 6p21.3
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ando A, Kikuti YY, Shigenari A, Kawata H, Okamoto N, Shiina T, Chen L, Ikemura T, Abe K, Kimura M, Inoko H: cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the centromeric end of the human MHC region. Genomics. 1996 Aug 1;35(3):600-2. [PubMed Link Image]
  4. Ohno S, Nishikawa K, Honda Y, Nakajin S: Expression in E. coli and tissue distribution of the human homologue of the mouse Ke 6 gene, 17beta-hydroxysteroid dehydrogenase type 8. Mol Cell Biochem. 2008 Feb;309(1-2):209-15. Epub 2007 Nov 3. [PubMed Link Image]
  5. Chen Z, Kastaniotis AJ, Miinalainen IJ, Rajaram V, Wierenga RK, Hiltunen JK: 17beta-hydroxysteroid dehydrogenase type 8 and carbonyl reductase type 4 assemble as a ketoacyl reductase of human mitochondrial FAS. FASEB J. 2009 Nov;23(11):3682-91. Epub 2009 Jul 1. [PubMed Link Image]
  6. Rotinen M, Celay J, Alonso MM, Arrazola A, Encio I, Villar J: Estradiol induces type 8 17beta-hydroxysteroid dehydrogenase expression: crosstalk between estrogen receptor alpha and C/EBPbeta. J Endocrinol. 2009 Jan;200(1):85-92. Epub 2008 Oct 13. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 5738
Enzyme 46 Name 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
Enzyme 46 Synonyms
  1. 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
  2. 3-beta-HSD I
  3. Trophoblast antigen FDO161G
  4. 3-beta-hydroxy-Delta(5)-steroid dehydrogenase
  5. 3-beta-hydroxy-5-ene steroid dehydrogenase
  6. Progesterone reductase
  7. Steroid Delta-isomerase
  8. Delta-5-3-ketosteroid isomerase
Enzyme 46 Gene Name HSD3B1
Enzyme 46 Protein Sequence >4-isomerase type 1 
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLE
GDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVF
IYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTL
YTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRAL
QDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEI
VSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSL
VDRHKETLKSKTQ
Enzyme 46 Number of Residues 373
Enzyme 46 Molecular Weight 42251.2
Enzyme 46 Theoretical pI 8.98
Enzyme 46 GO Classification
Function
  • 3-beta-hydroxy-delta5-steroid dehydrogenase activity
  • binding
  • catalytic activity
  • oxidoreductase activity
  • steroid dehydrogenase activity
  • steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • steroid biosynthetic process
  • steroid metabolic process
Component
—
Enzyme 46 General Function Involved in 3-beta-hydroxy-delta5-steroid dehydrogenase activity
Enzyme 46 Specific Function 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. Efficiently catalyzes the transformation of pregnenolone to progesterone, 17-alpha-hydroxypregnenolone to 17- alpha-hydroxyprogesterone, DHEA to 4-androstenedione, dihydrotestosterone to 5-alpha-androstane-3 beta,17 beta-diol, dehydroepiandrosterone to androstenedione and 5-alpha-androstan-3 beta,17 beta-diol to 5-alpha-dihydrotestosterone
Enzyme 46 Pathways
Enzyme 46 Reactions
  • a 3-oxo-Delta5-steroid = a 3-oxo-Delta4-steroid [RN:R02644]
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • 288-308
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID P14060 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name 3BHS1_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1122 bp 
ATGACGGGCTGGAGCTGCCTTGTGACAGGAGCAGGAGGGTTTCTGGGACAGAGGATCATC
CGCCTCTTGGTGAAGGAGAAGGAGCTGAAGGAGATCAGGGTCTTGGACAAGGCCTTCGGA
CCAGAATTGAGAGAGGAATTTTCTAAACTCCAGAACAAGACCAAGCTGACAGTGCTGGAA
GGAGACATTCTGGATGAGCCATTCCTGAAGAGAGCCTGCCAGGACGTCTCGGTCATCATC
CACACCGCCTGTATCATTGATGTCTTCGGTGTCACTCACAGAGAGTCTATCATGAATGTC
AATGTGAAAGGTACCCAGCTCCTGTTAGAGGCCTGTGTCCAAGCTAGTGTGCCAGTCTTC
ATCTACACCAGTAGCATAGAGGTAGCCGGGCCCAACTCCTACAAGGAAATCATCCAGAAT
GGCCATGAAGAAGAGCCTCTGGAAAACACATGGCCCGCTCCATACCCACACAGCAAAAAG
CTTGCTGAGAAGGCTGTACTGGCGGCTAACGGGTGGAATCTGAAAAACGGCGGCACCCTG
TACACTTGTGCCTTACGACCCATGTATATCTATGGGGAAGGAAGCCGATTCCTTTCTGCT
AGTATAAACGAGGCCCTGAACAACAATGGGATCCTGTCAAGTGTTGGAAAGTTCTCCACT
GTTAACCCAGTCTATGTTGGCAATGTGGCCTGGGCCCACATTCTGGCCTTGAGGGCCCTG
CAGGACCCCAAGAAGGCCCCAAGCATCCGAGGACAGTTCTACTATATCTCAGATGACACG
CCTCACCAAAGCTATGATAACCTTAATTACACCCTGAGCAAAGAGTTCGGCCTCCGCCTT
GATTCCAGATGGAGCTTTCCTTTATCCCTGATGTATTGGATTGGCTTCCTGCTGGAAATA
GTGAGCTTCCTACTCAGGCCAATTTACACCTATCGACCGCCCTTCAACCGCCACATAGTC
ACATTGTCAAATAGCGTATTCACCTTCTCTTATAAGAAGGCTCAGCGAGATCTGGCGTAT
AAGCCACTCTACAGCTGGGAGGAAGCCAAGCAGAAAACGGTGGAGTGGGTTGGTTCCCTT
GTGGACCGGCACAAGGAGACCCTGAAGTCCAAGACTCAGTGA
Enzyme 46 GenBank Gene ID M27137 Link Image
Enzyme 46 GeneCard ID HSD3B1 Link Image
Enzyme 46 GenAtlas ID HSD3B1 Link Image
Enzyme 46 HGNC ID HGNC:5217 Link Image
Enzyme 46 Chromosome Location 1
Enzyme 46 Locus 1p13.1
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Luu The V, Lachance Y, Labrie C, Leblanc G, Thomas JL, Strickler RC, Labrie F: Full length cDNA structure and deduced amino acid sequence of human 3 beta-hydroxy-5-ene steroid dehydrogenase. Mol Endocrinol. 1989 Aug;3(8):1310-2. [PubMed Link Image]
  2. Lorence MC, Murry BA, Trant JM, Mason JI: Human 3 beta-hydroxysteroid dehydrogenase/delta 5----4isomerase from placenta: expression in nonsteroidogenic cells of a protein that catalyzes the dehydrogenation/isomerization of C21 and C19 steroids. Endocrinology. 1990 May;126(5):2493-8. [PubMed Link Image]
  3. Lorence MC, Corbin CJ, Kamimura N, Mahendroo MS, Mason JI: Structural analysis of the gene encoding human 3 beta-hydroxysteroid dehydrogenase/delta 5----4-isomerase. Mol Endocrinol. 1990 Dec;4(12):1850-5. [PubMed Link Image]
  4. Lachance Y, Luu-The V, Labrie C, Simard J, Dumont M, de Launoit Y, Guerin S, Leblanc G, Labrie F: Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase gene and its expression in mammalian cells. J Biol Chem. 1990 Nov 25;265(33):20469-75. [PubMed Link Image]
  5. Nickson DA, McBride MW, Zeinali S, Hawes CS, Petropoulos A, Mueller UW, Sutcliffe RG: Molecular cloning and expression of human trophoblast antigen FDO161G and its identification as 3 beta-hydroxy-5-ene steroid dehydrogenase. J Reprod Fertil. 1991 Sep;93(1):149-56. [PubMed Link Image]
  6. Dumont M, Luu-The V, Dupont E, Pelletier G, Labrie F: Characterization, expression, and immunohistochemical localization of 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in human skin. J Invest Dermatol. 1992 Oct;99(4):415-21. [PubMed Link Image]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 5739
Enzyme 47 Name Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Enzyme 47 Synonyms
  1. D-xylose 1-dehydrogenase
  2. D-xylose-NADP dehydrogenase
  3. Dimeric dihydrodiol dehydrogenase
  4. Hum2DD
Enzyme 47 Gene Name DHDH
Enzyme 47 Protein Sequence >Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase 
MALRWGIVSVGLISSDFTAVLQTLPRSEHQVVAVAARDLSRAKEFAQKHDIPKAYGSYEE
LAKDPSVEVAYIGTQHPQHKAAVMLCLAAGKAVLCEKPTGVNAAEVREMVAEARSRALFL
MEAIWTRFFPASEALRSVLAQGTLGDLRVARAEFGKNLIHVPRAVDRAQAGGALLDIGIY
CVQFTSMVFGGQKPEKISVVGRRHETGVDDTVTVLLQYPGEVHGSFTCSITVQLSNTASV
SGTKGMVQLLNPCWCPTELVVKGEHKEFPLPPVPKDCNFDNGAGMSYEAKHVWECLRKGM
KESPVIPLSESELLADILEEVRKAIGVTFPQDKR
Enzyme 47 Number of Residues 334
Enzyme 47 Molecular Weight 36381.7
Enzyme 47 Theoretical pI 7.22
Enzyme 47 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
Component
—
Enzyme 47 General Function Involved in catalytic activity
Enzyme 47 Specific Function Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+ [RN:R00814]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 5771250 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q9UQ10 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name DHDH_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >1005 bp 
ATGGCGCTGCGCTGGGGCATCGTGTCTGTCGGCCTCATCTCCAGCGACTTCACAGCCGTG
CTGCAGACGCTGCCTCGCTCTGAGCACCAGGTGGTGGCGGTGGCGGCCCGCGATCTGAGC
CGTGCGAAGGAGTTTGCACAGAAACACGACATCCCCAAGGCCTACGGCTCCTATGAGGAG
CTGGCCAAGGACCCGAGCGTGGAGGTGGCCTACATTGGCACCCAGCACCCCCAGCACAAG
GCGGCGGTGATGCTGTGCTTGGCGGCGGGCAAGGCCGTTCTGTGCGAGAAGCCCACGGGC
GTGAACGCGGCGGAAGTTCGCGAGATGGTCGCGGAGGCCCGATCCCGAGCCCTCTTCCTT
ATGGAGGCCATCTGGACCCGCTTCTTTCCTGCCTCCGAGGCTCTGAGGTCTGTTTTGGCC
CAGGGAACTCTAGGAGACCTCCGGGTGGCTCGGGCAGAATTTGGGAAGAATCTCATCCAC
GTTCCCCGGGCCGTAGACCGGGCCCAGGCTGGGGGGGCCCTGCTGGACATCGGCATCTAC
TGTGTCCAGTTCACCTCCATGGTCTTTGGAGGGCAGAAGCCAGAGAAGATTTCTGTCGTG
GGAAGGCGTCATGAAACAGGTGTGGATGACACTGTCACGGTGCTCCTGCAGTACCCAGGG
GAGGTCCATGGCAGCTTCACCTGCAGCATCACCGTGCAGCTCTCCAACACGGCCTCCGTG
AGCGGCACCAAGGGCATGGTACAGCTCCTCAACCCCTGCTGGTGCCCGACCGAGCTGGTG
GTGAAGGGGGAGCATAAGGAGTTCCCGCTGCCCCCAGTCCCAAAGGACTGCAATTTTGAC
AACGGGGCAGGCATGAGTTATGAGGCCAAGCACGTCTGGGAGTGCCTACGCAAGGGTATG
AAGGAAAGTCCTGTGATTCCCCTGTCGGAAAGTGAGCTCCTGGCTGACATCCTTGAAGAG
GTGAGGAAGGCCATTGGAGTCACCTTCCCCCAAGACAAACGCTGA
Enzyme 47 GenBank Gene ID AB021933 Link Image
Enzyme 47 GeneCard ID DHDH Link Image
Enzyme 47 GenAtlas ID DHDH Link Image
Enzyme 47 HGNC ID HGNC:17887 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 19q13.3
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Arimitsu E, Aoki S, Ishikura S, Nakanishi K, Matsuura K, Hara A: Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases. Biochem J. 1999 Sep 15;342 Pt 3:721-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 5749
Enzyme 48 Name Cholesterol 7-alpha-monooxygenase
Enzyme 48 Synonyms
  1. CYPVII
  2. Cholesterol 7-alpha-hydroxylase
  3. Cytochrome P450 7A1
Enzyme 48 Gene Name CYP7A1
Enzyme 48 Protein Sequence >Cholesterol 7-alpha-monooxygenase 
MMTTSLIWGIAIAACCCLWLILGIRRRQTGEPPLENGLIPYLGCALQFGANPLEFLRANQ
RKHGHVFTCKLMGKYVHFITNPLSYHKVLCHGKYFDWKKFHFATSAKAFGHRSIDPMDGN
TTENINDTFIKTLQGHALNSLTESMMENLQRIMRPPVSSNSKTAAWVTEGMYSFCYRVMF
EAGYLTIFGRDLTRRDTQKAHILNNLDNFKQFDKVFPALVAGLPIHMFRTAHNAREKLAE
SLRHENLQKRESISELISLRMFLNDTLSTFDDLEKAKTHLVVLWASQANTIPATFWSLFQ
MIRNPEAMKAATEEVKRTLENAGQKVSLEGNPICLSQAELNDLPVLDSIIKESLRLSSAS
LNIRTAKEDFTLHLEDGSYNIRKDDIIALYPQLMHLDPEIYPDPLTFKYDRYLDENGKTK
TTFYCNGLKLKYYYMPFGSGATICPGRLFAIHEIKQFLILMLSYFELELIEGQAKCPPLD
QSRAGLGILPPLNDIEFKYKFKHL
Enzyme 48 Number of Residues 504
Enzyme 48 Molecular Weight 57660.2
Enzyme 48 Theoretical pI 8.34
Enzyme 48 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
—
Component
—
Enzyme 48 General Function Involved in monooxygenase activity
Enzyme 48 Specific Function Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis
Enzyme 48 Pathways
Enzyme 48 Reactions
  • cholesterol + NADPH + H+ + O2 = 7alpha-hydroxycholesterol + NADP+ + H2O [RN:R01463]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 75517898 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID P22680 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name CP7A1_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >1515 bp 
ATGATGACCACATCTTTGATTTGGGGGATTGCTATAGCAGCATGCTGTTGTCTATGGCTT
ATTCTTGGAATTAGGAGAAGGCAAACGGGTGAACCACCTCTAGAGAATGGATTAATTCCA
TACCTGGGCTGTGCTCTGCAATTTGGTGCCAATCCTCTTGAGTTCCTCAGAGCAAATCAA
AGGAAACATGGTCATGTTTTTACCTGCAAACTAATGGGAAAATATGTCCATTTCATCACA
AATCCCTTGTCATACCATAAGGTGTTGTGCCACGGAAAATATTTTGATTGGAAAAAATTT
CACTTTGCTACTTCTGCGAAGGCATTTGGGCACAGAAGCATTGACCCGATGGATGGAAAT
ACCACTGAAAACATAAACGACACTTTCATCAAAACCCTGCAGGGCCATGCCTTGAATTCC
CTCACGGAAAGCATGATGGAAAACCTCCAACGTATCATGAGACCTCCAGTCTCCTCTAAC
TCAAAGACCGCTGCCTGGGTGACAGAAGGGATGTATTCTTTCTGCTACCGAGTGATGTTT
GAAGCTGGGTATTTAACTATCTTTGGCAGAGATCTTACAAGGCGGGACACACAGAAAGCA
CATATTCTAAACAATCTTGACAACTTCAAGCAATTCGACAAAGTCTTTCCAGCCCTGGTA
GCAGGCCTCCCCATTCACATGTTCAGGACTGCGCACAATGCCCGGGAGAAACTGGCAGAG
AGCTTGAGGCACGAGAACCTCCAAAAGAGGGAAAGCATCTCAGAACTGATCAGCCTGCGC
ATGTTTCTCAATGACACTTTGTCCACCTTTGATGATCTGGAGAAGGCCAAGACACACCTC
GTGGTCCTCTGGGCATCGCAAGCAAACACCATTCCAGCGACTTTCTGGAGTTTATTTCAA
ATGATTAGGAACCCAGAAGCAATGAAAGCAGCTACTGAAGAAGTGAAAAGAACATTAGAG
AATGCTGGTCAAAAAGTCAGCTTGGAAGGCAATCCTATTTGTTTGAGTCAAGCAGAACTG
AATGACCTGCCAGTATTAGATAGTATAATCAAGGAATCGCTGAGGCTTTCCAGTGCCTCC
CTCAACATCCGGACAGCTAAGGAGGATTTCACTTTGCACCTTGAGGACGGTTCCTACAAC
ATCCGAAAAGATGACATCATAGCTCTTTACCCACAGTTAATGCACTTAGATCCAGAAATC
TACCCAGACCCTTTGACTTTTAAATATGATAGGTATCTTGATGAAAACGGGAAGACAAAG
ACTACCTTCTATTGTAATGGACTCAAGTTAAAGTATTACTACATGCCCTTTGGATCGGGA
GCTACAATATGTCCTGGAAGATTGTTCGCTATCCACGAAATCAAGCAATTTTTGATTCTG
ATGCTTTCTTATTTTGAATTGGAGCTTATAGAGGGCCAAGCTAAATGTCCACCTTTGGAC
CAGTCCCGGGCAGGCTTGGGCATTTTGCCGCCATTGAATGATATTGAATTTAAATATAAA
TTCAAGCATTTGTGA
Enzyme 48 GenBank Gene ID BC101777 Link Image
Enzyme 48 GeneCard ID CYP7A1 Link Image
Enzyme 48 GenAtlas ID CYP7A1 Link Image
Enzyme 48 HGNC ID HGNC:2651 Link Image
Enzyme 48 Chromosome Location 8
Enzyme 48 Locus 8q11-q12
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Nishimoto M, Noshiro M, Okuda K: Structure of the gene encoding human liver cholesterol 7 alpha-hydroxylase. Biochim Biophys Acta. 1993 Feb 20;1172(1-2):147-50. [PubMed Link Image]
  2. Noshiro M, Okuda K: Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7 alpha-hydroxylase. FEBS Lett. 1990 Jul 30;268(1):137-40. [PubMed Link Image]
  3. Karam WG, Chiang JY: Polymorphisms of human cholesterol 7 alpha-hydroxylase. Biochem Biophys Res Commun. 1992 Jun 15;185(2):588-95. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wang DP, Chiang JY: Structure and nucleotide sequences of the human cholesterol 7 alpha-hydroxylase gene (CYP7). Genomics. 1994 Mar 15;20(2):320-3. [PubMed Link Image]
  6. Molowa DT, Chen WS, Cimis GM, Tan CP: Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase gene. Biochemistry. 1992 Mar 10;31(9):2539-44. [PubMed Link Image]
  7. Abrahamsson A, Gustafsson U, Ellis E, Nilsson LM, Sahlin S, Bjorkhem I, Einarsson C: Feedback regulation of bile acid synthesis in human liver: importance of HNF-4alpha for regulation of CYP7A1. Biochem Biophys Res Commun. 2005 May 6;330(2):395-9. [PubMed Link Image]
  8. Li T, Chanda D, Zhang Y, Choi HS, Chiang JY: Glucose stimulates cholesterol 7alpha-hydroxylase gene transcription in human hepatocytes. J Lipid Res. 2010 Apr;51(4):832-42. Epub 2009 Oct 28. [PubMed Link Image]
  9. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 5754
Enzyme 49 Name Alcohol dehydrogenase [NADP+]
Enzyme 49 Synonyms
  1. Aldehyde reductase
  2. Aldo-keto reductase family 1 member A1
Enzyme 49 Gene Name AKR1A1
Enzyme 49 Protein Sequence >Alcohol dehydrogenase [NADP+] 
MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEAL
KEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFER
GDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRP
AVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEK
YGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIV
PMLTVDGKRVPRDAGHPLYPFNDPY
Enzyme 49 Number of Residues 325
Enzyme 49 Molecular Weight 36572.7
Enzyme 49 Theoretical pI 6.79
Enzyme 49 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 49 General Function Involved in oxidoreductase activity
Enzyme 49 Specific Function Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4- nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D- glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN)
Enzyme 49 Pathways
Enzyme 49 Reactions
  • an alcohol + NADP+ = an aldehyde + NADPH + H+ [RN:R07328]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein Not Available
Enzyme 49 UniProtKB/Swiss-Prot ID P14550 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name AK1A1_HUMAN Link Image
Enzyme 49 PDB ID 2ALR Link Image
Enzyme 49 PDB File Show
Enzyme 49 3D Structure
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >978 bp 
ATGGCGGCTTCCTGTGTTCTACTGCACACTGGGCAGAAGATGCCTCTGATTGGTCTGGGT
ACCTGGAAGAGTGAGCCTGGTCAGGTAAAAGCAGCTGTTAAGTATGCCCTTAGCGTAGGC
TACCGCCACATTGATTGTGCTGCTATCTACGGCAATGAGCCTGAGATTGGGGAGGCCCTG
AAGGAGGACGTGGGACCAGGCAAGGCGGTGCCTCGGGAGGAGCTGTTTGTGACATCCAAG
CTGTGGAACACCAAGCACCACCCCGAGGATGTGGAGCCTGCCCTCCGGAAGACTCTGGCT
GACCTCCAGCTGGAGTATCTGGACCTGTACCTGATGCACTGGCCTTATGCCTTTGAGCGG
GGAGACAACCCCTTCCCCAAGAATGCTGATGGGACTATATGCTACGACTCCACCCACTAC
AAGGAGACTTGGAAGGCTCTGGAGGCACTGGTGGCTAAGGGGCTGGTGCAGGCGCTGGGC
CTGTCCAACTTCAACAGTCGGCAGATTGATGACATACTCAGTGTGGCCTCCGTGCGTCCA
GCTGTCTTGCAGGTGGAATGCCACCCATACTTGGCTCAAAATGAGCTAATTGCCCACTGC
CAAGCACGTGGCTTGGAGGTAACTGCTTATAGCCCTTTGGGCTCCTCTGATCGTGCATGG
CGTGATCCTGATGAGCCTGTCCTGCTGGAGGAACCAGTAGTCCTGGCATTGGCTGAAAAG
TATGGCCGATCTCCAGCTCAGATCTTGCTCAGGTGGCAGGTCCAGCGGAAAGTGATCTGC
ATCCCCAAAAGTATCACTCCTTCTCGAATCCTTCAGAACATCAAGGTGTTTGACTTCACC
TTTAGCCCAGAAGAGATGAAGCAGCTAAATGCCCTGAACAAAAATTGGAGATATATTGTG
CCTATGCTTACGGTGGATGGGAAGAGAGTCCCAAGGGATGCAGGGCATCCTCTGTACCCC
TTTAATGACCCGTACTGA
Enzyme 49 GenBank Gene ID J04794 Link Image
Enzyme 49 GeneCard ID AKR1A1 Link Image
Enzyme 49 GenAtlas ID AKR1A1 Link Image
Enzyme 49 HGNC ID HGNC:380 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 1p33-p32
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed Link Image]
  2. Fujii J, Hamaoka R, Matsumoto A, Fujii T, Yamaguchi Y, Egashira M, Miyoshi O, Niikawa N, Taniguchi N: The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33-->p32. Cytogenet Cell Genet. 1999;84(3-4):230-2. [PubMed Link Image]
  3. Barski OA, Gabbay KH, Bohren KM: Characterization of the human aldehyde reductase gene and promoter. Genomics. 1999 Sep 1;60(2):188-98. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Wermuth B, Omar A, Forster A, di Francesco C, Wolf M, von Wartburg JP, Bullock B, Gabbay KH: Primary structure of aldehyde reductase from human liver. Prog Clin Biol Res. 1987;232:297-307. [PubMed Link Image]
  8. Barski OA, Gabbay KH, Grimshaw CE, Bohren KM: Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry. 1995 Sep 5;34(35):11264-75. [PubMed Link Image]
  9. O'connor T, Ireland LS, Harrison DJ, Hayes JD: Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem J. 1999 Oct 15;343 Pt 2:487-504. [PubMed Link Image]
  10. Palackal NT, Burczynski ME, Harvey RG, Penning TM: Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1). Chem Biol Interact. 2001 Jan 30;130-132(1-3):815-24. [PubMed Link Image]
  11. Bains OS, Takahashi RH, Pfeifer TA, Grigliatti TA, Reid RE, Riggs KW: Two allelic variants of aldo-keto reductase 1A1 exhibit reduced in vitro metabolism of daunorubicin. Drug Metab Dispos. 2008 May;36(5):904-10. Epub 2008 Feb 14. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ: Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):859-68. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 5810
Enzyme 50 Name Aldehyde dehydrogenase family 3 member B2
Enzyme 50 Synonyms
  1. Aldehyde dehydrogenase 8
Enzyme 50 Gene Name ALDH3B2
Enzyme 50 Protein Sequence >Aldehyde dehydrogenase family 3 member B2 
MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSE
ISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAAT
KHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQERLL
PALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDRYIAPTVL
VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERT
SSGSFGGNEGFTYISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEKLKEI
HYPPYTDWNQQLLRWGMGSQSCTLL
Enzyme 50 Number of Residues 385
Enzyme 50 Molecular Weight 42634.6
Enzyme 50 Theoretical pI 5.86
Enzyme 50 GO Classification
Function
  • aldehyde dehydrogenase [NAD(P)+] activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • cellular aldehyde metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 50 General Function Involved in oxidoreductase activity
Enzyme 50 Specific Function An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H
Enzyme 50 Pathways
Enzyme 50 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+ [RN:R00538 R00634]
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 21751068 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID P48448 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name AL3B2_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1158 bp 
ATGGAGGATGAACCACGGTCCACGAACCTGTTCATGAAGCTGGACTCGGTCTTCATCTGG
AAGGAACCCTTTGGCCTGGTCCTCATCATCGCACCCTGGAACTACCCACTGAACCTGACC
CTGGTGCTCCTGGTGGGCGCCCTCGCCGCAGGGAATTGCGTGGTGCTGAAGCCGTCAGAA
ATCAGCCAGGGCACAGAGAAGGTCCTGGCTGAGGTGCTGCCCCAGTACCTGGACCAGAGC
TGCTTTGCCGTGGTGCTGGGCGGACCCCAGGAGACAGGGCAGCTGCTAGAGCACAAGTTG
GACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTCATGACTGCTGCCACC
AAGCACCTGACGCCTGTCACCCTGGAGCTGGGGGTCAAGAACCCCTGCTACGTGGACGAC
AACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCTGCTACTTCAATGCCGGC
CAGACCTGCGTGGCCCCTGACTACGTCCTGTGCAGCCCCGAGATGCAGGAGAGGCTGCTG
CCCGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCAAAC
CTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGCGGC
CGCGTGGCCATTGGGGGCCAGAGCAACGAGAGCGATCGCTACATCGCCCCCACGGTGCTG
GTGGACGTGCAGGAGACGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTGCCC
ATCGTGAACGTGCAGAGCGTGGACGAGGCCATCAAGTTCATCAACCGGCAGGAGAAGCCC
CTGGCCCTGTACGCCTTCTCCAACAGCAGCCAGGTTGTGAACCAGATGCTGGAGCGGACC
AGCAGCGGCAGCTTTGGAGGCAATGAGGGCTTCACCTACATATCTCTGCTGTCCGTGCCA
TTCGGGGGAGTCGGCCACAGTGGGATGGGCCGGTACCACGGCAAGTTCACCTTCGACACC
TTCTCCCACCACCGCACCTGCCTGCTCGCCCCCTCCGGCCTGGAGAAATTAAAGGAGATC
CGCTACCCACCCTATACCGACTGGAACCAGCAGCTGTTACGCTGGGGCATGGGCTCCCAG
AGCTGCACCCTCCTGTGA
Enzyme 50 GenBank Gene ID AK092464 Link Image
Enzyme 50 GeneCard ID ALDH3B2 Link Image
Enzyme 50 GenAtlas ID ALDH3B2 Link Image
Enzyme 50 HGNC ID HGNC:411 Link Image
Enzyme 50 Chromosome Location 1
Enzyme 50 Locus 11q13
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Hsu LC, Chang WC, Lin SW, Yoshida A: Cloning and characterization of genes encoding four additional human aldehyde dehydrogenase isozymes. Adv Exp Med Biol. 1995;372:159-68. [PubMed Link Image]
  2. Hsu LC, Chang WC: Sequencing and expression of the human ALDH8 encoding a new member of the aldehyde dehydrogenase family. Gene. 1996 Oct 3;174(2):319-22. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 5819
Enzyme 51 Name 7-dehydrocholesterol reductase
Enzyme 51 Synonyms
  1. 7-DHC reductase
  2. Putative sterol reductase SR-2
  3. Sterol Delta(7)-reductase
Enzyme 51 Gene Name DHCR7
Enzyme 51 Protein Sequence >7-dehydrocholesterol reductase 
MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMA
CDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHK
FLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPL
LWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFN
GRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHD
HFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDL
FRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCL
ACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF
Enzyme 51 Number of Residues 475
Enzyme 51 Molecular Weight 54489.0
Enzyme 51 Theoretical pI 8.82
Enzyme 51 GO Classification
Function
—
Process
—
Component
  • cell part
  • membrane
Enzyme 51 General Function Involved in 7-dehydrocholesterol reductase activity
Enzyme 51 Specific Function Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC)
Enzyme 51 Pathways
Enzyme 51 Reactions
  • cholesterol + NADP+ = cholesta-5,7-dien-3beta-ol + NADPH + H+ [RN:R01456]
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • 40-60 154-174 177-197 266-286 306-326 331-351 420-440
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 4191398 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q9UBM7 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name DHCR7_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >1428 bp 
ATGGCTGCAAAATCGCAACCCAACATTCCCAAAGCCAAGAGTCTAGATGGCGTCACCAAT
GACAGAACCGCATCTCAAGGGCAGTGGGGCCGTGCCTGGGAGGTGGACTGGTTTTCACTG
GCGAGCGTCATCTTCCTACTGCTGTTCGCCCCCTTCATCGTCTACTACTTCATCATGGCT
TGTGACCAATACAGCTGCGCCCTGACCGGCCCTGTGGTGGACATCGTCACCGGACATGCT
CGGCTCTCGGACATCTGGGCCAAGACTCCACCTATAACGAGGAAAGCCGCCCAGCTCTAT
ACCTTGTGGGTCACCTTCCAGGTGCTTCTGTACACGTCTCTCCCTGACTTCTGCCATAAG
TTTCTACCCGGCTACGTAGGAGGCATCCAGGAGGGGGCCGTGACTCCTGCAGGGGTTGTG
AACAAGTATCAGATCAACGGCCTGCAAGCCTGGCTCCTCACGCACCTGCTCTGGTTTGCA
AACGCTCATCTCCTGTCCTGGTTCTCGCCCACCATCATCTTCGACAACTGGATCCCACTG
CTGTGGTGCGCCAACATCCTTGGCTATGCCGTCTCCACCTTCGCCATGGTCAAGGGCTAC
TTCTTCCCCACCAGCGCCAGAGACTGCAAATTCACAGGCAATTTCTTTTACAACTACATG
ATGGGCATCGAGTTTAACCCTCGGATCGGGAAGTGGTTTGACTTCAAGCTGTTCTTCAAT
GGGCGCCCCGGGATCGTCGCCTGGACCCTCATCAACCTGTCCTTCGCAGCGAAGCAGCGG
GAGCTCCACAGCCATGTGACCAATGCCATGGTCCTGGTCAACGTCCTGCAGGCCATCTAC
GTGATTGACTTCTTCTGGAACGAAACCTGGTACCTGAAGACCATTGACATCTGCCATGAC
CACTTCGGGTGGTACCTGGGCTGGGGCGACTGTGTCTGGCTGCCTTATCTTTACACGCTG
CAGGGTCTGTACTTGGTGTACCACCCCGTGCAGCTGTCCACCCCGCACGCCGTGGGCGTC
CTGCTGCTGGGCCTGGTGGGCTACTACATCTTCCGGGTGGCCAACCACCAGAAGGACCTG
TTCCGCCGCACGGATGGGCGCTGCCTCATCTGGGGCAGGAAGCCCAAGGTCATCGAGTGC
TCCTACACATCCGCCGACGGGCAGAGGCACCACAGCAAGCTGCTGGTGTCGGGCTTCTGG
GGCGTGGCCCGCCACTTCAACTACGTCGGCGACCTGATGGGCAGCCTGGCCTACTGCCTG
GCCTGTGGCGGTGGCCACCTGCTGCCCTACTTCTACATCATCTACATGGCCATCCTGCTG
ACCCACCGCTGCCTCCGGGACGAGCACCGCTGCGCCAGCAAGTACGGCCGGGACTGGGAG
CGCTACACCGCCGCAGTGCCTTACCGCCTGCTGCCTGGAATCTTCTAA
Enzyme 51 GenBank Gene ID AF096305 Link Image
Enzyme 51 GeneCard ID DHCR7 Link Image
Enzyme 51 GenAtlas ID DHCR7 Link Image
Enzyme 51 HGNC ID HGNC:2860 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 11q13.4
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Waterham HR, Wijburg FA, Hennekam RC, Vreken P, Poll-The BT, Dorland L, Duran M, Jira PE, Smeitink JA, Wevers RA, Wanders RJ: Smith-Lemli-Opitz syndrome is caused by mutations in the 7-dehydrocholesterol reductase gene. Am J Hum Genet. 1998 Aug;63(2):329-38. [PubMed Link Image]
  2. Moebius FF, Fitzky BU, Lee JN, Paik YK, Glossmann H: Molecular cloning and expression of the human delta7-sterol reductase. Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1899-902. [PubMed Link Image]
  3. Holmer L, Pezhman A, Worman HJ: The human lamin B receptor/sterol reductase multigene family. Genomics. 1998 Dec 15;54(3):469-76. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wassif CA, Maslen C, Kachilele-Linjewile S, Lin D, Linck LM, Connor WE, Steiner RD, Porter FD: Mutations in the human sterol delta7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome. Am J Hum Genet. 1998 Jul;63(1):55-62. [PubMed Link Image]
  6. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. Fitzky BU, Witsch-Baumgartner M, Erdel M, Lee JN, Paik YK, Glossmann H, Utermann G, Moebius FF: Mutations in the Delta7-sterol reductase gene in patients with the Smith-Lemli-Opitz syndrome. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8181-6. [PubMed Link Image]
  11. Witsch-Baumgartner M, Fitzky BU, Ogorelkova M, Kraft HG, Moebius FF, Glossmann H, Seedorf U, Gillessen-Kaesbach G, Hoffmann GF, Clayton P, Kelley RI, Utermann G: Mutational spectrum in the Delta7-sterol reductase gene and genotype-phenotype correlation in 84 patients with Smith-Lemli-Opitz syndrome. Am J Hum Genet. 2000 Feb;66(2):402-12. [PubMed Link Image]
  12. Krakowiak PA, Nwokoro NA, Wassif CA, Battaile KP, Nowaczyk MJ, Connor WE, Maslen C, Steiner RD, Porter FD: Mutation analysis and description of sixteen RSH/Smith-Lemli-Opitz syndrome patients: polymerase chain reaction-based assays to simplify genotyping. Am J Med Genet. 2000 Sep 18;94(3):214-27. [PubMed Link Image]
  13. Jira PE, Wanders RJ, Smeitink JA, De Jong J, Wevers RA, Oostheim W, Tuerlings JH, Hennekam RC, Sengers RC, Waterham HR: Novel mutations in the 7-dehydrocholesterol reductase gene of 13 patients with Smith--Lemli--Opitz syndrome. Ann Hum Genet. 2001 May;65(Pt 3):229-36. [PubMed Link Image]
  14. Witsch-Baumgartner M, Ciara E, Loffler J, Menzel HJ, Seedorf U, Burn J, Gillessen-Kaesbach G, Hoffmann GF, Fitzky BU, Mundy H, Clayton P, Kelley RI, Krajewska-Walasek M, Utermann G: Frequency gradients of DHCR7 mutations in patients with Smith-Lemli-Opitz syndrome in Europe: evidence for different origins of common mutations. Eur J Hum Genet. 2001 Jan;9(1):45-50. [PubMed Link Image]
  15. Langius FA, Waterham HR, Romeijn GJ, Oostheim W, de Barse MM, Dorland L, Duran M, Beemer FA, Wanders RJ, Poll-The BT: Identification of three patients with a very mild form of Smith-Lemli-Opitz syndrome. Am J Med Genet A. 2003 Sep 15;122(1):24-9. [PubMed Link Image]
  16. Waye JS, Krakowiak PA, Wassif CA, Sterner AL, Eng B, Nakamura LM, Nowaczyk MJ, Porter FD: Identification of nine novel DHCR7 missense mutations in patients with Smith-Lemli-Opitz syndrome (SLOS). Hum Mutat. 2005 Jul;26(1):59. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 5822
Enzyme 52 Name 3-oxo-5-beta-steroid 4-dehydrogenase
Enzyme 52 Synonyms
  1. Aldo-keto reductase family 1 member D1
  2. Delta(4)-3-ketosteroid 5-beta-reductase
  3. Delta(4)-3-oxosteroid 5-beta-reductase
Enzyme 52 Gene Name AKR1D1
Enzyme 52 Protein Sequence >3-oxo-5-beta-steroid 4-dehydrogenase 
MDLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQN
EHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIE
VPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELIL
NKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLK
DALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE
ALNKNVRFVELLMWRDHPEYPFHDEY
Enzyme 52 Number of Residues 326
Enzyme 52 Molecular Weight 37376.6
Enzyme 52 Theoretical pI 7.58
Enzyme 52 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 52 General Function Involved in oxidoreductase activity
Enzyme 52 Specific Function Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7- alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4- cholesten-3-one can also act as substrates
Enzyme 52 Pathways
Enzyme 52 Reactions
  • (1) 5beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+ [RN:R02609]
  • (2) 17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH + H+ [RN:R02893]
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 431857 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID P51857 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name AK1D1_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >981 bp 
ATGGATCTCAGTGCTGCAAGTCACCGCATACCTCTAAGTGATGGAAACAGCATTCCCATC
ATCGGACTTGGTACCTACTCAGAACCTAAATCGACCCCTAAGGGAGCCTGTGCAACATCG
GTGAAGGTTGCTATTGACACAGGGTACCGACATATTGATGGGGCCTACATCTACCAAAAT
GAACACGAAGTTGGGGAGGCCATCAGGGAGAAGATAGCAGAAGGAAAGGTGCGGAGGGAA
GATATCTTCTACTGTGGAAAGCTATGGGCTACAAATCATGTCCCAGAGATGGTCCGCCCA
ACCCTGGAGAGGACACTCAGGGTCCTCCAGCTAGATTATGTGGATCTTTACATCATTGAA
GTACCCATGGCCTTTAAGCCAGGAGATGAAATATACCCTAGAGATGAGAATGGCAAATGG
TTATATCACAAGTCAAATCTGTGTGCCACTTGGGAGGCGATGGAAGCTTGCAAAGACGCT
GGCTTGGTGAAATCCCTGGGAGTGTCCAATTTTAACCGCAGGCAGCTGGAGCTCATCCTG
AACAAGCCAGGACTCAAACACAAGCCAGTCAGCAACCAGGTTGAGTGCCATCCGTATTTC
ACCCAGCCAAAACTCTTGAAATTTTGCCAACAACATGACATTGTCATTACTGCATATAGC
CCTTTGGGGACCAGTAGGAATCCAATCTGGGTGAATGTTTCTTCTCCACCTTTGTTAAAG
GATGCACTTCTAAACTCATTGGGGAAAAGGTACAATAAGACAGCAGCTCAAATTGTTTTG
CGTTTCAACATCCAGCGAGGGGTGGTTGTCATTCCTAAAAGCTTTAATCTTGAAAGGATC
AAAGAAAATTTTCAGATCTTTGACTTTTCTCTCACTGAAGAAGAAATGAAGGACATTGAA
GCCTTGAATAAAAATGTCCGCTTTGTAGAATTGCTCATGTGGCGCGATCATCCTGAATAC
CCATTTCATGATGAATACTGA
Enzyme 52 GenBank Gene ID Z28339 Link Image
Enzyme 52 GeneCard ID AKR1D1 Link Image
Enzyme 52 GenAtlas ID AKR1D1 Link Image
Enzyme 52 HGNC ID HGNC:388 Link Image
Enzyme 52 Chromosome Location 7
Enzyme 52 Locus 7q32-q33
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Kondo KH, Kai MH, Setoguchi Y, Eggertsen G, Sjoblom P, Setoguchi T, Okuda KI, Bjorkhem I: Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme. Eur J Biochem. 1994 Jan 15;219(1-2):357-63. [PubMed Link Image]
  2. Charbonneau A, The VL: Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim Biophys Acta. 2001 Jan 26;1517(2):228-35. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Di Costanzo L, Drury JE, Penning TM, Christianson DW: Crystal structure of human liver Delta4-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis. J Biol Chem. 2008 Jun 13;283(24):16830-9. Epub 2008 Apr 11. [PubMed Link Image]
  7. Lemonde HA, Custard EJ, Bouquet J, Duran M, Overmars H, Scambler PJ, Clayton PT: Mutations in SRD5B1 (AKR1D1), the gene encoding delta(4)-3-oxosteroid 5beta-reductase, in hepatitis and liver failure in infancy. Gut. 2003 Oct;52(10):1494-9. [PubMed Link Image]
  8. Gonzales E, Cresteil D, Baussan C, Dabadie A, Gerhardt MF, Jacquemin E: SRD5B1 (AKR1D1) gene analysis in delta(4)-3-oxosteroid 5beta-reductase deficiency: evidence for primary genetic defect. J Hepatol. 2004 Apr;40(4):716-8. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 5939
Enzyme 53 Name Glutamate dehydrogenase 2, mitochondrial
Enzyme 53 Synonyms
  1. GDH 2
Enzyme 53 Gene Name GLUD2
Enzyme 53 Protein Sequence >Glutamate dehydrogenase 2, mitochondrial 
MYRYLAKALLPSRAGPAALGSAANHSAALLGRGRGQPAAASQPGLALAARRHYSELVADR
EDDPNFFKMVEGFFDRGASIVEDKLVKDLRTQESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTENELEKITRRFTMELAKKGFIGPGVDVPAPDMNTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFR
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLLSVQESLERKFGK
HGGTIPIVPTAEFQDSISGASEKDIVHSALAYTMERSARQIMHTAMKYNLGLDLRTAAYV
NAIEKVFKVYSEAGVTFT
Enzyme 53 Number of Residues 558
Enzyme 53 Molecular Weight 61433.5
Enzyme 53 Theoretical pI 8.67
Enzyme 53 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 53 General Function Involved in oxidoreductase activity
Enzyme 53 Specific Function Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission
Enzyme 53 Pathways
Enzyme 53 Reactions
  • L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+ [RN:R00243 R00248]
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID P49448 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name DHE4_HUMAN Link Image
Enzyme 53 PDB ID 1L1F Link Image
Enzyme 53 PDB File Show
Enzyme 53 3D Structure
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >1677 bp 
ATGTACCGCTACCTGGCCAAAGCGCTGCTGCCGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCCGCGGCCAACCACTCGGCCGCGTTGCTGGGCCGGGGCCGCGGACAGCCCGCCGCCGCC
TCGCAGCCGGGGCTCGCATTGGCCGCCCGGCGCCACTACAGCGAGTTGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGTTGGTGAAGGACCTGAGGACCCAGGAAAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACCGAAAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAGAAGGGCTTTATTGGTCCTGGCGTTGAT
GTGCCTGCTCCAGACATGAACACAGGTGAGCGGGAGATGTCCTGGATTGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAACTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTAGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGTCGACTGTGACATACTGATC
CCAGCTGCCACTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGATAAGATCTTCCTGGAGAGA
AACATTTTGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCCTGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGTATATCGGGTGCA
TCTGAGAAAGACATTGTGCACTCTGCCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCACACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTC
AATGCCATTGAAAAAGTCTTCAAAGTGTACAGTGAAGCTGGTGTGACCTTCACATAG
Enzyme 53 GenBank Gene ID AK313356 Link Image
Enzyme 53 GeneCard ID GLUD2 Link Image
Enzyme 53 GenAtlas ID GLUD2 Link Image
Enzyme 53 HGNC ID HGNC:4336 Link Image
Enzyme 53 Chromosome Location Not Available
Enzyme 53 Locus Not Available
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Shashidharan P, Michaelidis TM, Robakis NK, Kresovali A, Papamatheakis J, Plaitakis A: Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene. J Biol Chem. 1994 Jun 17;269(24):16971-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 5951
Enzyme 54 Name GMP reductase 2
Enzyme 54 Synonyms
  1. Guanosine 5'-monophosphate oxidoreductase 2
  2. Guanosine monophosphate reductase 2
Enzyme 54 Gene Name GMPR2
Enzyme 54 Protein Sequence >GMP reductase 2 
MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGT
FEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI
PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGI
GPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM
LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGD
VEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC
Enzyme 54 Number of Residues 348
Enzyme 54 Molecular Weight 37874.1
Enzyme 54 Theoretical pI 7.25
Enzyme 54 GO Classification
Function
  • GMP reductase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
Component
—
Enzyme 54 General Function Involved in catalytic activity
Enzyme 54 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation
Enzyme 54 Pathways
Enzyme 54 Reactions
  • inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH + H+ [RN:R01134]
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein Not Available
Enzyme 54 UniProtKB/Swiss-Prot ID Q9P2T1 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name GMPR2_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >1047 bp 
ATGCCTCATATTGACAACGATGTGAAACTGGACTTCAAGGATGTCCTTTTGAGGCCCAAA
CGCAGTACCCTTAAGTCTCGAAGTGAGGTGGATCTCACAAGATCCTTTTCATTTCGGAAC
TCAAAGCAGACATACTCTGGGGTTCCCATCATTGCTGCCAATATGGATACTGTGGGCACC
TTTGAGATGGCCAAGGTTCTCTGTAAGTTCTCTCTCTTCACTGCTGTCCATAAGCACTAT
AGCCTCGTTCAGTGGCAAGAGTTTGCTGGCCAGAATCCTGACTGTCTTGAGCATCTGGCT
GCCAGCTCAGGCACAGGCTCTTCTGACTTTGAGCAGCTGGAACAGATCCTGGAAGCTATT
CCCCAGGTGAAGTATATATGCCTGGATGTGGCAAATGGCTACTCTGAACACTTTGTTGAA
TTTGTAAAAGATGTACGGAAGCGCTTCCCCCAGCACACCATCATGGCAGGGAATGTGGTA
ACAGGAGAGATGGTAGAAGAGCTCATCCTTTCTGGGGCTGACATCATCAAAGTGGGAATT
GGGCCAGGCTCTGTGTGTACTACTCGGAAGAAAACTGGAGTGGGGTATCCACAGCTCAGC
GCAGTGATGGAGTGTGCAGATGCTGCTCATGGCCTCAAAGGCCACATCATTTCAGATGGA
GGTTGCAGCTGTCCTGGGGATGTGGCCAAGGCTTTTGGGGCAGGAGCTGACTTCGTGATG
CTGGGTGGCATGCTGGCTGGGCACAGTGAGTCAGGTGGTGAGCTCATCGAGAGGGATGGC
AAGAAGTACAAGCTCTTCTATGGAATGAGTTCTGAAATGGCCATGAAGAAGTATGCTGGG
GGCGTGGCTGAGTACAGAGCCTCAGAGGGAAAGACAGTGGAAGTTCCTTTTAAAGGAGAT
GTGGAACATACCATCCGAGACATCCTAGGAGGGATCCGCTCTACGTGTACCTATGTGGGA
GCAGCTAAGCTCAAAGAGTTGAGCAGGAGAACTACCTTCATCCGAGTCACCCAGCAGGTG
AATCCAATCTTCAGTGAGGCGTGCTAG
Enzyme 54 GenBank Gene ID AF419346 Link Image
Enzyme 54 GeneCard ID GMPR2 Link Image
Enzyme 54 GenAtlas ID GMPR2 Link Image
Enzyme 54 HGNC ID HGNC:4377 Link Image
Enzyme 54 Chromosome Location 1
Enzyme 54 Locus 14q12
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y: NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. Int J Biochem Cell Biol. 2002 Sep;34(9):1035-50. [PubMed Link Image]
  2. Zhang J, Zhang W, Zou D, Chen G, Wan T, Zhang M, Cao X: Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells. J Cancer Res Clin Oncol. 2003 Feb;129(2):76-83. Epub 2003 Mar 1. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 5958
Enzyme 55 Name GMP reductase 1
Enzyme 55 Synonyms
  1. Guanosine 5'-monophosphate oxidoreductase 1
  2. Guanosine monophosphate reductase 1
Enzyme 55 Gene Name GMPR
Enzyme 55 Protein Sequence >GMP reductase 1 
MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGT
FEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAV
PQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGV
GPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVM
LGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGD
VENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
Enzyme 55 Number of Residues 345
Enzyme 55 Molecular Weight 37418.6
Enzyme 55 Theoretical pI 7.08
Enzyme 55 GO Classification
Function
  • GMP reductase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
Component
—
Enzyme 55 General Function Involved in catalytic activity
Enzyme 55 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides
Enzyme 55 Pathways
Enzyme 55 Reactions
  • inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH + H+ [RN:R01134]
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 56001065 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID P36959 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name GMPR1_HUMAN Link Image
Enzyme 55 PDB ID 2BLE Link Image
Enzyme 55 PDB File Show
Enzyme 55 3D Structure
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1038 bp 
ATGCCCCGCATAGATGCGGACCTCAAGCTCGACTTCAAGGATGTCCTGCTCCGACCTAAG
CGGAGCAGCCTCAAGAGCCGAGCCGAGGTGGATCTTGAACGCACCTTCACGTTTCGAAAT
TCAAAGCAGACCTACTCAGGGATTCCCATCATCGTGGCCAACATGGACACTGTGGGCACG
TTTGAGATGGCAGCCGTGATGTCACAGCACTCCATGTTTACAGCAATTCATAAGCATTAC
TCCCTGGATGACTGGAAGCTCTTTGCCACAAATCACCCAGAATGCCTGCAGAATGTAGCC
GTGAGTTCAGGCAGTGGGCAGAATGATCTGGAAAAGATGACCAGCATCCTGGAAGCTGTG
CCACAGGTTAAGTTTATTTGCCTGGATGTGGCCAATGGGTATTCAGAACATTTTGTGGAA
TTCGTGAAACTTGTCCGTGCCAAATTTCCTGAACACACCATTATGGCAGGGAACGTGGTG
ACAGGAGAAATGGTAGAAGAGCTTATTCTTTCCGGAGCAGATATCATCAAAGTGGGAGTT
GGACCAGGTTCTGTGTGCACCACCCGCACCAAGACGGGAGTGGGGTACCCCCAGCTGAGT
GCCGTCATTGAGTGTGCCGACTCTGCCCATGGCCTGAAGGGCCACATCATCTCTGATGGA
GGCTGTACGTGTCCAGGGGATGTCGCCAAAGCCTTTGGAGCTGGAGCAGATTTTGTCATG
CTGGGAGGAATGTTTTCGGGTCATACGGAGTGTGCTGGAGAAGTGTTTGAGAGGAACGGA
CGGAAGCTCAAGCTCTTCTACGGGATGAGCTCTGACACCGCCATGAACAAGCACGCAGGA
GGAGTTGCTGAGTACAGAGCCTCTGAGGGTAAGACTGTGGAAGTTCCTTACAAAGGAGAT
GTGGAAAACACTATCCTGGATATTCTCGGGGGACTGAGGTCCACGTGCACCTACGTGGGG
GCCGCCAAACTCAAGGAGCTCAGCAGGAGGGCAACATTCATCCGGGTGACCCAGCAGCAC
AACACCGTGTTCAGCTAA
Enzyme 55 GenBank Gene ID AL009031 Link Image
Enzyme 55 GeneCard ID GMPR Link Image
Enzyme 55 GenAtlas ID GMPR Link Image
Enzyme 55 HGNC ID HGNC:4376 Link Image
Enzyme 55 Chromosome Location 6
Enzyme 55 Locus 6p23
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. [PubMed Link Image]
  2. Kondoh T, Kanno H, Chang L, Yoshida A: Genomic structure and expression of human guanosine monophosphate reductase. Hum Genet. 1991 Dec;88(2):219-24. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Henikoff S, Smith JM: The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase. Cell. 1989 Sep 22;58(6):1021-2. [PubMed Link Image]
  6. Yoshida A, Kan YW: Origin of "fused" glucose-6-phosphate dehydrogenase. Cell. 1990 Jul 13;62(1):11-2. [PubMed Link Image]
  7. Kondoh T, Kanno H, Chang LF, Yoshida A: Identification of common variant alleles of the human guanosine monophosphate reductase gene. Hum Genet. 1991 Dec;88(2):225-7. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 5962
Enzyme 56 Name Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
Enzyme 56 Synonyms
  1. Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
  2. GAPDH-2
  3. Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
Enzyme 56 Gene Name GAPDHS
Enzyme 56 Protein Sequence >Glyceraldehyde-3-phosphate dehydrogenase, testis-specific 
MSKRDIVLTNVTVVQLLRQPCPVTRAPPPPEPKAEVEPQPQPEPTPVREEIKPPPPPLPP
HPATPPPKMVSVARELTVGINGFGRIGRLVLRACMEKGVKVVAVNDPFIDPEYMVYMFKY
DSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAAS
DHISAGAQRVVISAPSPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAKVIHERF
GIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKL
TGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLG
DTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSRDK
Enzyme 56 Number of Residues 408
Enzyme 56 Molecular Weight 44500.8
Enzyme 56 Theoretical pI 8.34
Enzyme 56 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • glyceraldehyde-3-phosphate dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • small molecule metabolic process
Component
—
Enzyme 56 General Function Involved in glyceraldehyde-3-phosphate dehydrogenase activity
Enzyme 56 Specific Function May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility
Enzyme 56 Pathways
Enzyme 56 Reactions
  • D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+ [RN:R01061]
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 3046742 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID O14556 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name G3PT_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >1227 bp 
ATGTCGAAGCGCGACATCGTCCTCACCAATGTCACCGTTGTCCAGTTGCTGCGACAGCCG
TGCCCGGTGACCAGAGCACCGCCCCCACCTGAGCCTAAGGCTGAAGTAGAGCCCCAGCCA
CAACCAGAGCCCACACCAGTCAGGGAGGAAATAAAGCCACCACCGCCACCACTGCCTCCT
CACCCCGCTACTCCTCCTCCTAAGATGGTGTCTGTGGCCCGGGAGCTGACTGTGGGCATC
AATGGATTTGGACGCATCGGTCGCCTGGTCCTGCGCGCCTGCATGGAGAAGGGTGTTAAG
GTGGTGGCTGTGAATGATCCATTCATTGACCCGGAATACATGGTGTACATGTTTAAGTAT
GACTCCACCCACGGCCGATACAAGGGAAGTGTGGAATTCAGGAATGGACAACTGGTCGTG
GACAACCATGAGATCTCTGTCTACCAGTGCAAAGAGCCCAAACAGATCCCCTGGAGGGCT
GTCGGGAGCCCCTACGTGGTGGAGTCCACAGGCGTGTACCTCTCCATACAGGCAGCTTCG
GACCACATCTCTGCAGGTGCTCAACGTGTGGTCATCTCCGCGCCCTCACCGGATGCACCA
ATGTTCGTCATGGGTGTCAATGAAAATGACTATAACCCTGGCTCCATGAACATTGTGAGC
AACGCGTCCTGCACCACCAACTGTTTGGCTCCCCTCGCCAAAGTCATCCACGAGCGATTT
GGGATCGTGGAAGGGTTGATGACCACAGTCCATTCCTACACGGCCACCCAGAAGACAGTG
GACGGGCCATCAAGGAAGGCCTGGCGAGATGGGCGGGGTGCCCACCAGAACATCATCCCA
GCCTCCACTGGGGCTGCGAAAGCTGTGACCAAAGTCATCCCAGAGCTCAAAGGGAAGCTG
ACAGGGATGGCGTTCCGGGTACCAACCCCGGATGTGTCTGTCGTGGACCTGACCTGCCGC
CTCGCCCAGCCTGCCCCCTACTCAGCCATCAAGGAGGCTGTAAAAGCAGCAGCCAAGGGG
CCCATGGCTGGCATCCTTGCCTACACCGAGGATGAGGTCGTCTCTACGGACTTCCTCGGT
GATACCCACTCGTCCATCTTCGATGCTAAGGCCGGCATTGCGCTCAATGACAATTTCGTG
AAGCTCATTTCATGGTACGACAACGAATATGGCTACAGTCACCGGGTGGTCGACCTCCTC
CGCTACATGTTCAGCCGAGACAAGTGA
Enzyme 56 GenBank Gene ID AJ005371 Link Image
Enzyme 56 GeneCard ID GAPDHS Link Image
Enzyme 56 GenAtlas ID GAPDHS Link Image
Enzyme 56 HGNC ID HGNC:24864 Link Image
Enzyme 56 Chromosome Location 1
Enzyme 56 Locus 19q13.12
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Welch JE, Brown PL, O'Brien DA, Magyar PL, Bunch DO, Mori C, Eddy EM: Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J Androl. 2000 Mar-Apr;21(2):328-38. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Neuhaus EM, Mashukova A, Barbour J, Wolters D, Hatt H: Novel function of beta-arrestin2 in the nucleus of mature spermatozoa. J Cell Sci. 2006 Aug 1;119(Pt 15):3047-56. Epub 2006 Jul 4. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 5967
Enzyme 57 Name Glutamate dehydrogenase 1, mitochondrial
Enzyme 57 Synonyms
  1. GDH 1
Enzyme 57 Gene Name GLUD1
Enzyme 57 Protein Sequence >Glutamate dehydrogenase 1, mitochondrial 
MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR
EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK
HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV
NAIEKVFKVYNEAGVTFT
Enzyme 57 Number of Residues 558
Enzyme 57 Molecular Weight 61397.3
Enzyme 57 Theoretical pI 7.91
Enzyme 57 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 57 General Function Involved in oxidoreductase activity
Enzyme 57 Specific Function May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate
Enzyme 57 Pathways
Enzyme 57 Reactions
  • L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+ [RN:R00243 R00248]
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 31707 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID P00367 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name DHE3_HUMAN Link Image
Enzyme 57 PDB ID 1L1F Link Image
Enzyme 57 PDB File Show
Enzyme 57 3D Structure
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1677 bp 
ATGTACCGCTACCTGGGCGAAGCGCTGTTGCTGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCGGCGTCCGCCGACTCGGCCGCGTTGCTGGGCTGGGCCCGGGGACAGCCCGCCGCCGCC
CCGCAGCCGGGGCTGGCATTGGCCGCCCGGCGCCACTACAGCGAGGCGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGCTGGTGGAGGACCTGAGGACCCGGGAGAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACTGATAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAAAAGGGCTTTATTGGTCCTGGCATTGAT
GTGCCTGCTCCAGACATGAGCACAGGTGAGCGGGAGATGTCCTGGATCGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAATTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTGGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGCCGACTGTGACATACTGATC
CCAGCTGCCAGTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGACAAGATCTTCCTGGAGAGA
AACATTATGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCATGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGGATATCGGGTGCA
TCTGAGAAAGACATCGTGCACTCTGGCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCGCACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTT
AATGCCATTGAGAAAGTCTTCAAAGTGTACAATGAAGCTGGTGTGACCTTCACATAG
Enzyme 57 GenBank Gene ID X07674 Link Image
Enzyme 57 GeneCard ID GLUD1 Link Image
Enzyme 57 GenAtlas ID GLUD1 Link Image
Enzyme 57 HGNC ID HGNC:4335 Link Image
Enzyme 57 Chromosome Location 1
Enzyme 57 Locus 10q23.3
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10. [PubMed Link Image]
  2. Amuro N, Yamaura M, Goto Y, Okazaki T: Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. Biochem Biophys Res Commun. 1988 May 16;152(3):1395-400. [PubMed Link Image]
  3. Nakatani Y, Schneider M, Banner C, Freese E: Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 1988 Jul 11;16(13):6237. [PubMed Link Image]
  4. Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N: Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc Natl Acad Sci U S A. 1988 May;85(10):3494-8. [PubMed Link Image]
  5. Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J: The human glutamate dehydrogenase gene family: gene organization and structural characterization. Genomics. 1993 Apr;16(1):150-60. [PubMed Link Image]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Julliard JH, Smith EL: Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem. 1979 May 10;254(9):3427-38. [PubMed Link Image]
  9. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  10. Banner C, Silverman S, Thomas JW, Lampel KA, Vitkovic L, Huie D, Wenthold RJ: Isolation of a human brain cDNA for glutamate dehydrogenase. J Neurochem. 1987 Jul;49(1):246-52. [PubMed Link Image]
  11. Tzimagiorgis G, Leversha MA, Chroniary K, Goulielmos G, Sargent CA, Ferguson-Smith M, Moschonas NK: Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. Hum Genet. 1993 Jun;91(5):433-8. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  15. Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA: Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol. 2001 Mar 23;307(2):707-20. [PubMed Link Image]
  16. Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA: Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J. 2002 Apr 1;363(Pt 1):81-7. [PubMed Link Image]
  17. Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA: The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. [PubMed Link Image]
  18. Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ: Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry. 2003 Apr 1;42(12):3446-56. [PubMed Link Image]
  19. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed Link Image]
  20. Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M: Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7. [PubMed Link Image]
  21. Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y: Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. [PubMed Link Image]
  22. Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J: Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. [PubMed Link Image]
  23. MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA: Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 5968
Enzyme 58 Name Glyceraldehyde-3-phosphate dehydrogenase
Enzyme 58 Synonyms
  1. GAPDH
Enzyme 58 Gene Name GAPDH
Enzyme 58 Protein Sequence >Glyceraldehyde-3-phosphate dehydrogenase 
MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTV
KAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVI
ISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHA
ITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV
SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAG
IALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE
Enzyme 58 Number of Residues 335
Enzyme 58 Molecular Weight 36053.0
Enzyme 58 Theoretical pI 8.73
Enzyme 58 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • glyceraldehyde-3-phosphate dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolic process
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • small molecule metabolic process
Component
—
Enzyme 58 General Function Involved in glyceraldehyde-3-phosphate dehydrogenase activity
Enzyme 58 Specific Function Independent of its glycolytic activity it is also involved in membrane trafficking in the early secretory pathway
Enzyme 58 Pathways
Enzyme 58 Reactions
  • D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+ [RN:R01061]
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 21104392 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID P04406 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name G3P_HUMAN Link Image
Enzyme 58 PDB ID 1J0X Link Image
Enzyme 58 PDB File Show
Enzyme 58 3D Structure
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1008 bp 
ATGGGGAAGGTGAAGGTCGGAGTCAACGGATTTGGTCGTATTGGGCGCCTGGTCACCAGG
GCTGCTTTTAACTCTGGTAAAGTGGATATTGTTGCCATCAATGACCCCTTCATTGACCTC
AACTACATGGTTTACATGTTCCAATATGATTCCACCCATGGCAAATTCCATGGCACCGTC
AAGGCTGAGAACGGGAAGCTTGTCATCAATGGAAATCCCATCACCATCTTCCAGGAGCGA
GATCCCTCCAAAATCAAGTGGGGCGATGCTGGCGCTGAGTACGTCGTGGAGTCCACTGGC
GTCTTCACCACCATGGAGAAGGCTGGGGCTCATTTGCAGGGGGGAGCCAAAAGGGTCATC
ATCTCTGCCCCCTCTGCTGATGCCCCCATGTTCGTCATGGGTGTGAACCATGAGAAGTAT
GACAACAGCCTCAAGATCATCAGCAATGCCTCCTGCACCACCAACTGCTTAGCACCCCTG
GCCAAGGTCATCCATGACAACTTTGGTATCGTGGAAGGACTCATGACCACAGTCCATGCC
ATCACTGCCACCCAGAAGACTGTGGATGGCCCCTCCGGGAAACTGTGGCGTGATGGCCGC
GGGGCTCTCCAGAACATCATCCCTGCCTCTACTGGCGCTGCCAAGGCTGTGGGCAAGGTC
ATCCCTGAGCTGAACGGGAAGCTCACTGGCATGGCCTTCCGTGTCCCCACTGCCAACGTG
TCAGTGGTGGACCTGACCTGCCGTCTAGAAAAACCTGCCAAATATGATGACATCAAGAAG
GTGGTGAAGCAGGCGTCGGAGGGCCCCCTCAAGGGCATCCTGGGCTACACTGAGCACCAG
GTGGTCTCCTCTGACTTCAACAGCGACACCCACTCCTCCACCTTTGACGCTGGGGCTGGC
ATTGCCCTCAACGACCACTTTGTCAAGCTCATTTCCTGGTATGACAACGAATTTGGCTAC
AGCAACAGGGTGGTGGACCTCATGGCCCACATGGCCTCCAAGGAGTAA
Enzyme 58 GenBank Gene ID AB062273 Link Image
Enzyme 58 GeneCard ID GAPDH Link Image
Enzyme 58 GenAtlas ID GAPDH Link Image
Enzyme 58 HGNC ID HGNC:4141 Link Image
Enzyme 58 Chromosome Location 1
Enzyme 58 Locus 12p13
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Hanauer A, Mandel JL: The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a human cDNA and of an X chromosome linked pseudogene; amazing complexity of the gene family in mouse. EMBO J. 1984 Nov;3(11):2627-33. [PubMed Link Image]
  2. Arcari P, Martinelli R, Salvatore F: The complete sequence of a full length cDNA for human liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species. Nucleic Acids Res. 1984 Dec 11;12(23):9179-89. [PubMed Link Image]
  3. Tso JY, Sun XH, Kao TH, Reece KS, Wu R: Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene. Nucleic Acids Res. 1985 Apr 11;13(7):2485-502. [PubMed Link Image]
  4. Tokunaga K, Nakamura Y, Sakata K, Fujimori K, Ohkubo M, Sawada K, Sakiyama S: Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers. Cancer Res. 1987 Nov 1;47(21):5616-9. [PubMed Link Image]
  5. Allen RW, Trach KA, Hoch JA: Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem. 1987 Jan 15;262(2):649-53. [PubMed Link Image]
  6. Ercolani L, Florence B, Denaro M, Alexander M: Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene. J Biol Chem. 1988 Oct 25;263(30):15335-41. [PubMed Link Image]
  7. Meyer-Siegler K, Mauro DJ, Seal G, Wurzer J, deRiel JK, Sirover MA: A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8460-4. [PubMed Link Image]
  8. Ye Z, Connor JR: cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs. Biochem Biophys Res Commun. 2000 Aug 18;275(1):223-7. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. Nowak K, Wolny M, Banas T: The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase. FEBS Lett. 1981 Nov 16;134(2):143-6. [PubMed Link Image]
  11. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  12. Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9. [PubMed Link Image]
  13. Nowak K, Kuczek M, Ostropolska L, Malarska A, Wolny M, Baranowski T: The covalent structure of glyceraldehyde-phosphate dehydrogenase from human muscles. Isolation and amino acid sequences of peptides from tryptic digest. Hoppe Seylers Z Physiol Chem. 1975 Jul;356(7):1181-3. [PubMed Link Image]
  14. Tisdale EJ: Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway. J Biol Chem. 2002 Feb 1;277(5):3334-41. Epub 2001 Nov 27. [PubMed Link Image]
  15. Mazzola JL, Sirover MA: Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function. Biochim Biophys Acta. 2003 Jun 20;1622(1):50-6. [PubMed Link Image]
  16. Wakasugi K, Nakano T, Morishima I: Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase. Biochemistry. 2005 Jan 11;44(1):225-32. [PubMed Link Image]
  17. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  18. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  19. Bosch-Comas A, Lindsten K, Gonzalez-Duarte R, Masucci MG, Marfany G: The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins. Cell Mol Life Sci. 2006 Mar;63(6):723-34. [PubMed Link Image]
  20. Wong JJ, Pung YF, Sze NS, Chin KC: HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets. Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10735-40. Epub 2006 Jun 30. [PubMed Link Image]
  21. Seo J, Jeong J, Kim YM, Hwang N, Paek E, Lee KJ: Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase. J Proteome Res. 2008 Feb;7(2):587-602. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  24. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  27. Mercer WD, Winn SI, Watson HC: Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase. J Mol Biol. 1976 Jun 14;104(1):277-83. [PubMed Link Image]
  28. Ismail SA, Park HW: Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1508-13. Epub 2005 Oct 19. [PubMed Link Image]
  29. Jenkins JL, Tanner JJ: High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):290-301. Epub 2006 Feb 22. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 5973
Enzyme 59 Name Biliverdin reductase A
Enzyme 59 Synonyms
  1. BVR A
  2. Biliverdin-IX alpha-reductase
Enzyme 59 Gene Name BLVRA
Enzyme 59 Protein Sequence >Biliverdin reductase A 
MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLE
DALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKV
LHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLF
GELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLEN
VPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK
Enzyme 59 Number of Residues 296
Enzyme 59 Molecular Weight 33428.2
Enzyme 59 Theoretical pI 6.41
Enzyme 59 GO Classification
Function
  • biliverdin reductase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
  • transition metal ion binding
  • zinc ion binding
Process
  • heme catabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin catabolic process
  • porphyrin metabolic process
  • tetrapyrrole metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 59 General Function Involved in biliverdin reductase activity
Enzyme 59 Specific Function Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor
Enzyme 59 Pathways
Enzyme 59 Reactions
  • bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+ [RN:R02391 R02393]
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 33589854 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID P53004 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name BIEA_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >891 bp 
ATGAATGCAGAGCCCGAGAGGAAGTTTGGCGTGGTGGTGGTTGGTGTTGGCCGAGCCGGC
TCCGTGCGGATGAGGGACTTGCGGAATCCACACCCTTCCTCAGCGTTCCTGAACCTGATT
GGCTTCGTGTCGAGAAGGGAGCTCGGGAGCATTGATGGAGTCCAGCAGATTTCTTTGGAG
GATGCTCTTTCCAGCCAAGAGGTGGAGGTCGCCTATATCTGCAGTGAGAGCTCCAGCCAT
GAGGACTACATCAGGCAGTTCCTTAATGCTGGCAAGCACGTCCTTGTGGAATACCCCATG
ACACTGTCATTGGCGGCCGCTCAGGAACTGTGGGAGCTGGCTGAGCAGAAAGGAAAAGTC
TTGCACGAGGAGCATGTTGAACTCTTGATGGAGGAATTCGCTTTCCTGAAAAAAGAAGTG
GTGGGGAAAGACCTGCTGAAAGGGTCGCTCCTCTTCACAGCTGGCCCGTTGGAAGAAGAG
CGGTTTGGCTTCCCTGCATTCAGCGGCATCTCTCGCCTGACCTGGCTGGTCTCCCTCTTT
GGGGAGCTTTCTCTTGTGTCTGCCACTTTGGAAGAGCGAAAGGAAGATCAGTATATGAAA
ATGACAGTGTGTCTGGAGACAGAGAAGAAAAGTCCACTGTCATGGATTGAAGAAAAAGGA
CCTGGTCTAAAACGAAACAGATATTTAAGCTTCCATTTCAAGTCTGGGTCCTTGGAGAAT
GTGCCAAATGTAGGAGTGAATAAGAACATATTTCTGAAAGATCAAAATATATTTGTCCAG
AAACTCTTGGGCCAGTTCTCTGAGAAGGAACTGGCTGCTGAAAAGAAACGCATCCTGCAC
TGCCTGGGGCTTGCAGAAGAAATCCAGAAATATTGCTGTTCAAGGAAGTAA
Enzyme 59 GenBank Gene ID NM_000712.3 Link Image
Enzyme 59 GeneCard ID BLVRA Link Image
Enzyme 59 GenAtlas ID BLVRA Link Image
Enzyme 59 HGNC ID HGNC:1062 Link Image
Enzyme 59 Chromosome Location 7
Enzyme 59 Locus 7p14-cen
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Komuro A, Tobe T, Nakano Y, Yamaguchi T, Tomita M: Cloning and characterization of the cDNA encoding human biliverdin-IX alpha reductase. Biochim Biophys Acta. 1996 Nov 11;1309(1-2):89-99. [PubMed Link Image]
  2. Maines MD, Polevoda BV, Huang TJ, McCoubrey WK Jr: Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes. Eur J Biochem. 1996 Jan 15;235(1-2):372-81. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Maines MD, Trakshel GM: Purification and characterization of human biliverdin reductase. Arch Biochem Biophys. 1993 Jan;300(1):320-6. [PubMed Link Image]
  7. Yamaguchi T, Komoda Y, Nakajima H: Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization. J Biol Chem. 1994 Sep 30;269(39):24343-8. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 5974
Enzyme 60 Name Flavin reductase
Enzyme 60 Synonyms
  1. FR
  2. Biliverdin reductase B
  3. BVR-B
  4. Biliverdin-IX beta-reductase
  5. Green heme-binding protein
  6. GHBP
  7. NADPH-dependent diaphorase
  8. NADPH-flavin reductase
  9. FLR
Enzyme 60 Gene Name BLVRB
Enzyme 60 Protein Sequence >Flavin reductase 
MAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAAD
VDKTVAGQDAVIVLLGTRNDLSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTK
VPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGDQPLTGAYTVTLDGRGPSRVISKHD
LGHFMLRCLTTDEYDGHSTYPSHQYQ
Enzyme 60 Number of Residues 206
Enzyme 60 Molecular Weight 22119.2
Enzyme 60 Theoretical pI 7.76
Enzyme 60 GO Classification
Function
  • binding
  • catalytic activity
Process
  • metabolic process
Component
—
Enzyme 60 General Function Involved in catalytic activity
Enzyme 60 Specific Function Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin
Enzyme 60 Pathways
Enzyme 60 Reactions
  • reduced riboflavin + NADP+ = riboflavin + NADPH + H+ [RN:R05707]
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein Not Available
Enzyme 60 UniProtKB/Swiss-Prot ID P30043 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name BLVRB_HUMAN Link Image
Enzyme 60 PDB ID 1HE5 Link Image
Enzyme 60 PDB File Show
Enzyme 60 3D Structure
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >621 bp 
ATGGCCGTCAAGAAGATCGCGATCTTCGGCGCCACTGGCCAGACCGGGCTCACCACCCTG
GCGCAGGCGGTGCAAGCAGGTTACGAAGTGACAGTGCTGGTGCGGGACTCCTCCAGGCTG
CCATCAGAGGGGCCCCGGCCGGCCCACGTGGTAGTGGGAGATGTTCTGCAGGCAGCCGAT
GTGGACAAGACCGTGGCTGGGCAGGACGCTGTCATCGTGCTGCTGGGCACCCGCAATGAC
CTCAGTCCCACGACAGTGATGTCCGAGGGCGCCCGGAACATTGTGGCAGCCATGAAGGCT
CATGGTGTGGACAAGGTCGTGGCCTGCACCTCGGCTTTCCTGCTCTGGGACCCTACCAAG
GTGCCCCCACGACTGCAGGCTGTGACTGATGACCACATCCGGATGCACAAGGTGCTGCGG
GAATCAGGCCTGAAGTACGTGGCTGTGATGCCGCCACACATAGGAGACCAGCCACTAACT
GGGGCGTACACAGTGACCCTGGATGGACGAGGGCCCTCAAGGGTCATCTCCAAACATGAC
CTGGGCCATTTCATGCTGCGCTGCCTCACCACCGATGAGTACGACGGACACAGCACCTAC
CCCTCCCACCAGTACCAGTAG
Enzyme 60 GenBank Gene ID D26308 Link Image
Enzyme 60 GeneCard ID BLVRB Link Image
Enzyme 60 GenAtlas ID BLVRB Link Image
Enzyme 60 HGNC ID HGNC:1063 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 19q13.1-q13.2
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Chikuba K, Yubisui T, Shirabe K, Takeshita M: Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1170-6. [PubMed Link Image]
  2. Komuro A, Tobe T, Hashimoto K, Nakano Y, Yamaguchi T, Nakajima H, Tomita M: Molecular cloning and expression of human liver biliverdin-IX beta reductase. Biol Pharm Bull. 1996 Jun;19(6):796-804. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yamaguchi T, Komuro A, Nakano Y, Tomita M, Nakajima H: Complete amino acid sequence of biliverdin-IX beta reductase from human liver. Biochem Biophys Res Commun. 1993 Dec 30;197(3):1518-23. [PubMed Link Image]
  7. Yamaguchi T, Komoda Y, Nakajima H: Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization. J Biol Chem. 1994 Sep 30;269(39):24343-8. [PubMed Link Image]
  8. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  9. Golaz O, Hughes GJ, Frutiger S, Paquet N, Bairoch A, Pasquali C, Sanchez JC, Tissot JD, Appel RD, Walzer C, et al.: Plasma and red blood cell protein maps: update 1993. Electrophoresis. 1993 Nov;14(11):1223-31. [PubMed Link Image]
  10. Shalloe F, Elliott G, Ennis O, Mantle TJ: Evidence that biliverdin-IX beta reductase and flavin reductase are identical. Biochem J. 1996 Jun 1;316 ( Pt 2):385-7. [PubMed Link Image]
  11. Cunningham O, Gore MG, Mantle TJ: Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B). Biochem J. 2000 Jan 15;345 Pt 2:393-9. [PubMed Link Image]
  12. Smith LJ, Browne S, Mulholland AJ, Mantle TJ: Computational and experimental studies on the catalytic mechanism of biliverdin-IXbeta reductase. Biochem J. 2008 May 1;411(3):475-84. [PubMed Link Image]
  13. Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M: Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme. Nat Struct Biol. 2001 Mar;8(3):215-20. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 5992
Enzyme 61 Name Corticosteroid 11-beta-dehydrogenase isozyme 1
Enzyme 61 Synonyms
  1. 11-beta-hydroxysteroid dehydrogenase 1
  2. 11-DH
  3. 11-beta-HSD1
Enzyme 61 Gene Name HSD11B1
Enzyme 61 Protein Sequence >Corticosteroid 11-beta-dehydrogenase isozyme 1 
MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAH
VVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNH
ITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMV
AAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEE
CALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK
Enzyme 61 Number of Residues 292
Enzyme 61 Molecular Weight 32400.7
Enzyme 61 Theoretical pI 8.77
Enzyme 61 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 61 General Function Involved in oxidoreductase activity
Enzyme 61 Specific Function Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7- ketocholesterol to 7-beta-hydroxycholesterol
Enzyme 61 Pathways
Enzyme 61 Reactions
  • an 11beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+ [RN:R03203]
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • 8-24
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein Not Available
Enzyme 61 UniProtKB/Swiss-Prot ID P28845 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name DHI1_HUMAN Link Image
Enzyme 61 PDB ID 1XU9 Link Image
Enzyme 61 PDB File Show
Enzyme 61 3D Structure
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >879 bp 
ATGGCTTTTATGAAAAAATATCTCCTCCCCATTCTGGGGCTCTTCATGGCCTACTACTAC
TATTCTGCAAACGAGGAATTCAGACCAGAGATGCTCCAAGGAAAGAAAGTGATTGTCACA
GGGGCCAGCAAAGGGATCGGAAGAGAGATGGCTTATCATCTGGCGAAGATGGGAGCCCAT
GTGGTGGTGACAGCGAGGTCAAAAGAAACTCTACAGAAGGTGGTATCCCACTGCCTGGAG
CTTGGAGCAGCCTCAGCACACTACATTGCTGGCACCATGGAAGACATGACCTTCGCAGAG
CAATTTGTTGCCCAAGCAGGAAAGCTCATGGGAGGACTAGACATGCTCATTCTCAACCAC
ATCACCAACACTTCTTTGAATCTTTTTCATGATGATATTCACCATGTGCGCAAAAGCATG
GAAGTCAACTTCCTCAGTTACGTGGTCCTGACTGTAGCTGCCTTGCCCATGCTGAAGCAG
AGCAATGGAAGCATTGTTGTCGTCTCCTCTCTGGCTGGGAAAGTGGCTTATCCAATGGTT
GCTGCCTATTCTGCAAGCAAGTTTGCTTTGGATGGGTTCTTCTCCTCCATCAGAAAGGAA
TATTCAGTGTCCAGGGTCAATGTATCAATCACTCTCTGTGTTCTTGGCCTCATAGACACA
GAAACAGCCATGAAGGCAGTTTCTGGGATAGTCCATATGCAAGCAGCTCCAAAGGAGGAA
TGTGCCCTGGAGATCATCAAAGGGGGAGCTCTGCGCCAAGAAGAAGTGTATTATGACAGC
TCACTCTGGACCACTCTTCTGATCAGAAATCCATGCAGGAAGATCCTGGAATTTCTCTAC
TCAACGAGCTATAATATGGACAGATTCATAAACAAGTAG
Enzyme 61 GenBank Gene ID AK313973 Link Image
Enzyme 61 GeneCard ID HSD11B1 Link Image
Enzyme 61 GenAtlas ID HSD11B1 Link Image
Enzyme 61 HGNC ID HGNC:5208 Link Image
Enzyme 61 Chromosome Location 1
Enzyme 61 Locus 1q32-q41
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Tannin GM, Agarwal AK, Monder C, New MI, White PC: The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization. J Biol Chem. 1991 Sep 5;266(25):16653-8. [PubMed Link Image]
  2. Draper N, Echwald SM, Lavery GG, Walker EA, Fraser R, Davies E, Sorensen TI, Astrup A, Adamski J, Hewison M, Connell JM, Pedersen O, Stewart PM: Association studies between microsatellite markers within the gene encoding human 11beta-hydroxysteroid dehydrogenase type 1 and body mass index, waist to hip ratio, and glucocorticoid metabolism. J Clin Endocrinol Metab. 2002 Nov;87(11):4984-90. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Odermatt A, Arnold P, Stauffer A, Frey BM, Frey FJ: The N-terminal anchor sequences of 11beta-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane. J Biol Chem. 1999 Oct 1;274(40):28762-70. [PubMed Link Image]
  7. Draper N, Walker EA, Bujalska IJ, Tomlinson JW, Chalder SM, Arlt W, Lavery GG, Bedendo O, Ray DW, Laing I, Malunowicz E, White PC, Hewison M, Mason PJ, Connell JM, Shackleton CH, Stewart PM: Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency. Nat Genet. 2003 Aug;34(4):434-9. [PubMed Link Image]
  8. Frick C, Atanasov AG, Arnold P, Ozols J, Odermatt A: Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the endoplasmic reticulum lumen is dependent on its N-terminal region sharing similar topological determinants with 50-kDa esterase. J Biol Chem. 2004 Jul 23;279(30):31131-8. Epub 2004 May 19. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  10. Hosfield DJ, Wu Y, Skene RJ, Hilgers M, Jennings A, Snell GP, Aertgeerts K: Conformational flexibility in crystal structures of human 11beta-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation. J Biol Chem. 2005 Feb 11;280(6):4639-48. Epub 2004 Oct 28. [PubMed Link Image]
  11. Sorensen B, Winn M, Rohde J, Shuai Q, Wang J, Fung S, Monzon K, Chiou W, Stolarik D, Imade H, Pan L, Deng X, Chovan L, Longenecker K, Judge R, Qin W, Brune M, Camp H, Frevert EU, Jacobson P, Link JT: Adamantane sulfone and sulfonamide 11-beta-HSD1 Inhibitors. Bioorg Med Chem Lett. 2007 Jan 15;17(2):527-32. Epub 2006 Oct 7. [PubMed Link Image]
  12. Yuan C, St Jean DJ Jr, Liu Q, Cai L, Li A, Han N, Moniz G, Askew B, Hungate RW, Johansson L, Tedenborg L, Pyring D, Williams M, Hale C, Chen M, Cupples R, Zhang J, Jordan S, Bartberger MD, Sun Y, Emery M, Wang M, Fotsch C: The discovery of 2-anilinothiazolones as 11beta-HSD1 inhibitors. Bioorg Med Chem Lett. 2007 Nov 15;17(22):6056-61. Epub 2007 Sep 25. [PubMed Link Image]
  13. Wang H, Ruan Z, Li JJ, Simpkins LM, Smirk RA, Wu SC, Hutchins RD, Nirschl DS, Van Kirk K, Cooper CB, Sutton JC, Ma Z, Golla R, Seethala R, Salyan ME, Nayeem A, Krystek SR Jr, Sheriff S, Camac DM, Morin PE, Carpenter B, Robl JA, Zahler R, Gordon DA, Hamann LG: Pyridine amides as potent and selective inhibitors of 11beta-hydroxysteroid dehydrogenase type 1. Bioorg Med Chem Lett. 2008 Jun 1;18(11):3168-72. Epub 2008 May 1. [PubMed Link Image]
  14. Hale C, Veniant M, Wang Z, Chen M, McCormick J, Cupples R, Hickman D, Min X, Sudom A, Xu H, Matsumoto G, Fotsch C, St Jean DJ Jr, Wang M: Structural characterization and pharmacodynamic effects of an orally active 11beta-hydroxysteroid dehydrogenase type 1 inhibitor. Chem Biol Drug Des. 2008 Jan;71(1):36-44. Epub 2007 Dec 7. [PubMed Link Image]
  15. Julian LD, Wang Z, Bostick T, Caille S, Choi R, DeGraffenreid M, Di Y, He X, Hungate RW, Jaen JC, Liu J, Monshouwer M, McMinn D, Rew Y, Sudom A, Sun D, Tu H, Ursu S, Walker N, Yan X, Ye Q, Powers JP: Discovery of novel, potent benzamide inhibitors of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) exhibiting oral activity in an enzyme inhibition ex vivo model. J Med Chem. 2008 Jul 10;51(13):3953-60. Epub 2008 Jun 14. [PubMed Link Image]
  16. Rew Y, McMinn DL, Wang Z, He X, Hungate RW, Jaen JC, Sudom A, Sun D, Tu H, Ursu S, Villemure E, Walker NP, Yan X, Ye Q, Powers JP: Discovery and optimization of piperidyl benzamide derivatives as a novel class of 11beta-HSD1 inhibitors. Bioorg Med Chem Lett. 2009 Mar 15;19(6):1797-801. Epub 2009 Jan 23. [PubMed Link Image]
  17. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 6002
Enzyme 62 Name Dihydropyrimidine dehydrogenase [NADP+]
Enzyme 62 Synonyms
  1. DHPDHase
  2. DPD
  3. Dihydrothymine dehydrogenase
  4. Dihydrouracil dehydrogenase
Enzyme 62 Gene Name DPYD
Enzyme 62 Protein Sequence >Dihydropyrimidine dehydrogenase [NADP+] 
MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFD
DIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDN
PLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPE
KMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDV
VNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQD
QGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVF
IVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWN
EDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGG
DVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGL
KFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMY
GPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDS
GADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSI
ARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTS
IARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYL
KSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQ
NVAFSPLKRNCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCY
MTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLS
VNPVC
Enzyme 62 Number of Residues 1025
Enzyme 62 Molecular Weight 111400.3
Enzyme 62 Theoretical pI 7.05
Enzyme 62 GO Classification
Function
  • binding
  • catalytic activity
  • dihydroorotate dehydrogenase activity
  • dihydroorotate oxidase activity
  • electron carrier activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, quinone or related compound as acceptor
Process
  • 'de novo' pyrimidine base biosynthetic process
  • UMP biosynthetic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
  • pyrimidine base biosynthetic process
  • pyrimidine base metabolic process
  • pyrimidine nucleoside monophosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside monophosphate biosynthetic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 62 General Function Involved in electron carrier activity
Enzyme 62 Specific Function Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil
Enzyme 62 Pathways
Enzyme 62 Reactions
  • 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+ [RN:R00978]
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 6729338 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q12882 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name DPYD_HUMAN Link Image
Enzyme 62 PDB ID 1GTE Link Image
Enzyme 62 PDB File Show
Enzyme 62 3D Structure
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >3078 bp 
ATGGCCCCTGTGCTCAGTAAGGACTCGGCGGACATCGAGAGTATCCTGGCTTTAAATCCT
CGAACACAAACTCATGCAACTCTGTGTTCCACTTCGGCCAAGAAATTAGACAAGAAACAT
TGGAAAAGAAATCCTGATAAGAACTGCTTTAATTGTGAGAAGCTGGAGAATAATTTTGAT
GACATCAAGCACACGACTCTTGGTGAGCGAGGAGCTCTCCGAGAAGCAATGAGATGCCTG
AAATGTGCAGATGCCCCGTGTCAGAAGAGCTGTCCAACTAATCTTGATATTAAATCATTC
ATCACAAGTATTGCAAACAAGAACTATTATGGAGCTGCTAAGATGATATTTTCTGACAAC
CCACTTGGTCTGACTTGTGGAATGGTATGTCCAACCTCTGATCTTTGTGTAGGTGGATGC
AATTTATATGCCACTGAAGAGGGACCCATTAATATTGGTGGATTGCAGCAATTTGCTACT
GAGGTATTCAAAGCAATGAGTATCCCACAGATCAGAAATCCTTCGCTGCCTCCCCCAGAA
AAAATGTCTGAAGCCTATTCTGCAAAGATTGCTCTTTTTGGTGCTGGGCCTGCAAGTATA
AGTTGTGCTTCCTTTTTGGCTCGATTGGGGTACTCTGACATCACTATATTTGAAAAACAA
GAATATGTTGGTGGTTTAAGTACTTCTGAAATTCCTCAGTTCCGGCTGCCGTATGATGTA
GTGAATTTTGAGATTGAGCTAATGAAGGACCTTGGTGTAAAGATAATTTGCGGTAAAAGC
CTTTCAGTGAATGAAATGACTCTTAGCACTTTGAAAGAAAAAGGCTACAAAGCTGCTTTC
ATTGGAATAGGTTTGCCAGAACCCAATAAAGATGCCATCTTCCAAGGCCTGACGCAGGAC
CAGGGGTTTTATACATCCAAAGACTTTTTGCCACTTGTAGCCAAAGGCAGTAAAGCAGGA
ATGTGCGCCTGTCACTCTCCATTGCCATCGATACGGGGAGTCGTGATCGTACTTGGAGCT
GGAGACACTGCCTTTGACTGTGCAACATCTGCTCTACGTTGTGGAGCTCGCCGTGTGTTC
ATCGTCTTCAGAAAAGGCTTTGTTAATATAAGAGCTGTCCCTGAGGAGATGGAACTTGCT
AAGGAAGAAAAGTGTGAATTTCTGCCATTCCTGTCCCCACGGAAGGTTATAGTAAAAGGT
GGGAGAATTGTTGCTATGCAGTTTGTTCGGACAGAGCAAGATGAAACTGGAAAATGGAAT
GAAGATGAAGATCAGATGGTCCATCTGAAAGCCGATGTGGTCATCAGTGCCTTTGGTTCA
GTTCTGAGTGATCCTAAAGTAAAAGAAGCCTTGAGCCCTATAAAATTTAACAGATGGGGT
CTCCCAGAAGTAGATCCAGAAACTATGCAAACTAGTGAAGCATGGGTATTTGCAGGTGGT
GATGTCGTTGGTTTGGCTAACACTACAGTGGAATCGGTGAATGATGGAAAGCAAGCTTCT
TGGTACATTCACAAATACGTACAGTCACAATATGGAGCTTCCGTTTCTGCCAAGCCTGAA
CTACCCCTCTTTTACACTCCTATTGATCTGGTGGACATTAGTGTAGAAATGGCCGGATTG
AAGTTTATAAATCCTTTTGGTCTTGCTAGCGCAACTCCAGCCACCAGCACATCAATGATT
CGAAGAGCTTTTGAAGCTGGATGGGGTTTTGCCCTCACCAAAACTTTCTCTCTTGATAAG
GACATTGTGACAAATGTTTCCCCCAGAATCATCCGGGGAACCACCTCTGGCCCCATGTAT
GGCCCTGGACAAAGCTCCTTTCTGAATATTGAGCTCATCAGTGAGAAAACGGCTGCATAT
TGGTGTCAAAGTGTCACTGAACTAAAGGCTGACTTTCCAGACAACATTGTGATTGCTAGC
ATTATGTGCAGTTACAATAAAAATGACTGGACGGAACTTGCCAAGAAGTCTGAGGATTCT
GGAGCAGATGCCCTGGAGTTAAATTTATCATGTCCACATGGCATGGGAGAAAGAGGAATG
GGCCTGGCCTGTGGGCAGGATCCAGAGCTGGTGCGGAACATCTGCCGCTGGGTTAGGCAA
GCTGTTCAGATTCCTTTTTTTGCCAAGCTGACCCCAAATGTCACTGATATTGTGAGCATC
GCAAGAGCTGCAAAGGAAGGTGGTGCCAATGGCGTTACAGCCACCAACACTGTCTCAGGT
CTGATGGGATTAAAATCTGATGGCACACCTTGGCCAGCAGTGGGGATTGCAAAGCGAACT
ACATATGGAGGAGTGTCTGGGACAGCAATCAGACCTATTGCTTTGAGAGCTGTGACCTCC
ATTGCTCGTGCTCTGCCTGGATTTCCCATTTTGGCTACTGGTGGAATTGACTCTGCTGAA
AGTGGTCTTCAGTTTCTCCATAGTGGTGCTTCCGTCCTCCAGGTATGCAGTGCCATTCAG
AATCAGGATTTCACTGTGATCGAAGACTACTGCACTGGCCTCAAAGCCCTGCTTTATCTG
AAAAGCATTGAAGAACTACAAGACTGGGATGGACAGAGTCCAGCTACTGTGAGTCACCAG
AAAGGGAAACCAGTTCCACGTATAGCTGAACTCATGGACAAGAAACTGCCAAGTTTTGGA
CCTTATCTGGAACAGCGCAAGAAAATCATAGCAGAAAACAAGATTAGACTGAAAGAACAA
AATGTAGCTTTTTCACCACTTAAGAGAAACTGTTTTATCCCCAAAAGGCCTATTCCTACC
ATCAAGGATGTAATAGGAAAAGCACTGCAGTACCTTGGAACATTTGGTGAATTGAGCAAC
GTAGAGCAAGTTGTGGCTATGATTGATGAAGAAATGTGTATCAACTGTGGTAAATGCTAC
ATGACCTGTAATGATTCTGGCTACCAGGCTATACAGTTTGATCCAGAAACCCACCTGCCC
ACCATAACCGACACTTGTACAGGCTGTACTCTGTGTCTCAGTGTTTGCCCTATTGTCGAC
TGCATCAAAATGGTTTCCAGGACAACACCTTATGAACCAAAGAGAGGCGTACCCTTATCT
GTGAATCCGGTGTGTTAA
Enzyme 62 GenBank Gene ID AB003063 Link Image
Enzyme 62 GeneCard ID DPYD Link Image
Enzyme 62 GenAtlas ID DPYD Link Image
Enzyme 62 HGNC ID HGNC:3012 Link Image
Enzyme 62 Chromosome Location 1
Enzyme 62 Locus 1p22
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Yokota H, Fernandez-Salguero P, Furuya H, Lin K, McBride OW, Podschun B, Schnackerz KD, Gonzalez FJ: cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria. J Biol Chem. 1994 Sep 16;269(37):23192-6. [PubMed Link Image]
  2. Johnson MR, Wang K, Tillmanns S, Albin N, Diasio RB: Structural organization of the human dihydropyrimidine dehydrogenase gene. Cancer Res. 1997 May 1;57(9):1660-3. [PubMed Link Image]
  3. Ogura K, Nishiyama T, Takubo H, Kato A, Okuda H, Arakawa K, Fukushima M, Nagayama S, Kawaguchi Y, Watabe T: Suicidal inactivation of human dihydropyrimidine dehydrogenase by (E)-5-(2-bromovinyl)uracil derived from the antiviral, sorivudine. Cancer Lett. 1998 Jan 9;122(1-2):107-13. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Vreken P, Van Kuilenburg AB, Meinsma R, Smit GP, Bakker HD, De Abreu RA, van Gennip AH: A point mutation in an invariant splice donor site leads to exon skipping in two unrelated Dutch patients with dihydropyrimidine dehydrogenase deficiency. J Inherit Metab Dis. 1996;19(5):645-54. [PubMed Link Image]
  8. Fernandez-Salguero PM, Sapone A, Wei X, Holt JR, Jones S, Idle JR, Gonzalez FJ: Lack of correlation between phenotype and genotype for the polymorphically expressed dihydropyrimidine dehydrogenase in a family of Pakistani origin. Pharmacogenetics. 1997 Apr;7(2):161-3. [PubMed Link Image]
  9. Lu ZH, Zhang R, Diasio RB: Purification and characterization of dihydropyrimidine dehydrogenase from human liver. J Biol Chem. 1992 Aug 25;267(24):17102-9. [PubMed Link Image]
  10. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Dihydropyrimidine dehydrogenase (DPD) deficiency: identification and expression of missense mutations C29R, R886H and R235W. Hum Genet. 1997 Dec;101(3):333-8. [PubMed Link Image]
  13. Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Identification of novel point mutations in the dihydropyrimidine dehydrogenase gene. J Inherit Metab Dis. 1997 Jul;20(3):335-8. [PubMed Link Image]
  14. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 6060
Enzyme 63 Name Alcohol dehydrogenase class-3
Enzyme 63 Synonyms
  1. Alcohol dehydrogenase 5
  2. Alcohol dehydrogenase class chi chain
  3. Alcohol dehydrogenase class-III
  4. Glutathione-dependent formaldehyde dehydrogenase
  5. FALDH
  6. FDH
  7. GSH-FDH
  8. S-(hydroxymethyl)glutathione dehydrogenase
Enzyme 63 Gene Name ADH5
Enzyme 63 Protein Sequence >Alcohol dehydrogenase class-3 
MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGC
FPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGK
GLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGY
GAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATEC
INPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEE
IATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFE
LMHSGKSIRTVVKI
Enzyme 63 Number of Residues 374
Enzyme 63 Molecular Weight 39723.9
Enzyme 63 Theoretical pI 7.54
Enzyme 63 GO Classification
Function
  • S-(hydroxymethyl)glutathione dehydrogenase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • transition metal ion binding
  • zinc ion binding
Process
  • alcohol metabolic process
  • ethanol metabolic process
  • ethanol oxidation
  • metabolic process
  • monohydric alcohol metabolic process
  • oxidation reduction
  • small molecule metabolic process
Component
—
Enzyme 63 General Function Involved in zinc ion binding
Enzyme 63 Specific Function Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione
Enzyme 63 Pathways
Enzyme 63 Reactions
  • S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+ [RN:R06983 R07140]
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 178134 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID P11766 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name ADHX_HUMAN Link Image
Enzyme 63 PDB ID 1MC5 Link Image
Enzyme 63 PDB File Show
Enzyme 63 3D Structure
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >1125 bp 
ATGGCGAACGAGGTTATCAAGTGCAAGGCTGCAGTTGCTTGGGAGGCTGGAAAGCCTCTC
TCCATAGAGGAGATAGAGGTGGCACCCCCAAAGGCTCATGAAGTTCGAATCAAGATCATT
GCCACTGCGGTTTGCCACACCGATGCCTATACCCTGAGTGGAGCTGATCCTGAGGGTTGT
TTTCCAGTGATCTTGGGACATGAAGGTGCTGGAATTGTGGAAAGTGTTGGTGAGGGAGTT
ACTAAGCTGAAGGCGGGTGACACTGTCATCCCACTTTACATCCCACAGTGTGGAGAATGC
AAATTTTGTCTAAATCCTAAAACTAACCTTTGCCAGAAGATAAGAGTCACTCAAGGGAAA
GGATTAATGCCAGATGGTACCAGCAGATTTACTTGCAAAGGAAAGACAATTTTGCATTAC
ATGGGAACCAGCACATTTTCTGAATACACAGTTGTGGCTGATATCTCTGTTGCTAAAATA
GATCCTTTAGCACCTTTGGATAAAGTCTGCCTTCTAGGTTGTGGCATTTCAACCGGTTAT
GGTGCTGCTGTGAACACTGCCAAGTTGGAGCCTGGCTCTGTTTGTGCCGTCTTTGGTCTG
GGAGGAGTCGGATTGGCAGTTATCATGGGCTGTAAAGTGGCTGGTGCTTCCCGGATCATT
GGTGTGGACATCAATAAAGATAAATTTGCAAGGGCCAAAGAGTTTGGAGCCACTGAATGT
ATTAACCCTCAGGATTTTAGTAAACCCATCCAGGAAGTGCTCATTGAGATGACCGATGGA
GGAGTGGACTATTCCTTTGAATGTATTGGTAATGTGAAGGTCATGAGAGCAGCACTTGAG
GCATGTCACAAGGGCTGGGGCGTCAGCGTCGTGGTTGGAGTAGCTGCTTCAGGTGAAGAA
ATTGCCACTCGTCCATTCCAGCTGGTAACAGGTCGCACATGGAAAGGCACTGCCTTTGGA
GGATGGAAGAGTGTAGAAAGTGTCCCAAAGTTGGTGTCTGAATATATGTCCAAAAAGATA
AAAGTTGATGAATTTGTGACTCACAATCTGTCTTTTGATGAAATCAACAAAGCCTTTGAA
CTGATGCATTCTGGAAAGAGCATTCGAACTGTTGTAAAGATTTAA
Enzyme 63 GenBank Gene ID M30471 Link Image
Enzyme 63 GeneCard ID ADH5 Link Image
Enzyme 63 GenAtlas ID ADH5 Link Image
Enzyme 63 HGNC ID HGNC:253 Link Image
Enzyme 63 Chromosome Location 4
Enzyme 63 Locus 4q21-q25
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Sharma CP, Fox EA, Holmquist B, Jornvall H, Vallee BL: cDNA sequence of human class III alcohol dehydrogenase. Biochem Biophys Res Commun. 1989 Oct 31;164(2):631-7. [PubMed Link Image]
  2. Giri PR, Krug JF, Kozak C, Moretti T, O'Brien SJ, Seuanez HN, Goldman D: Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA. Biochem Biophys Res Commun. 1989 Oct 16;164(1):453-60. [PubMed Link Image]
  3. Hur MW, Edenberg HJ: Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase. Gene. 1992 Nov 16;121(2):305-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kaiser R, Holmquist B, Hempel J, Vallee BL, Jornvall H: Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes. Biochemistry. 1988 Feb 23;27(4):1132-40. [PubMed Link Image]
  6. Holmquist B, Moulis JM, Engeland K, Vallee BL: Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Biochemistry. 1993 May 18;32(19):5139-44. [PubMed Link Image]
  7. Engeland K, Hoog JO, Holmquist B, Estonius M, Jornvall H, Vallee BL: Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2491-4. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Yang ZN, Bosron WF, Hurley TD: Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J Mol Biol. 1997 Jan 24;265(3):330-43. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 6062
Enzyme 64 Name Alcohol dehydrogenase 1B
Enzyme 64 Synonyms
  1. Alcohol dehydrogenase subunit beta
Enzyme 64 Gene Name ADH1B
Enzyme 64 Protein Sequence >Alcohol dehydrogenase 1B 
MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNP
RGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQ
NLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTVLTF
Enzyme 64 Number of Residues 375
Enzyme 64 Molecular Weight 39854.2
Enzyme 64 Theoretical pI 8.38
Enzyme 64 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 64 General Function Involved in zinc ion binding
Enzyme 64 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 64 Pathways
Enzyme 64 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326 R07327]
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 34577061 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID P00325 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name ADH1B_HUMAN Link Image
Enzyme 64 PDB ID 1HSZ Link Image
Enzyme 64 PDB File Show
Enzyme 64 3D Structure
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >1128 bp 
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGGTAAAGAAA
CCCTTTTCCATTGAGGATGTGGAGGTTGCACCTCCTAAGGCTTATGAAGTTCGCATTAAG
ATGGTGGCTGTAGGAATCTGTCACACAGATGACCACGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAGTTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGGGGGAAGCCCATTCACCAC
TTCCTTGGCACCAGCACCTTCTCCCAGTACACGGTGGTGGATGAGAATGCAGTGGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTCTCGACTGGT
TATGGGTCTGCAGTTAACGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAATTTGCAAAGGCCAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATTCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGCGTCATCGTAGGGGTACCTCCTGCTTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACCTGGAAGGGGGCTGTTTAT
GGTGGCTTTAAGAGTAAAGAAGGTATCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCACTGGATGCGTTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCGTCCTGACGTTTTGA
Enzyme 64 GenBank Gene ID NM_000668.4 Link Image
Enzyme 64 GeneCard ID ADH1B Link Image
Enzyme 64 GenAtlas ID ADH1B Link Image
Enzyme 64 HGNC ID HGNC:250 Link Image
Enzyme 64 Chromosome Location 4
Enzyme 64 Locus 4q23
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Ikuta T, Fujiyoshi T, Kurachi K, Yoshida A: Molecular cloning of a full-length cDNA for human alcohol dehydrogenase. Proc Natl Acad Sci U S A. 1985 May;82(9):2703-7. [PubMed Link Image]
  2. Heden LO, Hoog JO, Larsson K, Lake M, Lagerholm E, Holmgren A, Vallee BL, Jornvall H, von Bahr-Lindstrom H: cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions. FEBS Lett. 1986 Jan 6;194(2):327-32. [PubMed Link Image]
  3. Duester G, Smith M, Bilanchone V, Hatfield GW: Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. J Biol Chem. 1986 Feb 15;261(5):2027-33. [PubMed Link Image]
  4. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed Link Image]
  5. Carr LG, Xu Y, Ho WH, Edenberg HJ: Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit. Alcohol Clin Exp Res. 1989 Aug;13(4):594-6. [PubMed Link Image]
  6. Matsuo Y, Yokoyama R, Yokoyama S: The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide. Eur J Biochem. 1989 Aug 1;183(2):317-20. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Hempel J, Buhler R, Kaiser R, Holmquist B, de Zalenski C, von Wartburg JP, Vallee B, Jornvall H: Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme. Eur J Biochem. 1984 Dec 17;145(3):437-45. [PubMed Link Image]
  9. Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ: Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification. Genomics. 1988 Apr;2(3):209-14. [PubMed Link Image]
  10. Jornvall H, Hempel J, Vallee BL, Bosron WF, Li TK: Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme. Proc Natl Acad Sci U S A. 1984 May;81(10):3024-8. [PubMed Link Image]
  11. Burnell JC, Carr LG, Dwulet FE, Edenberg HJ, Li TK, Bosron WF: The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding. Biochem Biophys Res Commun. 1987 Aug 14;146(3):1127-33. [PubMed Link Image]
  12. Hurley TD, Bosron WF, Hamilton JA, Amzel LM: Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. [PubMed Link Image]
  13. Hurley TD, Bosron WF, Stone CL, Amzel LM: Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. J Mol Biol. 1994 Jun 10;239(3):415-29. [PubMed Link Image]
  14. Davis GJ, Bosron WF, Stone CL, Owusu-Dekyi K, Hurley TD: X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J Biol Chem. 1996 Jul 19;271(29):17057-61. [PubMed Link Image]
  15. Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 2001 Apr;10(4):697-706. [PubMed Link Image]
  16. Borras E, Coutelle C, Rosell A, Fernandez-Muixi F, Broch M, Crosas B, Hjelmqvist L, Lorenzo A, Gutierrez C, Santos M, Szczepanek M, Heilig M, Quattrocchi P, Farres J, Vidal F, Richart C, Mach T, Bogdal J, Jornvall H, Seitz HK, Couzigou P, Pares X: Genetic polymorphism of alcohol dehydrogenase in europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1. Hepatology. 2000 Apr;31(4):984-9. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 6064
Enzyme 65 Name Alcohol dehydrogenase 1A
Enzyme 65 Synonyms
  1. Alcohol dehydrogenase subunit alpha
Enzyme 65 Gene Name ADH1A
Enzyme 65 Protein Sequence >Alcohol dehydrogenase 1A 
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNP
QGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTILMF
Enzyme 65 Number of Residues 375
Enzyme 65 Molecular Weight 39858.4
Enzyme 65 Theoretical pI 8.02
Enzyme 65 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 65 General Function Involved in zinc ion binding
Enzyme 65 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 65 Pathways
Enzyme 65 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326 R07327]
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein Not Available
Enzyme 65 UniProtKB/Swiss-Prot ID P07327 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name ADH1A_HUMAN Link Image
Enzyme 65 PDB ID 1HSO Link Image
Enzyme 65 PDB File Show
Enzyme 65 3D Structure
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >1128 bp 
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTGGAGGTTGCACCTCCTAAGGCCCATGAAGTTCGTATTAAG
ATGGTGGCTGTAGGAATCTGTGGCACAGATGACCACGTGGTTAGTGGTACCATGGTGACC
CCACTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCACTCGCTATTCCTCAGTGTGGAAAA
TGCAGAATTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAACGATGTAAGCAATCCT
CAGGGGACCCTGCAGGATGGCACCAGCAGGTTCACCTGCAGGAGGAAGCCCATCCACCAC
TTCCTTGGCATCAGCACCTTCTCACAGTACACAGTGGTGGATGAAAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCTCTAGAGAAAGTCTGTCTCATTGGCTGTGGATTTTCAACTGGT
TATGGGTCTGCAGTCAATGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTATTATGGGCTGTAAAGCAGCTGGGGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAATTTGCAAAGGCCAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATCCAGGAGGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCATTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATCGTAGGGGTACCTCCTGATTCCCAA
AACCTCTCAATGAACCCTATGCTGCTACTGACTGGACGTACCTGGAAGGGAGCTATTCTT
GGTGGCTTTAAAAGTAAAGAATGTGTCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCATTGGATGCATTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCATTCTGATGTTTTGA
Enzyme 65 GenBank Gene ID M12963 Link Image
Enzyme 65 GeneCard ID ADH1A Link Image
Enzyme 65 GenAtlas ID ADH1A Link Image
Enzyme 65 HGNC ID HGNC:249 Link Image
Enzyme 65 Chromosome Location 4
Enzyme 65 Locus 4q23
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. von Bahr-Lindstrom H, Hoog JO, Heden LO, Kaiser R, Fleetwood L, Larsson K, Lake M, Holmquist B, Holmgren A, Hempel J, et al.: cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase. Biochemistry. 1986 May 6;25(9):2465-70. [PubMed Link Image]
  2. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed Link Image]
  3. Matsuo Y, Yokoyama S: Molecular structure of the human alcohol dehydrogenase 1 gene. FEBS Lett. 1989 Jan 16;243(1):57-60. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yasunami M, Kikuchi I, Sarapata D, Yoshida A: The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome. Genomics. 1990 Jun;7(2):152-8. [PubMed Link Image]
  7. Gibbons BJ, Hurley TD: Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors. Biochemistry. 2004 Oct 5;43(39):12555-62. [PubMed Link Image]
  8. Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 2001 Apr;10(4):697-706. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 6065
Enzyme 66 Name Alcohol dehydrogenase 6
Enzyme 66 Synonyms Not Available
Enzyme 66 Gene Name ADH6
Enzyme 66 Protein Sequence >Alcohol dehydrogenase 6 
MCTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLD
LLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK
TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTG
FGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE
CLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASV
QLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAV
ELMKTGKW
Enzyme 66 Number of Residues 368
Enzyme 66 Molecular Weight 39088.3
Enzyme 66 Theoretical pI 7.83
Enzyme 66 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 66 General Function Involved in zinc ion binding
Enzyme 66 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 66 Pathways
Enzyme 66 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326 R07327]
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 4501939 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID P28332 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name ADH6_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >1107 bp 
ATGAGTACTACAGGCCAAGTCATCAGATGCAAAGCAGCCATACTCTGGAAGCCTGGTGCA
CCATTTTCTATTGAAGAGGTAGAAGTGGCCCCACCAAAGGCAAAGGAAGTTCGCATAAAG
GTTGTGGCCACCGGACTGTGTGGTACAGAGATGAAAGTGTTGGGGAGTAAACACTTGGAC
CTCTTGTATCCCACCATCTTGGGCCATGAAGGGGCTGGAATCGTTGAGAGTATTGGAGAA
GGAGTAAGCACAGTGAAACCAGGTGACAAAGTTATCACACTCTTTCTGCCACAGTGTGGA
GAATGTACCTCTTGCCTGAATTCTGAGGGCAATTTTTGTATACAATTCAAACAGTCAAAA
ACCCAACTGATGTCTGATGGTACCAGCAGGTTTACCTGCAAGGGAAAATCAATATATCAC
TTTGGTAATACCAGCACCTTCTGTGAATACACAGTGATAAAGGAAATCTCAGTTGCCAAG
ATTGATGCAGTCGCTCCTCTAGAGAAAGTATGCCTAATTAGCTGTGGCTTTTCCACTGGG
TTTGGTGCTGCAATCAATACTGCCAAGGTGACTCCAGGTTCTACCTGTGCTGTGTTTGGC
CTGGGAGGAGTCGGCTTGTCTGTTGTCATGGGTTGTAAAGCAGCAGGAGCAGCCAGGATC
ATTGGAGTGGATGTCAACAAGGAGAAATTTAAGAAGGCACAGGAATTGGGTGCTACTGAG
TGCCTCAACCCTCAGGACTTAAAGAAACCCATTCAAGAAGTTTTATTTGATATGACAGAT
GCTGGTATAGACTTCTGCTTTGAGGCCATTGGAAATCTGGACGTTCTGGCAGCTGCCCTC
GCCTCCTGCAATGAGAGCTATGGGGTCTGTGTGGTTGTTGGGGTGTTGCCTGCCAGTGTT
CAACTCAAAATCAGTGGCCAGTTGTTCTTCTCAGGACGTTCTTTGAAGGGTTCTGTTTTT
GGAGGCTGGAAGAGCAGACAGCACATCCCTAAACTGGTTGCTGATTATATGGCAGAGAAG
TTGAATCTAGATCCACTAATTACTCATACTCTGAATCTTGATAAAATCAATGAAGCAGTT
GAATTAATGAAAACTGGAAAATGGTAA
Enzyme 66 GenBank Gene ID NM_000672.3 Link Image
Enzyme 66 GeneCard ID ADH6 Link Image
Enzyme 66 GenAtlas ID ADH6 Link Image
Enzyme 66 HGNC ID HGNC:255 Link Image
Enzyme 66 Chromosome Location 4
Enzyme 66 Locus 4q23
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Yasunami M, Chen CS, Yoshida A: A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7610-4. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 6066
Enzyme 67 Name Alcohol dehydrogenase 1C
Enzyme 67 Synonyms
  1. Alcohol dehydrogenase subunit gamma
Enzyme 67 Gene Name ADH1C
Enzyme 67 Protein Sequence >Alcohol dehydrogenase 1C 
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNP
RGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGF
DLLRSGKSIRTVLTF
Enzyme 67 Number of Residues 375
Enzyme 67 Molecular Weight 39867.3
Enzyme 67 Theoretical pI 8.38
Enzyme 67 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 67 General Function Involved in zinc ion binding
Enzyme 67 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 67 Pathways
Enzyme 67 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326 R07327]
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 28404 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID P00326 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name ADH1G_HUMAN Link Image
Enzyme 67 PDB ID 1HT0 Link Image
Enzyme 67 PDB File Show
Enzyme 67 3D Structure
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >1128 bp 
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTAGAGGTTGCACCTCCTAAGGCTCATGAAGTTCGCATTAAG
ATGGTGGCTGCAGGAATCTGTCGTTCAGATGAGCATGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAAAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAATTTGCAAAAACCCAGAAAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGCGGGAAGCCCATCCACCAC
TTCGTCGGCGTCAGCACCTTCTCCCAGTACACAGTGGTGGATGAGAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTTTCGACTGGT
TATGGGTCTGCAGTCAAAGTTGCCAAGGTCACCCCAGGGTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGTTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCTGTGGACATCAACAAGGACAAATTTGCAAAGGCTAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATTCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCAGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATTGTAGGGGTACCTCCTGATTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACGTGGAAAGGAGCTATTTTT
GGAGGCTTTAAGAGTAAAGAATCTGTCCCCAAACTTGTGGCTGACTTTATGGCTAAGAAG
TTTTCACTGGATGCATTAATAACAAATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCGCTCTGGAAAGAGTATCCGTACCGTCCTGACGTTTTGA
Enzyme 67 GenBank Gene ID X04299 Link Image
Enzyme 67 GeneCard ID ADH1C Link Image
Enzyme 67 GenAtlas ID ADH1C Link Image
Enzyme 67 HGNC ID HGNC:251 Link Image
Enzyme 67 Chromosome Location 4
Enzyme 67 Locus 4q23
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Hoog JO, Heden LO, Larsson K, Jornvall H, von Bahr-Lindstrom H: The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties. Eur J Biochem. 1986 Sep 1;159(2):215-8. [PubMed Link Image]
  2. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed Link Image]
  3. Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R: Molecular structure of the human alcohol dehydrogenase 3 gene. Jpn J Genet. 1992 Apr;67(2):167-71. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Buhler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jornvall H: Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain. Eur J Biochem. 1984 Dec 17;145(3):447-53. [PubMed Link Image]
  7. Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 2001 Apr;10(4):697-706. [PubMed Link Image]
  8. Gibbons BJ, Hurley TD: Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors. Biochemistry. 2004 Oct 5;43(39):12555-62. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 6070
Enzyme 68 Name Dihydrofolate reductase
Enzyme 68 Synonyms Not Available
Enzyme 68 Gene Name DHFR
Enzyme 68 Protein Sequence >Dihydrofolate reductase 
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFS
IPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSS
VYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKF
EVYEKND
Enzyme 68 Number of Residues 187
Enzyme 68 Molecular Weight 21452.6
Enzyme 68 Theoretical pI 7.60
Enzyme 68 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • dihydrofolate reductase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • glycine biosynthetic process
  • glycine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide biosynthetic process
  • nucleotide metabolic process
  • oxidation reduction
  • serine family amino acid metabolic process
Component
—
Enzyme 68 General Function Involved in dihydrofolate reductase activity
Enzyme 68 Specific Function Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis
Enzyme 68 Pathways
Enzyme 68 Reactions
  • 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ [RN:R00939]
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 182724 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID P00374 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name DYR_HUMAN Link Image
Enzyme 68 PDB ID 1MVT Link Image
Enzyme 68 PDB File Show
Enzyme 68 3D Structure
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >564 bp 
ATGGTTGGTTCGCTAAACTGCATCGTCGCTGTGTCCCAGAACATGGGCATCGGCAAGAAC
GGGGACCTGCCCTGGCCACCGCTCAGGAATGAATTCAGATATTTCCAGAGAATGACCACA
ACCTCTTCAGTAGAAGGTAAACAGAATCTGGTGATTATGGGTAAGAAGACCTGGTTCTCC
ATTCCTGAGAAGAATCGACCTTTAAAGGGTAGAATTAATTTAGTTCTCAGCAGAGAACTC
AAGGAACCTCCACAAGGAGCTCATTTTCTTTCCAGAAGTCTAGATGATGCCTTAAAACTT
ACTGAACAACCAGAATTAGCAAATAAAGTAGACATGGTCTGGATAGTTGGTGGCAGTTCT
GTTTATAAGGAAGCCATGAATCACCCAGGCCATCTTAAACTATTTGTGACAAGGATCATG
CAAGACTTTGAAAGTGACACGTTTTTTCCAGAAATTGATTTGGAGAAATATAAACTTCTG
CCAGAATACCCAGGTGTTCTCTCTGATGTCCAGGAGGAGAAAGGCATTAAGTACAAATTT
GAAGTATATGAGAAGAATGATTAA
Enzyme 68 GenBank Gene ID J00140 Link Image
Enzyme 68 GeneCard ID DHFR Link Image
Enzyme 68 GenAtlas ID DHFR Link Image
Enzyme 68 HGNC ID HGNC:2861 Link Image
Enzyme 68 Chromosome Location 5
Enzyme 68 Locus 5q11.2-q13.2
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Chen MJ, Shimada T, Moulton AD, Cline A, Humphries RK, Maizel J, Nienhuis AW: The functional human dihydrofolate reductase gene. J Biol Chem. 1984 Mar 25;259(6):3933-43. [PubMed Link Image]
  2. Masters JN, Attardi G: The nucleotide sequence of the cDNA coding for the human dihydrofolic acid reductase. Gene. 1983 Jan-Feb;21(1-2):59-63. [PubMed Link Image]
  3. Yang JK, Masters JN, Attardi G: Human dihydrofolate reductase gene organization. Extensive conservation of the G + C-rich 5' non-coding sequence and strong intron size divergence from homologous mammalian genes. J Mol Biol. 1984 Jun 25;176(2):169-87. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Oefner C, D'Arcy A, Winkler FK: Crystal structure of human dihydrofolate reductase complexed with folate. Eur J Biochem. 1988 Jun 1;174(2):377-85. [PubMed Link Image]
  6. Davies JF 2nd, Delcamp TJ, Prendergast NJ, Ashford VA, Freisheim JH, Kraut J: Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. Biochemistry. 1990 Oct 9;29(40):9467-79. [PubMed Link Image]
  7. Stockman BJ, Nirmala NR, Wagner G, Delcamp TJ, DeYarman MT, Freisheim JH: Sequence-specific 1H and 15N resonance assignments for human dihydrofolate reductase in solution. Biochemistry. 1992 Jan 14;31(1):218-29. [PubMed Link Image]
  8. Lewis WS, Cody V, Galitsky N, Luft JR, Pangborn W, Chunduru SK, Spencer HT, Appleman JR, Blakley RL: Methotrexate-resistant variants of human dihydrofolate reductase with substitutions of leucine 22. Kinetics, crystallography, and potential as selectable markers. J Biol Chem. 1995 Mar 10;270(10):5057-64. [PubMed Link Image]
  9. Cody V, Galitsky N, Luft JR, Pangborn W, Rosowsky A, Blakley RL: Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523. Biochemistry. 1997 Nov 11;36(45):13897-903. [PubMed Link Image]
  10. Gangjee A, Vidwans AP, Vasudevan A, Queener SF, Kisliuk RL, Cody V, Li R, Galitsky N, Luft JR, Pangborn W: Structure-based design and synthesis of lipophilic 2,4-diamino-6-substituted quinazolines and their evaluation as inhibitors of dihydrofolate reductases and potential antitumor agents. J Med Chem. 1998 Aug 27;41(18):3426-34. [PubMed Link Image]
  11. Klon AE, Heroux A, Ross LJ, Pathak V, Johnson CA, Piper JR, Borhani DW: Atomic structures of human dihydrofolate reductase complexed with NADPH and two lipophilic antifolates at 1.09 a and 1.05 a resolution. J Mol Biol. 2002 Jul 12;320(3):677-93. [PubMed Link Image]
  12. Cody V, Galitsky N, Luft JR, Pangborn W, Gangjee A: Analysis of two polymorphic forms of a pyrido[2,3-d]pyrimidine N9-C10 reversed-bridge antifolate binary complex with human dihydrofolate reductase. Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):654-61. Epub 2003 Mar 25. [PubMed Link Image]
  13. Cody V, Luft JR, Pangborn W, Gangjee A: Analysis of three crystal structure determinations of a 5-methyl-6-N-methylanilino pyridopyrimidine antifolate complex with human dihydrofolate reductase. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1603-9. Epub 2003 Aug 19. [PubMed Link Image]
  14. Cody V, Luft JR, Pangborn W, Gangjee A, Queener SF: Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry. Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):646-55. Epub 2004 Mar 23. [PubMed Link Image]
  15. Cody V, Luft JR, Pangborn W: Understanding the role of Leu22 variants in methotrexate resistance: comparison of wild-type and Leu22Arg variant mouse and human dihydrofolate reductase ternary crystal complexes with methotrexate and NADPH. Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):147-55. Epub 2005 Jan 19. [PubMed Link Image]
  16. Kovalevskaya NV, Smurnyy YD, Polshakov VI, Birdsall B, Bradbury AF, Frenkiel T, Feeney J: Solution structure of human dihydrofolate reductase in its complex with trimethoprim and NADPH. J Biomol NMR. 2005 Sep;33(1):69-72. [PubMed Link Image]
  17. Reynolds RC, Campbell SR, Fairchild RG, Kisliuk RL, Micca PL, Queener SF, Riordan JM, Sedwick WD, Waud WR, Leung AK, Dixon RW, Suling WJ, Borhani DW: Novel boron-containing, nonclassical antifolates: synthesis and preliminary biological and structural evaluation. J Med Chem. 2007 Jul 12;50(14):3283-9. Epub 2007 Jun 15. [PubMed Link Image]
  18. Cody V, Pace J, Makin J, Piraino J, Queener SF, Rosowsky A: Correlations of inhibitor kinetics for Pneumocystis jirovecii and human dihydrofolate reductase with structural data for human active site mutant enzyme complexes. Biochemistry. 2009 Mar 3;48(8):1702-11. [PubMed Link Image]
  19. Volpato JP, Yachnin BJ, Blanchet J, Guerrero V, Poulin L, Fossati E, Berghuis AM, Pelletier JN: Multiple conformers in active site of human dihydrofolate reductase F31R/Q35E double mutant suggest structural basis for methotrexate resistance. J Biol Chem. 2009 Jul 24;284(30):20079-89. Epub 2009 May 28. [PubMed Link Image]
  20. Gangjee A, Li W, Kisliuk RL, Cody V, Pace J, Piraino J, Makin J: Design, synthesis, and X-ray crystal structure of classical and nonclassical 2-amino-4-oxo-5-substituted-6-ethylthieno[2,3-d]pyrimidines as dual thymidylate synthase and dihydrofolate reductase inhibitors and as potential antitumor agents. J Med Chem. 2009 Aug 13;52(15):4892-902. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 6127
Enzyme 69 Name Testosterone 17-beta-dehydrogenase 3
Enzyme 69 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase type 3
  2. 17-beta-HSD 3
  3. Testicular 17-beta-hydroxysteroid dehydrogenase
Enzyme 69 Gene Name HSD17B3
Enzyme 69 Protein Sequence >Testosterone 17-beta-dehydrogenase 3 
MGDVLEQFFILTGLLVCLACLAKCVRFSRCVLLNYWKVLPKSFLRSMGQWAVITGAGDGI
GKAYSFELAKRGLNVVLISRTLEKLEAIATEIERTTGRSVKIIQADFTKDDIYEHIKEKL
AGLEIGILVNNVGMLPNLLPSHFLNAPDEIQSLIHCNITSVVKMTQLILKHMESRQKGLI
LNISSGIALFPWPLYSMYSASKAFVCAFSKALQEEYKAKEVIIQVLTPYAVSTAMTKYLN
TNVITKTADEFVKESLNYVTIGGETCGCLAHEILAGFLSLIPAWAFYSGAFQRLLLTHYV
AYLKLNTKVR
Enzyme 69 Number of Residues 310
Enzyme 69 Molecular Weight 34515.3
Enzyme 69 Theoretical pI 8.84
Enzyme 69 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 69 General Function Involved in oxidoreductase activity
Enzyme 69 Specific Function Favors the reduction of androstenedione to testosterone. Uses NADPH while the two other EDH17B enzymes use NADH
Enzyme 69 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 69 Reactions
  • testosterone + NADP+ = androst-4-ene-3,17-dione + NADPH + H+ [RN:R01838]
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein Not Available
Enzyme 69 UniProtKB/Swiss-Prot ID P37058 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name DHB3_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >933 bp 
ATGGGGGACGTCCTGGAACAGTTCTTCATCCTCACAGGGCTGCTGGTGTGCCTGGCCTGC
CTGGCGAAGTGCGTGAGATTCTCCAGATGTGTTTTACTGAACTACTGGAAAGTTTTGCCA
AAGTCTTTCTTGCGGTCAATGGGACAGTGGGCAGTGATCACTGGAGCAGGCGATGGAATT
GGGAAAGCGTACTCGTTCGAGCTAGCAAAACGTGGACTCAATGTTGTCCTTATTAGCCGG
ACGCTGGAAAAACTAGAGGCCATTGCCACAGAGATCGAGCGGACTACAGGGAGGAGTGTG
AAGATTATACAAGCAGATTTTACAAAAGATGACATCTACGAGCATATTAAAGAAAAACTT
GCAGGCTTAGAAATTGGAATTTTAGTCAACAATGTCGGAATGCTTCCAAACCTTCTCCCA
AGCCATTTCCTGAACGCACCGGATGAAATCCAGAGCCTCATCCATTGTAACATCACCTCC
GTAGTCAAGATGACACAGCTAATTCTGAAACATATGGAATCAAGGCAGAAAGGTCTCATC
CTGAACATTTCTTCTGGGATAGCCCTGTTTCCTTGGCCTCTCTACTCCATGTACTCAGCT
TCCAAGGCGTTTGTGTGCGCATTTTCCAAGGCCCTGCAAGAGGAATATAAAGCAAAAGAA
GTCATCATCCAGGTGCTGACCCCATATGCTGTCTCGACTGCAATGACAAAGTATCTAAAT
ACAAATGTGATAACCAAGACTGCTGATGAGTTTGTCAAAGAGTCATTGAATTATGTCACA
ATTGGAGGTGAAACCTGTGGCTGCCTTGCCCATGAAATCTTGGCGGGCTTTCTGAGCCTG
ATCCCGGCCTGGGCCTTCTACAGCGGTGCCTTCCAAAGGCTGCTCCTGACACACTATGTG
GCATACCTGAAGCTCAACACCAAGGTCAGGTAG
Enzyme 69 GenBank Gene ID U05659 Link Image
Enzyme 69 GeneCard ID HSD17B3 Link Image
Enzyme 69 GenAtlas ID HSD17B3 Link Image
Enzyme 69 HGNC ID HGNC:5212 Link Image
Enzyme 69 Chromosome Location 9
Enzyme 69 Locus 9q22
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Geissler WM, Davis DL, Wu L, Bradshaw KD, Patel S, Mendonca BB, Elliston KO, Wilson JD, Russell DW, Andersson S: Male pseudohermaphroditism caused by mutations of testicular 17 beta-hydroxysteroid dehydrogenase 3. Nat Genet. 1994 May;7(1):34-9. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Andersson S, Geissler WM, Wu L, Davis DL, Grumbach MM, New MI, Schwarz HP, Blethen SL, Mendonca BB, Bloise W, Witchel SF, Cutler GB Jr, Griffin JE, Wilson JD, Russel DW: Molecular genetics and pathophysiology of 17 beta-hydroxysteroid dehydrogenase 3 deficiency. J Clin Endocrinol Metab. 1996 Jan;81(1):130-6. [PubMed Link Image]
  4. Bilbao JR, Loridan L, Audi L, Gonzalo E, Castano L: A novel missense (R80W) mutation in 17-beta-hydroxysteroid dehydrogenase type 3 gene associated with male pseudohermaphroditism. Eur J Endocrinol. 1998 Sep;139(3):330-3. [PubMed Link Image]
  5. Moghrabi N, Hughes IA, Dunaif A, Andersson S: Deleterious missense mutations and silent polymorphism in the human 17beta-hydroxysteroid dehydrogenase 3 gene (HSD17B3). J Clin Endocrinol Metab. 1998 Aug;83(8):2855-60. [PubMed Link Image]
  6. Lindqvist A, Hughes IA, Andersson S: Substitution mutation C268Y causes 17 beta-hydroxysteroid dehydrogenase 3 deficiency. J Clin Endocrinol Metab. 2001 Feb;86(2):921-3. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 6128
Enzyme 70 Name Estradiol 17-beta-dehydrogenase 1
Enzyme 70 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase type 1
  2. 17-beta-HSD 1
  3. 20 alpha-hydroxysteroid dehydrogenase
  4. 20-alpha-HSD
  5. E2DH
  6. Placental 17-beta-hydroxysteroid dehydrogenase
Enzyme 70 Gene Name HSD17B1
Enzyme 70 Protein Sequence >Estradiol 17-beta-dehydrogenase 1 
MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSL
ETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTV
RMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVH
LSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEV
FLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGG
GAGPGAEDEAGRSAVGDPELGDPPAAPQ
Enzyme 70 Number of Residues 328
Enzyme 70 Molecular Weight 34979.7
Enzyme 70 Theoretical pI 5.42
Enzyme 70 GO Classification
Function
  • binding
  • catalytic activity
  • estradiol 17-beta-dehydrogenase activity
  • oxidoreductase activity
  • steroid dehydrogenase activity
  • steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • estrogen biosynthetic process
  • lipid metabolic process
  • metabolic process
  • oxidation reduction
  • primary metabolic process
  • steroid biosynthetic process
  • steroid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 70 General Function Involved in estradiol 17-beta-dehydrogenase activity
Enzyme 70 Specific Function Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH
Enzyme 70 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 70 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02352 R02353]
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • None
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 23365 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID P14061 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name DHB1_HUMAN Link Image
Enzyme 70 PDB ID 1QYX Link Image
Enzyme 70 PDB File Show
Enzyme 70 3D Structure
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >987 bp 
ATGGCCCGCACCGTGGTGCTCATCACCGGCTGTTCCTCGGGCATCGGCCTGCACTTGGCC
GTACGTCTGGCTTCAGATCCATCCCAGAGCTTCAAAGTGTATGCCACGTTGAGGGACCTG
AAAACACAGGGCCGGCTGTGGGAGGCGGCCCGGGCCCTGGCATGCCCTCCGGGATCCCTG
GAGACGTTGCAGCTGGACGTAAGGGACTCAAAATCCGTGGCCGCTGCCCGGGAACGCGTG
ACTGAGGGCCGCGTGGACGTGCTGGTGTGTAACGCAGGCCTGGGCCTGCTGGGGCCGCTG
GAGGCGCTGGGGGAGGACGCCGTGGCCTCTGTGCTGGACGTGAATGTAGTAGGGACTGTG
CGGATGCTGCAGGCCTTCCTGCCAGACATGAAGAGGCGCGGTTCGGGACGCGTGTTGGTG
ACCGGGAGCGTGGGAGGATTGATGGGGCTGCCTTTCAATGACGTTTATTGCGCCAGCAAG
TTCGCGCTCGAAGGCTTATGCGAGAGTCTGGCGGTTCTGCTGCTGCCCTTTGGGGTCCAC
TTGAGCCTGATCGAGTGCGGCCCAGTGCACACCGCCTTCATGGAGAAGGTGTTGGGCAGC
CCAGAGGAGGTGCTGGACCGCACGGACATCCACACCTTCCACCGCTTCTACCAATACCTC
GCCCACAGCAAGCAAGTCTTTCGCGAGGCGGCGCAGAACCCTGAGGAGGTGGCGGAGGTC
TTCCTCACCGCTTTGCGCGCCCCGAAGCCGACCCTGCGCTACTTCACCACCGAGCGCTTC
CTGCCCCTGCTGCGGATGCGCCTGGACGACCCCAGCGGCTCCAACTACGTCACCGCCATG
CACCGGGAAGTGTTCGGCGACGTTCCGGCAAAGGCCGAGGCTGGGGCCGAGGCTGGGGGC
GGGGCCGGGCCTGGGGCAGAGGACGAGGCCGGGCGCAGTGCGGTGGGGGACCCTGAGCTC
GGCGATCCTCCGGCCGCCCCGCAGTAA
Enzyme 70 GenBank Gene ID X13440 Link Image
Enzyme 70 GeneCard ID HSD17B1 Link Image
Enzyme 70 GenAtlas ID HSD17B1 Link Image
Enzyme 70 HGNC ID HGNC:5210 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 17q11-q21
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Peltoketo H, Isomaa V, Maentausta O, Vihko R: Complete amino acid sequence of human placental 17 beta-hydroxysteroid dehydrogenase deduced from cDNA. FEBS Lett. 1988 Oct 24;239(1):73-7. [PubMed Link Image]
  2. Luu The V, Labrie C, Zhao HF, Couet J, Lachance Y, Simard J, Leblanc G, Cote J, Berube D, Gagne R, et al.: Characterization of cDNAs for human estradiol 17 beta-dehydrogenase and assignment of the gene to chromosome 17: evidence of two mRNA species with distinct 5'-termini in human placenta. Mol Endocrinol. 1989 Aug;3(8):1301-9. [PubMed Link Image]
  3. Luu-The V, Labrie C, Simard J, Lachance Y, Zhao HF, Couet J, Leblanc G, Labrie F: Structure of two in tandem human 17 beta-hydroxysteroid dehydrogenase genes. Mol Endocrinol. 1990 Feb;4(2):268-75. [PubMed Link Image]
  4. Luu-The V, Labrie C, Zhao HF, Couet J, Lachance Y, Simard J, Cote J, Leblanc G, Lagace L, Berube D, et al.: Purification, cloning, complementary DNA structure, and predicted amino acid sequence of human estradiol 17 beta-dehydrogenase. Ann N Y Acad Sci. 1990;595:40-52. [PubMed Link Image]
  5. Peltoketo H, Isomaa V, Vihko R: Genomic organization and DNA sequences of human 17 beta-hydroxysteroid dehydrogenase genes and flanking regions. Localization of multiple Alu sequences and putative cis-acting elements. Eur J Biochem. 1992 Oct 1;209(1):459-66. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Burns DJ, Engel LL, Bethune JL: Amino acid composition and subunit structure. Human placental 17 -estradiol dehydrogenase. Biochemistry. 1972 Jul 4;11(14):2699-703. [PubMed Link Image]
  9. Nicolas JC, Harris JI: Human placental 17 -oestradiol dehydrogenase. Sequence of a tryptic peptide containing an essential cysteine. FEBS Lett. 1973 Jan 15;29(2):173-6. [PubMed Link Image]
  10. Murdock GL, Chin CC, Warren JC: Human placental estradiol 17 beta-dehydrogenase: sequence of a histidine-bearing peptide in the catalytic region. Biochemistry. 1986 Feb 11;25(3):641-6. [PubMed Link Image]
  11. Murdock GL, Chin CC, Offord RE, Bradshaw RA, Warren JC: Human placental estradiol 17 beta-dehydrogenase. Identification of a single histidine residue affinity-labeled by both 3-bromoacetoxyestrone and 12 beta-bromoacetoxy-4-estrene-3,17-dione. J Biol Chem. 1983 Oct 10;258(19):11460-4. [PubMed Link Image]
  12. Baker ME: Human placental 17 beta-hydroxysteroid dehydrogenase is homologous to NodG protein of Rhizobium meliloti. Mol Endocrinol. 1989 May;3(5):881-4. [PubMed Link Image]
  13. Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX: Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution. Structure. 1995 May 15;3(5):503-13. [PubMed Link Image]
  14. Azzi A, Rehse PH, Zhu DW, Campbell RL, Labrie F, Lin SX: Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol. Nat Struct Biol. 1996 Aug;3(8):665-8. [PubMed Link Image]
  15. Breton R, Housset D, Mazza C, Fontecilla-Camps JC: The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors. Structure. 1996 Aug 15;4(8):905-15. [PubMed Link Image]
  16. Mazza C, Breton R, Housset D, Fontecilla-Camps JC: Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase. J Biol Chem. 1998 Apr 3;273(14):8145-52. [PubMed Link Image]
  17. Sawicki MW, Erman M, Puranen T, Vihko P, Ghosh D: Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+. Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):840-5. [PubMed Link Image]
  18. Han Q, Campbell RL, Gangloff A, Huang YW, Lin SX: Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17beta-hydroxysteroid dehydrogenase. C-18/c-19 steroid discrimination and enzyme-induced strain. J Biol Chem. 2000 Jan 14;275(2):1105-11. [PubMed Link Image]
  19. Qiu W, Campbell RL, Gangloff A, Dupuis P, Boivin RP, Tremblay MR, Poirier D, Lin SX: A concerted, rational design of type 1 17beta-hydroxysteroid dehydrogenase inhibitors: estradiol-adenosine hybrids with high affinity. FASEB J. 2002 Nov;16(13):1829-31. Epub 2002 Sep 5. [PubMed Link Image]
  20. Gangloff A, Shi R, Nahoum V, Lin SX: Pseudo-symmetry of C19 steroids, alternative binding orientations, and multispecificity in human estrogenic 17beta-hydroxysteroid dehydrogenase. FASEB J. 2003 Feb;17(2):274-6. Epub 2002 Dec 17. [PubMed Link Image]
  21. Shi R, Lin SX: Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation. J Biol Chem. 2004 Apr 16;279(16):16778-85. Epub 2004 Feb 13. [PubMed Link Image]
  22. Normand T, Narod S, Labrie F, Simard J: Detection of polymorphisms in the estradiol 17 beta-hydroxysteroid dehydrogenase II gene at the EDH17B2 locus on 17q11-q21. Hum Mol Genet. 1993 Apr;2(4):479-83. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 6129
Enzyme 71 Name 3-keto-steroid reductase
Enzyme 71 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 7
  2. 17-beta-HSD 7
  3. Estradiol 17-beta-dehydrogenase 7
Enzyme 71 Gene Name HSD17B7
Enzyme 71 Protein Sequence >3-keto-steroid reductase 
MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIV
QVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTA
EGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFS
LEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIW
TLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQ
KMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL
Enzyme 71 Number of Residues 341
Enzyme 71 Molecular Weight 38205.8
Enzyme 71 Theoretical pI 8.21
Enzyme 71 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 71 General Function Involved in oxidoreductase activity
Enzyme 71 Specific Function Responsible for the reduction of the keto group on the C-3 of sterols
Enzyme 71 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 71 Reactions
  • 4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+ [RN:R05691]
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • 230-250
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 6721095 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID P56937 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name DHB7_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >1026 bp 
ATGCGAAAGGTGGTTTTGATCACCGGGGCTAGCAGTGGCATTGGCCTGGCCCTCTGCAAG
CGGCTGCTGGCGGAAGATGATGAGCTTCATCTGTGTTTGGCGTGCAGGAACATGAGCAAG
GCAGAAGCTGTCTGTGCTGCTCTGCTGGCCTCTCACCCCACTGCTGAGGTCACCATTGTC
CAGGTGGATGTCAGCAACCTGCAGTCGGTCTTCCGGGCCTCCAAGGAACTTAAGCAAAGG
TTTCAGAGATTAGACTGTATATATCTAAATGCTGGGATCATGCCTAATCCACAACTAAAT
ATCAAAGCACTTTTCTTTGGCCTCTTTTCAAGAAAAGTGATTCATATGTTCTCCACAGCT
GAAGGCCTGCTGACCCAGGGTGATAAGATCACTGCTGATGGACTTCAGGAGGTGTTTGAG
ACCAATGTCTTTGGCCATTTTATCCTGATTCGGGAACTGGAGCCTCTCCTCTGTCACAGT
GACAATCCATCTCAGCTCATCTGGACATCATCTCGCAGTGCAAGGAAATCTAATTTCAGC
CTCGAGGACTTCCAGCACAGCAAAGGCAAGGAACCCTACAGCTCTTCCAAATATGCCACT
GACCTTTTGAGTGTGGCTTTGAACAGGAACTTCAACCAGCAGGGTCTCTATTCCAATGTG
GCCTGTCCAGGTACAGCATTGACCAATTTGACATATGGAATTCTGCCTCCGTTTATATGG
ACGCTGTTGATGCCGGCAATATTGCTACTTCGCTTTTTTGCAAATGCATTCACTTTGACA
CCATATAATGGAACAGAAGCTCTGGTATGGCTTTTCCACCAAAAGCCTGAATCTCTCAAT
CCTCTGATCAAATATCTGAGTGCCACCACTGGCTTTGGAAGAAATTATATTATGACCCAG
AAGATGGACCTAGATGAAGACACTGCTGAAAAATTTTATCAAAAGTTACTGGAACTGGAA
AAGCACATTAGGGTCACTATTCAAAAAACAGATAATCAGGCCAGGCTCAGTGGCTCATGC
CTATAA
Enzyme 71 GenBank Gene ID AF098786 Link Image
Enzyme 71 GeneCard ID HSD17B7 Link Image
Enzyme 71 GenAtlas ID HSD17B7 Link Image
Enzyme 71 HGNC ID HGNC:5215 Link Image
Enzyme 71 Chromosome Location 1
Enzyme 71 Locus 1q23
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Krazeisen A, Breitling R, Imai K, Fritz S, Moller G, Adamski J: Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7(1). FEBS Lett. 1999 Oct 29;460(2):373-9. [PubMed Link Image]
  2. Torn S, Nokelainen P, Kurkela R, Pulkka A, Menjivar M, Ghosh S, Coca-Prados M, Peltoketo H, Isomaa V, Vihko P: Production, purification, and functional analysis of recombinant human and mouse 17beta-hydroxysteroid dehydrogenase type 7. Biochem Biophys Res Commun. 2003 May 23;305(1):37-45. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Marijanovic Z, Laubner D, Moller G, Gege C, Husen B, Adamski J, Breitling R: Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis. Mol Endocrinol. 2003 Sep;17(9):1715-25. Epub 2003 Jun 26. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 6133
Enzyme 72 Name Alpha-aminoadipic semialdehyde synthase, mitochondrial
Enzyme 72 Synonyms
  1. LKR/SDH
  2. Lysine ketoglutarate reductase
  3. LKR
  4. LOR
  5. Saccharopine dehydrogenase
  6. SDH
Enzyme 72 Gene Name AASS
Enzyme 72 Protein Sequence >Alpha-aminoadipic semialdehyde synthase, mitochondrial 
MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQ
PSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANM
GLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFM
HIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPC
EYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIA
PYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTG
GSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLY
PYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTR
RKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKL
GFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGE
LGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMN
VMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTL
LRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLK
EAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRD
SFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFS
KEIYGPILERIKAEGIIYTTQSTIKP
Enzyme 72 Number of Residues 926
Enzyme 72 Molecular Weight 102130.9
Enzyme 72 Theoretical pI 6.62
Enzyme 72 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 72 General Function Involved in oxidoreductase activity
Enzyme 72 Specific Function Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively
Enzyme 72 Pathways
Enzyme 72 Reactions
  • N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ [RN:R02313]
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • None
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein Not Available
Enzyme 72 UniProtKB/Swiss-Prot ID Q9UDR5 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name AASS_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >2781 bp 
ATGCTGCAAGTACATAGGACTGGACTGGGCAGGCTGGGGGTCAGCCTCTCCAAGGGTCTT
CACCACAAAGCTGTGTTGGCCGTCCGGAGGGAGGATGTGAACGCCTGGGAGAGAAGGGCC
CCGCTAGCTCCCAAGCACATCAAAGGCATCACCAATCTGGGATACAAGGTCTTGATACAG
CCTTCGAATCGGCGGGCCATTCATGATAAGGACTATGTCAAAGCTGGTGGCATTCTTCAG
GAGGATATTTCTGAAGCTTGTCTAATTTTAGGAGTTAAAAGACCTCCAGAGGAAAAATTA
ATGTCCAGGAAGACTTATGCATTTTTCTCCCACACAATAAAAGCTCAGGAGGCCAATATG
GGCTTGTTGGATGAGATTCTAAAACAGGAAATTCGCCTTATTGATTATGAGAAAATGGTG
GATCATAGAGGAGTACGGGTAGTGGCATTTGGACAGTGGGCTGGTGTGGCAGGAATGATC
AACATTTTACATGGAATGGGTTTAAGGCTCCTTGCTTTGGGACATCACACACCTTTTATG
CACATTGGCATGGCTCATAACTACAGGAATAGCAGTCAGGCTGTGCAAGCTGTCCGTGAT
GCTGGCTATGAAATATCTTTGGGTTTGATGCCTAAGTCAATAGGACCCTTAACATTTGTG
TTCACAGGAACTGGTAATGTTTCTAAGGGAGCCCAAGCAATCTTTAATGAGCTACCTTGT
GAATATGTGGAGCCCCATGAATTAAAAGAAGTTTCCCAAACTGGAGACCTCAGAAAAGTG
TATGGGACGGTGTTAAGTCGTCATCATCATCTTGTCAGGAAAACAGATGCTGTGTATGAT
CCTGCAGAGTATGACAAACATCCGGAGCGCTACATAAGTCGTTTTAATACTGATATTGCA
CCCTATACAACTTGCTTAATTAATGGAATCTACTGGGAACAAAACACTCCTCGCCTCCTA
ACCCGCCAAGATGCTCAGAGTCTCCTGGCTCCGGGCAAGTTCTCACCTGCTGGTGTGGAA
GGCTGCCCTGCATTACCACACAAACTCGTGGCAATATGTGACATTTCAGCTGACACAGGA
GGGTCTATAGAGTTTATGACTGAGTGTACAACAATAGAGCATCCCTTTTGCATGTATGAT
GCAGACCAGCATATTATTCATGACAGTGTTGAAGGCTCGGGGATCCTGATGTGTTCCATT
GACAATTTGCCGGCACAGCTCCCAATTGAAGCTACAGAATGCTTTGGAGACATGCTTTAC
CCTTATGTTGAAGAAATGATATTATCAGACGCGACACAGCCTCTTGAAAGTCAGAATTTT
TCTCCTGTGGTGAGAGATGCAGTGATTACATCCAACGGTACATTACCTGATAAATATAAA
TATATCCAGACACTCCGGGAGAGCAGGGAACGTGCTCAGTCACTTTCAATGGGCACCAGG
AGAAAGGTTTTGGTTCTTGGATCTGGCTACATATCTGAGCCTGTATTAGAATATTTATCA
AGAGATGGCAATATAGAAATAACAGTAGGATCTGACATGAAGAATCAAATTGAACAGTTA
GGCAAGAAATATAATATTAATCCTGTTAGCATGGACATTTGTAAACAAGAAGAGAAGCTG
GGCTTCTTGGTGGCAAAACAGGATCTTGTCATCAGCTTGTTGCCTTATGTATTGCACCCT
CTTGTGGCCAAGGCCTGCATCACAAACAAAGTTAACATGGTCACTGCAAGCTACATCACA
CCAGCACTAAAAGAATTGGAAAAGAGTGTGGAAGATGCTGGCATCACAATCATTGGTGAA
TTGGGATTGGACCCTGGTCTGGATCACATGTTAGCAATGGAAACAATAGATAAAGCCAAG
GAAGTGGGAGCCACGATTGAATCATATATTTCCTACTGTGGTGGGCTTCCAGCCCCTGAA
CATTCAAACAATCCATTGAGATATAAATTTAGCTGGAGTCCAGTGGGAGTTTTGATGAAT
GTAATGCAGTCTGCCACCTATCTGCTCGATGGAAAGGTTGTGAATGTTGCAGGAGGCATC
TCCTTTCTTGATGCCGTTACGTCCATGGATTTTTTTCCAGGATTAAATTTGGAAGGCTAT
CCTAACAGAGACAGTACGAAATATGCTGAGATTTATGGCATTTCTTCTGCTCACACTTTG
TTGCGGGGGACACTGAGATATAAGGGATATATGAAAGCTTTGAATGGATTTGTAAAATTA
GGTCTTATAAACAGAGAAGCGCTTCCTGCCTTTAGACCTGAGGCCAACCCTCTCACCTGG
AAACAACTCCTCTGTGACCTAGTTGGGATTTCACCCTCCTCTGAGCATGATGTGTTGAAG
GAAGCTGTTCTTAAGAAACTAGGAGGAGACAATACCCAGTTGGAGGCTGCTGAATGGTTG
GGCTTACTTGGGGATGAACAAGTTCCTCAGGCAGAGTCCATTCTGGATGCCCTCTCCAAG
CATTTGGTCATGAAGCTTTCCTATGGTCCTGAAGAAAAAGATATGATTGTGATGAGAGAC
AGCTTTGGAATCAGACATCCTTCTGGACATTTAGAACATAAAACGATTGATCTTGTGGCT
TATGGGGACATCAATGGCTTTTCAGCCATGGCTAAAACCGTGGGGTTACCCACCGCCATG
GCAGCCAAAATGTTGCTTGATGGTGAAATTGGAGCCAAAGGCCTAATGGGGCCCTTTTCA
AAGGAGATCTATGGACCAATATTGGAGCGAATTAAAGCAGAAGGCATTATATATACTACA
CAGAGTACAATTAAACCATAA
Enzyme 72 GenBank Gene ID AF229180 Link Image
Enzyme 72 GeneCard ID AASS Link Image
Enzyme 72 GenAtlas ID AASS Link Image
Enzyme 72 HGNC ID HGNC:17366 Link Image
Enzyme 72 Chromosome Location 7
Enzyme 72 Locus 7q31.3
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Sacksteder KA, Biery BJ, Morrell JC, Goodman BK, Geisbrecht BV, Cox RP, Gould SJ, Geraghty MT: Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia. Am J Hum Genet. 2000 Jun;66(6):1736-43. Epub 2000 Apr 20. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 6135
Enzyme 73 Name Delta-1-pyrroline-5-carboxylate synthase
Enzyme 73 Synonyms
  1. P5CS
  2. Aldehyde dehydrogenase family 18 member A1
  3. Glutamate 5-kinase
  4. GK
  5. Gamma-glutamyl kinase
  6. Gamma-glutamyl phosphate reductase
  7. GPR
  8. Glutamate-5-semialdehyde dehydrogenase
  9. Glutamyl-gamma-semialdehyde dehydrogenase
Enzyme 73 Gene Name ALDH18A1
Enzyme 73 Protein Sequence >Delta-1-pyrroline-5-carboxylate synthase 
MLSQVYRCGFQPFNQHLLPWVKCTTVFRSHCIQPSVIRHVRSWSNIPFITVPLSRTHGKS
FAHRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAV
AFGKQRLRHEILLSQSVRQALHSGQNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQY
SICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVNV
ISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTK
SRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSGHVITDIVEGKKVGTFFSEVKPAG
PTVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAA
PLLKRLSLSTSKLNSLAIGLRQIAASSQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIF
ESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLVNTRE
EVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRL
VRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSE
VKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVF
WNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSDFSEHGSL
KYLHENLPIPQRNTN
Enzyme 73 Number of Residues 795
Enzyme 73 Molecular Weight 87301.5
Enzyme 73 Theoretical pI 7.13
Enzyme 73 GO Classification
Function
  • catalytic activity
  • glutamate 5-kinase activity
  • glutamate-5-semialdehyde dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline biosynthetic process
  • proline metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 73 General Function Involved in oxidoreductase activity
Enzyme 73 Specific Function ATP + L-glutamate = ADP + L-glutamate 5- phosphate
Enzyme 73 Pathways Not Available
Enzyme 73 Reactions
  • ATP + L-glutamate = ADP + L-glutamate 5-phosphate [RN:R00239]
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • None
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 1304314 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID P54886 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name P5CS_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >2388 bp 
ATGTTGAGTCAAGTTTACCGCTGTGGGTTCCAGCCCTTCAACCAACATCTTCTGCCCTGG
GTCAAGTGTACAACCGTCTTCAGATCTCATTGTATCCAGCCTTCAGTCATCAGACATGTT
CGTTCTTGGAGCAACATCCCGTTTATCACTGTACCCCTCAGTCGTACACATGGCAAGTCC
TTCGCCCACCGCAGTGAGCTGAAGCATGCCAAGAGAATCGTGGTGAAGCTCGGCAGTGCC
GTGGTGACCCGAGGGGATGAATGTGGCCTGGCCCTGGGGCGCTTGGCATCTATTGTTGAG
CAGGTATCAGTGCTGCAGAATCAGGGCAGAGAGATGATGCTGGTGACCAGTGGAGCCGTA
GCCTTTGGCAAACAAACGTTGCGCCATGAGATCCTTCTGTCTCAGAGCGTGCGGCAGGCC
CTCCACTCGGGGCAGAACCAGCTGAAAGAAATGGCAATTCCAGTCTTAGAGGCACGAGCC
TGTGCAGCTGCCGGACAGAGTGGGCTGATGGCCTTGTATGAGGCTATGTTTACCCAGTAC
AGCATCTGTGCTGCCCAGATTTTGGTGACCAATTTGGATTTCCATGATGAGCAGAAGCGC
CGGAACCTCAATGGAACACTTCATGAACTCCTTAGAATGAACATTGTCCCCATTGTCAAC
ACAAATGATGCTGTTGTCCCCCCAGCTGAGCCCAACAGTGACCTGCAGGGGGTAAATGTT
ATTAGTGTTAAAGATAATGATAGCCTGGCTGCCCGACTGGCTGTGGAAATGAAAACTGAT
CTCTTGATTGTCCTTCCAGATGTAGAAGGCCTTTTTGACAGCCCCCCAGGTTCAGATGAT
GCAAAGCTTATTGATATATTTTATCCCGGAGATCAGCAGTCTGTGACATTTGGACCCAAG
TCTAGAGTGGGAAATGGGTGCATGGAAGCCAAGGTGAAAAGCACCCTCTGGGCTTTGCAA
GGTGGCACTTCTGTTGTTATTGCCAATGGAACCCACCCAAAGGTGTCTGGGCACGTCATC
ACAGACATTGTGGAGGGGAAGAAAGTTGGTACCTTCTTTTCAGAAGTAAAGCCTGCAGGC
CCTACTGTTGAGCAGCAGGGAGAAATGGCGCGATCTGGAGGAAGGATGTTGGCCACCTTG
GAACCTGAGCAGAGAGCAGAAATTATCCATCATCTGGCTGATCTGTTGACGGACCAGCGT
GATGAGATCCTGTTAGCCAACAAAAAAGACTTGGAGGAGGCAGAGGGGAGACTTGCAGCT
CCTCTGCTGAAACGTTTAAGCCTCTCCACATCCAAATTGAACAGCCTGGCCATCGGTCTG
CGACAGATCGCAGCCTCCTCCCAGGACAGCGTGGGACGTGTTTTGCGCCGCACCCGAATC
GCCAAAAACTTGGAACTGGAACAAGTGACTGTCCCAATTGGAGTTCTGCTGGTGATCTTT
GAATCTCGTCCTGACTGTCCTACCCCAGGTGGCAGCTTTGCTATCGCAAGTGGCAATGGC
TTGTTACTCAAAGGAGGGAAGGAGGCTGCACACAGCAACCGGATTCTCCACCTCCTGACC
CAGGAGGCTCTCTCAATCCATGGAGTCAAGGAGGCCGTGCAACTGGTGAATACCAGAGAA
GAAGTTGAAGATCTTTGCCGCCTAGACAAAATGATAGATCTGATCATTCCACGTGGCTCT
TCCCAGCTGGTCAGAGACATCCAGAAAGCTGCTAAGGGGATTCCAGTGATGGGGCACAGC
GAAGGGATCTGTCACATGTATGTGGATTCCGAGGCCAGTGTTGATAAGGTCACCAGGCTA
GTCAGAGACTCTAAATGTGAATATCCAGCTGCCTGTAATGCTTTGGAGACTTTGTTAATC
CACCGGGATCTGCTCAGGACACCATTATTTGACCAGATCATTGATATGCTGAGAGTGGAA
CAGGTAAAAATTCATGCAGGCCCCAAATTTGCCTCCTATCTGACCTTCAGCCCCTCCGAA
GTGAAGTCACTCCGAACTGAGTATGGGGACCTGGAATTATGCATTGAAGTAGTGGACAAC
GTTCAGGATGCCATTGACCACATCCACAAGTATGGCAGCTCCCACACGGATGTCATCGTC
ACAGAGGACGAAAACACAGCGGAGTTCTTCCTGCAGCACGTAGACAGTGCCTGTGTGTTC
TGGAATGCCAGCACTCGCTTTTCTGATGGTTACCGCTTTGGACTGGGAGCTGAAGTGGGA
ATCAGTACATCGAGAATCCACGCCCGGGGACCAGTAGGACTTGAGGGACTGCTTACTACT
AAGTGGCTGCTGCGAGGGAAGGACCACGTGGTCTCAGATTTCTCAGAGCATGGAAGTTTA
AAATATCTTCATGAGAACCTCCCTATTCCTCAGAGAAACACCAACTGA
Enzyme 73 GenBank Gene ID X94453 Link Image
Enzyme 73 GeneCard ID ALDH18A1 Link Image
Enzyme 73 GenAtlas ID ALDH18A1 Link Image
Enzyme 73 HGNC ID HGNC:9722 Link Image
Enzyme 73 Chromosome Location 1
Enzyme 73 Locus 10q24.3
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Aral B, Schlenzig JS, Liu G, Kamoun P: Database cloning human delta 1-pyrroline-5-carboxylate synthetase (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in proline biosynthesis. C R Acad Sci III. 1996 Mar;319(3):171-8. [PubMed Link Image]
  2. Hu CA, Lin WW, Obie C, Valle D: Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem. 1999 Mar 5;274(10):6754-62. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Baumgartner MR, Hu CA, Almashanu S, Steel G, Obie C, Aral B, Rabier D, Kamoun P, Saudubray JM, Valle D: Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. Hum Mol Genet. 2000 Nov 22;9(19):2853-8. [PubMed Link Image]
  7. Bicknell LS, Pitt J, Aftimos S, Ramadas R, Maw MA, Robertson SP: A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome. Eur J Hum Genet. 2008 Oct;16(10):1176-86. Epub 2008 May 14. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 6138
Enzyme 74 Name NADP-dependent malic enzyme
Enzyme 74 Synonyms
  1. NADP-ME
  2. Malic enzyme 1
Enzyme 74 Gene Name ME1
Enzyme 74 Protein Sequence >NADP-dependent malic enzyme 
MEPEAPRRRHTHQRGYLLTRNPHLNKDLAFTLEERQQLNIHGLLPPSFNSQEIQVLRVVK
NFEHLNSDFDRYLLLMDLQDRNEKLFYRVLTSDIEKFMPIVYTPTVGLACQQYSLVFRKP
RGLFITIHDRGHIASVLNAWPEDVIKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTAC
GGMNPQECLPVILDVGTENEELLKDPLYIGLRQRRVRGSEYDDFLDEFMEAVSSKYGMNC
LIQFEDFANVNAFRLLNKYRNQYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTILFQ
GAGEAALGIAHLIVMALEKEGLPKEKAIKKIWLVDSKGLIVKGRASLTQEKEKFAHEHEE
MKNLEAIVQEIKPTALIGVAAIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECSAEQC
YKITKGRAIFASGSPFDPVTLPNGQTLYPGQGNNSYVFPGVALGVVACGLRQITDNIFLT
TAEVIAQQVSDKHLEEGRLYPPLNTIRDVSLKIAEKIVKDAYQEKTATVYPEPQNKEAFV
RSQMYSTDYDQILPDCYSWPEEVQKIQTKVDQ
Enzyme 74 Number of Residues 572
Enzyme 74 Molecular Weight 64149.1
Enzyme 74 Theoretical pI 6.01
Enzyme 74 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • malate dehydrogenase activity
  • malic enzyme activity
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • dicarboxylic acid metabolic process
  • malate metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
—
Enzyme 74 General Function Involved in oxidoreductase activity
Enzyme 74 Specific Function (S)-malate + NADP(+) = pyruvate + CO(2) + NADPH
Enzyme 74 Pathways
Enzyme 74 Reactions
  • (S)-malate + NADP+ = pyruvate + CO2 + NADPH [RN:R00216]
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • None
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 495123 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID P48163 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name MAOX_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >1719 bp 
ATGGAGCCCGAAGCCCCCCGTCGCCGCCACACCCATCAGCGCGGCTACCTGCTGACACGG
AACCCTCACCTCAACAAGGACTTGGCCTTTACCCTGGAAGAGAGACAGCAATTGAACATT
CATGGATTGTTGCCACCTTCCTTCAACAGTCAGGAGATCCAGGTTCTTAGAGTAGTAAAA
AATTTCGAGCATCTGAACTCTGACTTTGACAGGTATCTTCTCTTAATGGATCTCCAAGAT
AGAAATGAAAAACTCTTTTATAGAGTGCTGACATCTGACATTGAGAAATTCATGCCTATT
GTTTATACTCCCACTGTGGGTCTGGCTTGCCAACAATATAGTTTGGTGTTTCGGAAGCCA
AGAGGTCTCTTTATTACTATCCACGATCGAGGGCATATTGCTTCAGTTCTCAATGCATGG
CCAGAAGATGTCATCAAGGCCATTGTGGTGACTGATGGAGAGCGTATTCTTGGCTTGGGA
GACCTTGGCTGTAATGGAATGGGCATCCCTGTGGGTAAATTGGCTCTATATACAGCTTGC
GGAGGGATGAATCCTCAAGAATGTCTGCCTGTCATTCTGGATGTGGGAACCGAAAATGAG
GAGTTACTTAAAGATCCACTCTACATTGGACTACGGCAGAGAAGAGTAAGAGGTTCTGAA
TATGATGATTTTTTGGACGAATTCATGGAGGCAGTTTCTTCCAAGTATGGCATGAATTGC
CTTATTCAGTTTGAAGATTTTGCCAATGTGAATGCATTTCGTCTCCTGAACAAGTATCGA
AACCAGTATTGCACATTCAATGATGATATTCAAGGAACAGCATCTGTTGCAGTTGCAGGT
CTCCTTGCAGCTCTTCGAATAACCAAGAACAAACTGTCTGATCAAACAATACTATTCCAA
GGAGCTGGAGAGGCTGCCCTAGGGATTGCACACCTGATTGTGATGGCCTTGGAAAAAGAA
GGTTTACCAAAAGAGAAAGCCATCAAAAAGATATGGCTGGTTGATTCAAAAGGATTAATA
GTTAAGGGACGTGCTTCCTTAACACAAGAGAAAGAGAAGTTTGCCCATGAACATGAAGAA
ATGAAGAACCTAGAAGCCATTGTTCAAGAAATAAAACCAACTGCCCTCATAGGAGTTGCT
GCAATTGGTGGTGCATTCTCAGAACAAATTCTCAAAGATATGGCTGCCTTCAATGAACGG
CCTATTATTTTTGCTTTGAGTAATCCAACTAGCAAAGCAGAATGTTCTGCAGAGCAGTGC
TACAAAATAACCAAGGGACGTGCAATTTTTGCCAGTGGCAGTCCTTTTGATCCAGTCACT
CTTCCAAATGGACAGACCCTATATCCTGGCCAAGGCAACAATTCCTACGTGTTCCCTGGA
GTTGCTCTTGGTGTTGTGGCGTGTGGATTGAGGCAGATCACAGATAATATTTTCCTCACT
ACTGCTGAGGTTATAGCTCAGCAAGTGTCAGATAAACACTTGGAAGAGGGTCGGCTTTAT
CCTCCTTTGAATACCATTAGAGATGTTTCTCTGAAAATTGCAGAAAAGATTGTGAAAGAT
GCATACCAAGAAAAGACAGCCACAGTTTATCCTGAACCGCAAAACAAAGAAGCATTTGTC
CGCTCCCAGATGTATAGTACTGATTATGACCAGATTCTACCTGATTGTTATTCTTGGCCT
GAAGAGGTGCAGAAAATACAGACCAAAGTTGACCAGTAG
Enzyme 74 GenBank Gene ID X77244 Link Image
Enzyme 74 GeneCard ID ME1 Link Image
Enzyme 74 GenAtlas ID ME1 Link Image
Enzyme 74 HGNC ID HGNC:6983 Link Image
Enzyme 74 Chromosome Location 6
Enzyme 74 Locus 6q12
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Loeber G, Dworkin MB, Infante A, Ahorn H: Characterization of cytosolic malic enzyme in human tumor cells. FEBS Lett. 1994 May 16;344(2-3):181-6. [PubMed Link Image]
  2. Gonzalez-Manchon C, Ferrer M, Ayuso MS, Parrilla R: Cloning, sequencing and functional expression of a cDNA encoding a NADP-dependent malic enzyme from human liver. Gene. 1995 Jul 4;159(2):255-60. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chou WY, Huang SM, Chang GG: Nonidentity of the cDNA sequence of human breast cancer cell malic enzyme to that from the normal human cell. J Protein Chem. 1996 Apr;15(3):273-9. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 6140
Enzyme 75 Name NADP-dependent malic enzyme, mitochondrial
Enzyme 75 Synonyms
  1. NADP-ME
  2. Malic enzyme 3
Enzyme 75 Gene Name ME3
Enzyme 75 Protein Sequence >NADP-dependent malic enzyme, mitochondrial 
MGAALGTGTRLAPWPGRACGALPRWTPTAPAQGCHSKPGPARPVPLKKRGYDVTRNPHLN
KGMAFTLEERLQLGIHGLIPPCFLSQDVQLLRIMRYYERQQSDLDKYIILMTLQDRNEKL
FYRVLTSDVEKFMPIVYTPTVGLACQHYGLTFRRPRGLFITIHDKGHLATMLNSWPEDNI
KAVVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVNPQQCLPVLLDVGTNNEELLRD
PLYIGLKHQRVHGKAYDDLLDEFMQAVTDKFGINCLIQFEDFANANAFRLLNKYRNKYCM
FNDDIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKA
EATRKIWMVDSKGLIVKGRSHLNHEKEMFAQDHPEVNSLEEVVRLVKPTAIIGVAAIAGA
FTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTEGRGIFASGSPFKSVTLEDGK
TFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLST
IRDVSLRIAIKVLDYAYKHNLASYYPEPKDKEAFVRSLVYTPDYDSFTLDSYTWPKEAMN
VQTV
Enzyme 75 Number of Residues 604
Enzyme 75 Molecular Weight 67067.9
Enzyme 75 Theoretical pI 8.07
Enzyme 75 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • malate dehydrogenase activity
  • malic enzyme activity
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • dicarboxylic acid metabolic process
  • malate metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
—
Enzyme 75 General Function Involved in oxidoreductase activity
Enzyme 75 Specific Function (S)-malate + NADP(+) = pyruvate + CO(2) + NADPH
Enzyme 75 Pathways
Enzyme 75 Reactions
  • (S)-malate + NADP+ = pyruvate + CO2 + NADPH [RN:R00216]
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 535012 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q16798 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name MAON_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >1815 bp 
ATGGGTGCCGCGCTGGGGACAGGCACGCGGCTGGCTCCCTGGCCGGGCCGGGCCTGCGGC
GCCCTCCCGCGCTGGACACCCACCGCGCCCGCCCAAGGCTGCCACTCCAAGCCTGGCCCG
GCGCGCCCTGTGCCCCTGAAGAAGCGCGGATACGATGTCACCAGGAACCCTCATCTCAAC
AAGGGGATGGCCTTTACCCTTGAAGAAAGGCTGCAGCTTGGAATCCACGGCCTAATCCCG
CCCTGCTTTCTGAGCCAGGACGTCCAGCTCCTCCGAATCATGAGATATTACGAGCGGCAG
CAGAGTGACCTGGACAAGTACATCATTCTCATGACACTCCAAGACCGGAACGAGAAGCTC
TTCTACCGAGTGCTGACTTCGGATGTGGAGAAGTTCATGCCAATCGTGTACACGCCTACC
GTGGGGCTGGCCTGTCAGCACTATGGCCTGACTTTCCGCAGGCCCCGTGGACTGTTCATC
ACCATTCATGACAAAGGTCATCTTGCAACAATGCTGAATTCTTGGCCAGAAGACAATATT
AAGGCCGTGGTGGTGACTGATGGGGAGCGCATCCTGGGCCTGGGAGACCTGGGCTGCTAC
GGCATGGGCATCCCTGTGGGCAAGCTGGCCCTGTACACGGCATGCGGAGGGGTGAACCCG
CAGCAGTGCCTCCCTGTGCTGCTGGACGTCGGCACCAACAATGAGGAGCTGCTCAGAGAC
CCTCTGTACATCGGCCTGAAACACCAGCGCGTGCACGGGAAGGCATACGATGACTTGCTG
GATGAGTTCATGCAGGCTGTGACAGACAAGTTTGGAATAAATTGCCTCATCCAATTTGAA
GACTTCGCCAATGCCAATGCCTTCCGCCTGCTCAACAAATACCGTAACAAGTACTGCATG
TTCAATGATGACATCCAAGGCACAGCCTCCGTTGCTGTGGCAGGGATCTTGGCTGCTCTG
CGAATCACCAACAACAAGCTTTCCAATCACGTGTTTGTTTTCCAAGGTGCAGGCGAGGCA
GCTATGGGCATTGCCCACCTCCTTGTCATGGCCCTAGAGAAAGAAGGTGTACCGAAGGCA
GAGGCCACAAGAAAGATCTGGATGGTGGACTCTAAAGGGCTCATTGTCAAGGGGAGGAGC
CACCTGAACCATGAAAAGGAGATGTTTGCCCAAGACCATCCTGAAGTCAACTCCCTGGAG
GAGGTGGTGAGGCTGGTGAAGCCCACAGCCATCATAGGTGTTGCTGCCATCGCAGGAGCC
TTCACGGAGCAGATTCTGAGGGACATGGCCTCCTTCCACGAGCGCCCTATCATCTTTGCC
CTGAGCAACCCCACCAGCAAGGCCGAGTGCACGGCTGAGAAGTGCTACCGGGTCACCGAG
GGCCGAGGGATTTTTGCCAGTGGAAGTCCTTTTAAGAGTGTGACTCTGGAAGATGGCAAG
ACCTTCATTCCTGGGCAGGGAAACAATGCTTACGTGTTCCCCGGGGTGGCACTGGGAGTC
ATCGCCGGCGGGATCCGGCACATCCCAGATGAGATCTTCCTCCTGACAGCAGAGCAAATT
GCCCAGGAAGTCTCTGAGCAGCATCTGTCCCAGGGGAGACTCTATCCACCACTCAGCACC
ATCCGAGACGTGTCTTTGAGAATTGCCATCAAAGTTCTCGACTACGCGTACAAACACAAC
CTGGCTTCCTACTACCCAGAGCCTAAGGACAAGGAGGCTTTTGTAAGATCCCTGGTCTAC
ACTCCAGACTATGACTCCTTTACACTGGACAGCTACACTTGGCCCAAGGAAGCCATGAAT
GTTCAGACGGTCTGA
Enzyme 75 GenBank Gene ID X79440 Link Image
Enzyme 75 GeneCard ID ME3 Link Image
Enzyme 75 GenAtlas ID ME3 Link Image
Enzyme 75 HGNC ID HGNC:6985 Link Image
Enzyme 75 Chromosome Location 1
Enzyme 75 Locus 11cen-q22.3
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Loeber G, Maurer-Fogy I, Schwendenwein R: Purification, cDNA cloning and heterologous expression of the human mitochondrial NADP(+)-dependent malic enzyme. Biochem J. 1994 Dec 15;304 ( Pt 3):687-92. [PubMed Link Image]
  2. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 6143
Enzyme 76 Name NAD-dependent malic enzyme, mitochondrial
Enzyme 76 Synonyms
  1. NAD-ME
  2. Malic enzyme 2
Enzyme 76 Gene Name ME2
Enzyme 76 Protein Sequence >NAD-dependent malic enzyme, mitochondrial 
MLSRLRVVSTTCTLACRHLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIET
QDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLAC
SQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIP
VGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMK
AITDRYGRNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISK
PISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDS
YQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALS
NPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVIL
CNTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMA
FRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITE
Enzyme 76 Number of Residues 584
Enzyme 76 Molecular Weight 65442.9
Enzyme 76 Theoretical pI 7.67
Enzyme 76 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • malate dehydrogenase activity
  • malic enzyme activity
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • dicarboxylic acid metabolic process
  • malate metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
—
Enzyme 76 General Function Involved in oxidoreductase activity
Enzyme 76 Specific Function (S)-malate + NAD(+) = pyruvate + CO(2) + NADH
Enzyme 76 Pathways
Enzyme 76 Reactions
  • (S)-malate + NAD+ = pyruvate + CO2 + NADH [RN:R00214]
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein Not Available
Enzyme 76 UniProtKB/Swiss-Prot ID P23368 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name MAOM_HUMAN Link Image
Enzyme 76 PDB ID 1QR6 Link Image
Enzyme 76 PDB File Show
Enzyme 76 3D Structure
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >1755 bp 
ATGTTGTCCCGGTTAAGAGTAGTTTCCACCACTTGTACTTTGGCATGTCGACATTTGCAC
ATAAAAGAAAAAGGCAAGCCACTTATGCTGAACCCAAGAACAAACAAGGGAATGGCATTT
ACTTTACAAGAACGACAAATGCTTGGTCTTCAAGGACTTCTACCTCCCAAAATAGAGACA
CAAGATATTCAAGCCTTACGATTTCATAGAAACTTGAAGAAAATGACTAGCCCTTTGGAA
AAATATATCTACATAATGGGAATACAAGAAAGAAATGAGAAATTGTTTTATAGAATACTG
CAAGATGACATTGAGAGTTTAATGCCAATTGTATATACACCGACGGTTGGTCTTGCCTGC
TCCCAGTATGGACACATCTTTAGAAGACCTAAGGGATTATTTATTTCGATCTCAGACAGA
GGTCATGTTAGATCAATTGTGGATAACTGGCCAGAAAATCATGTTAAGGCTGTTGTAGTG
ACTGATGGAGAGAGAATTCTGGGTCTTGGAGATCTGGGTGTCTATGGAATGGGAATTCCA
GTAGGAAAACTTTGTTTGTATACAGCTTGTGCAGGAATACGGCCTGATAGATGCCTGCCA
GTGTGTATTGATGTGGGAACTGATAATATCGCACTCTTAAAAGACCCATTTTACATGGGC
TTGTACCAGAAACGAGATCGCACACAACAGTATGATGACCTGATTGATGAGTTTATGAAA
GCTATTACTGACAGATATGGCCGGAACACACTCATTCAGTTCGAAGACTTTGGAAATCAT
AATGCATTCAGGTTCTTGAGAAAGTACCGAGAAAAATATTGTACTTTCAATGATGATATT
CAAGGGACAGCTGCAGTAGCTCTAGCAGGTCTTCTTGCAGCACAAAAAGTTATTAGTAAA
CCAATCTCCGAACACAAAATCTTATTCCTTGGAGCAGGAGAGGCTGCTCTTGGAATTGCA
AATCTTATAGTTATGTCTATGGTAGAAAATGGCCTGTCAGAACAAGAGGCACAAAAGAAA
ATCTGGATGTTTGACAAGTATGGTTTATTAGTTAAGGGACGGAAAGCAAAAATAGATAGT
TATCAGGAACCATTTACTCACTCAGCCCCAGAGAGCATACCTGATACTTTTGAAGATGCA
GTGAATATACTGAAGCCTTCAACTATTATTGGAGTTGCAGGTGCTGGCCGTCTTTTCACT
CCTGATGTAATCAGAGCCATGGCCTCTATCAATGAAAGGCCTGTAATATTTGCATTAAGT
AATCCTACAGCACAGGCAGAGTGCACGGCTGAAGAAGCATATACACTTACAGAGGGCAGG
TGTTTGTTTGCCAGTGGCAGTCCATTTGGGCCAGTGAAACTTACAGATGGGCGAGTCTTT
ACACCAGGTCAAGGAAACAATGTTTATATTTTTCCAGGTGTGGCTTTAGCTGTTATTCTC
TGTAACACCCGGCATATTAGTGACAGTGTTTTCCTAGAAGCTGCAAAGGCCCTGACAAGC
CAATTGACAGATGAAGAGCTAGCCCAAGGGAGACTTTACCCACCGCTTGCTAATATTCAG
GAAGTTTCTATTAACATTGCTATTAAAGTTACAGAATACCTATATGCTAATAAAATGGCT
TTCCGATACCCAGAACCTGAAGACAAGGCCAAATATGTTAAAGAAAGAACATGGCGGAGT
GAATATGATTCCCTGCTGCCAGATGTGTATGAATGGCCAGAATCTGCATCAAGCCCTCCT
GTGATAACAGAATAG
Enzyme 76 GenBank Gene ID M55905 Link Image
Enzyme 76 GeneCard ID ME2 Link Image
Enzyme 76 GenAtlas ID ME2 Link Image
Enzyme 76 HGNC ID HGNC:6984 Link Image
Enzyme 76 Chromosome Location 6
Enzyme 76 Locus 6p25-p24|18q21
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Loeber G, Infante AA, Maurer-Fogy I, Krystek E, Dworkin MB: Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli. J Biol Chem. 1991 Feb 15;266(5):3016-21. [PubMed Link Image]
  2. Yanaihara N, Kohno T, Takakura S, Takei K, Otsuka A, Sunaga N, Takahashi M, Yamazaki M, Tashiro H, Fukuzumi Y, Fujimori Y, Hagiwara K, Tanaka T, Yokota J: Physical and transcriptional map of a 311-kb segment of chromosome 18q21, a candidate lung tumor suppressor locus. Genomics. 2001 Mar 1;72(2):169-79. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  5. Xu Y, Bhargava G, Wu H, Loeber G, Tong L: Crystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases. Structure. 1999;7(8):877-889. [PubMed Link Image]
  6. Yang Z, Floyd DL, Loeber G, Tong L: Structure of a closed form of human malic enzyme and implications for catalytic mechanism. Nat Struct Biol. 2000 Mar;7(3):251-7. [PubMed Link Image]
  7. Yang Z, Lanks CW, Tong L: Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate. Structure. 2002 Jul;10(7):951-60. [PubMed Link Image]
  8. Tao X, Yang Z, Tong L: Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism. Structure. 2003 Sep;11(9):1141-50. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 6178
Enzyme 77 Name Isocitrate dehydrogenase [NADP], mitochondrial
Enzyme 77 Synonyms
  1. IDH
  2. ICD-M
  3. IDP
  4. NADP(+)-specific ICDH
  5. Oxalosuccinate decarboxylase
Enzyme 77 Gene Name IDH2
Enzyme 77 Protein Sequence >Isocitrate dehydrogenase [NADP], mitochondrial 
MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPVVEMDGDEMTR
IIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDE
ARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYK
ATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAI
QKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKS
SGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQK
GRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIH
GLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQ
Enzyme 77 Number of Residues 452
Enzyme 77 Molecular Weight 50908.9
Enzyme 77 Theoretical pI 8.95
Enzyme 77 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • isocitrate dehydrogenase (NADP+) activity
  • isocitrate dehydrogenase activity
  • magnesium ion binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • isocitrate metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
—
Enzyme 77 General Function Involved in magnesium ion binding
Enzyme 77 Specific Function Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex
Enzyme 77 Pathways
Enzyme 77 Reactions
  • (1) isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ (overall reaction) [RN:R00267]
  • (2) (1a) isocitrate + NADP+ = oxalosuccinate + NADPH + H+ [RN:R01899]
  • (3) (1b) oxalosuccinate = 2-oxoglutarate + CO2 [RN:R00268]
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • None
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 872121 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID P48735 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name IDHP_HUMAN Link Image
Enzyme 77 PDB ID 1LWD Link Image
Enzyme 77 PDB File Show
Enzyme 77 3D Structure
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >1359 bp 
ATGGCCGGCTACCTGCGGGTCGTGCGCTCGCTCTGCAGAGCCTCAGGCTCGCGGCCGGCC
TGGGCGCCGGCGGCCCTGACAGCCCCCACCTCGCAAGAGCATCCGCGGCGCCACTATGCC
GACAAAAGGATCAAGGTGGCGAAGCCCGTGGTGGAGATGGATGGTGATGAGATGACCCGT
ATTATCTGGCAGTTCATCAAGGAGAAGCTCATCCTGCCCCACGTGGACATCCAGCTAAAG
TATTTTGACCTCGGGCTCCCAAACCGTGACCAGACTGATGACCAGGTCACCATTGACTCT
GCACTGGCCACCCAGAAGTACAGTGTGGCTGTCAAGTGTGCCACCATCACCCCTGATGAG
GCCCGTGTGGAAGAGTTCAAGCTGAAGAAGATGTGGAAAAGTCCCAATGGAACTATCCGG
AACATCCTGGGGGGGACTGTCTTCCGGGAGCCCATCATCTGCAAAAACATCCCACGCCTA
GTCCCTGGCTGGACCAAGCCCATCACCATTGGCAGGCACGCCCATGGCGACCAGTACAAG
GCCACAGACTTTGTGGCAGACCGGGCCGGCACTTTCAAAATGGTCTTCACCCCAAAAGAT
GGCAGTGGTGTCAAGGAGTGGGAAGTGTACAACTTTCCCGCAGGCGGCGTGGGCATGGGC
ATGTACAACACCGACGAGTCCATCTCAGGTTTTGCGCACAGCTGCTTCCAGTATGCCATC
CAGAAGAAATGGCCGCTGTACATGAGCACCAAGAACACCATACTGAAAGCCTACGATGGG
CGTTTCAAGGACATCTTCCAGGAGATCTTTGACAAGCACTATAAGACCGACTTCGACAAG
AATAAGATCTGGTATGAGCACCGGCTCATTGATGACATGGTGGCTCAGGTCCTCAAGTCT
TCGGGTGGCTTTGTGTGGGCCTGCAAGAACTATGACGGAGATGTGCAGTCAGACATCCTG
GCCCAGGGCTTTGGCTCCCTTGGCCTGATGACGTCCGTCCTGGTCTGCCCTGATGGGAAG
ACGATTGAGGCTGAGGCCGCTCATGGGACCGTCACCCGCCACTATCGGGAGCACCAGAAG
GGCCGGCCCACCAGCACCAACCCCATCGCCAGCATCTTTGCCTGGACACGTGGCCTGGAG
CACCGGGGGAAGCTGGATGGGAACCAAGACCTCATCAGGTTTGCCCAGATGCTGGAGAAG
GTGTGCGTGGAGACGGTGGAGAGTGGAGCCATGACCAAGGACCTGGCGGGCTGCATTCAC
GGCCTCAGCAATGTGAAGCTGAACGAGCACTTCCTGAACACCATGGACTTCCTCGACACC
ATCAAGAGCAACCTGGACAGAGCCCTGGGCAGGCAGTAG
Enzyme 77 GenBank Gene ID X69433 Link Image
Enzyme 77 GeneCard ID IDH2 Link Image
Enzyme 77 GenAtlas ID IDH2 Link Image
Enzyme 77 HGNC ID HGNC:5383 Link Image
Enzyme 77 Chromosome Location 1
Enzyme 77 Locus 15q26.1
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 6180
Enzyme 78 Name Isocitrate dehydrogenase [NADP] cytoplasmic
Enzyme 78 Synonyms
  1. IDH
  2. Cytosolic NADP-isocitrate dehydrogenase
  3. IDP
  4. NADP(+)-specific ICDH
  5. Oxalosuccinate decarboxylase
Enzyme 78 Gene Name IDH1
Enzyme 78 Protein Sequence >Isocitrate dehydrogenase [NADP] cytoplasmic 
MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDA
AEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRL
VSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAM
GMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFE
AQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDG
KTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALE
EVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL
Enzyme 78 Number of Residues 414
Enzyme 78 Molecular Weight 46659.0
Enzyme 78 Theoretical pI 7.00
Enzyme 78 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • isocitrate dehydrogenase (NADP+) activity
  • isocitrate dehydrogenase activity
  • magnesium ion binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • isocitrate metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
—
Enzyme 78 General Function Involved in magnesium ion binding
Enzyme 78 Specific Function Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH
Enzyme 78 Pathways
Enzyme 78 Reactions
  • (1) isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ (overall reaction) [RN:R00267]
  • (2) (1a) isocitrate + NADP+ = oxalosuccinate + NADPH + H+ [RN:R01899]
  • (3) (1b) oxalosuccinate = 2-oxoglutarate + CO2 [RN:R00268]
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • None
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 3641398 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID O75874 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name IDHC_HUMAN Link Image
Enzyme 78 PDB ID 1T0L Link Image
Enzyme 78 PDB File Show
Enzyme 78 3D Structure
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >1245 bp 
ATGTCCAAAAAAATCAGTGGCGGTTCTGTGGTAGAGATGCAAGGAGATGAAATGACACGA
ATCATTTGGGAATTGATTAAAGAGAAACTCATTTTTCCCTACGTGGAATTGGATCTACAT
AGCTATGATTTAGGCATAGAGAATCGTGATGCCACCAACGACCAAGTCACCAAGGATGCT
GCAGAAGCTATAAAGAAGCATAATGTTGGCGTCAAATGTGCCACTATCACTCCTGATGAG
AAGAGGGTTGAGGAGTTCAAGTTGAAACAAATGTGGAAATCACCAAATGGCACCATACGA
AATATTCTGGGTGGCACGGTCTTCAGAGAAGCCATTATCTGCAAAAATATCCCCCGGCTT
GTGAGTGGATGGGTAAAACCTATCATCATAGGTCGTCATGCTTATGGGGATCAATACAGA
GCAACTGATTTTGTTGTTCCTGGGCCTGGAAAAGTAGAGATAACCTACACACCAAGTGAC
GGAACCCAAAAGGTGACATACCTGGTACATAACTTTGAAGAAGGTGGTGGTGTTGCCATG
GGGATGTATAATCAAGATAAGTCAATTGAAGATTTTGCACACAGTTCCTTCCAGATGGCT
CTGTCTAAGGGTTGGCCTTTGTATCTGAGCACCAAAAACACTATTCTGAAGATATATGAT
GGGCGTTTTAAAGACATCTTTCAGGAGATATATGACAAGCAGTACAAGTCCCAGTTTGAA
GCTCAAAAGATCTGGTATGAGCATAGGCTCATCGACGACATGGTGGCCCAAGCTATGAAA
TCAGAGGGAGGCTTCATCTGGGCCTGTAAAAACTATGATGGTGACGTGCAGTCGGACTCT
GTGGCCCAAGGGTATGGCTCTCTCGGCATGATGACCAGCGTGCTGGTTTGTCCAGATGGC
AAGACAGTAGAAGCAGAGGCTGCCCACGGGACTGTAACCCGTCACTACCGCATGTACCAG
AAAGGACAGGAGACGTCCACCAACCTCATTGCTTCCATTTTTGCCTGGACCAGAGGGTTA
GCCCACAGAGCAAAGCTTGATAACAATAAAGAGCTTGCCTTCTTTGCAAATGCTTTGGAA
GAAGTCTCTATTGAGACAATTGAGGCTGGCTTCATGACCAAGGACTTGGCTGCTTGCATT
AGAGGTTTACCCAATGTGCAACGTTCTGACTACTTGAATACATTTGAGTTCATGGATAAA
CTTGGAGAAAACTTGAAGATCAAACTAGCTCAGGCCAAACTTTAA
Enzyme 78 GenBank Gene ID AF020038 Link Image
Enzyme 78 GeneCard ID IDH1 Link Image
Enzyme 78 GenAtlas ID IDH1 Link Image
Enzyme 78 HGNC ID HGNC:5382 Link Image
Enzyme 78 Chromosome Location 2
Enzyme 78 Locus 2q33.3
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Nekrutenko A, Hillis DM, Patton JC, Bradley RD, Baker RJ: Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family. Mol Biol Evol. 1998 Dec;15(12):1674-84. [PubMed Link Image]
  2. Geisbrecht BV, Gould SJ: The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase. J Biol Chem. 1999 Oct 22;274(43):30527-33. [PubMed Link Image]
  3. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  7. Xu X, Zhao J, Xu Z, Peng B, Huang Q, Arnold E, Ding J: Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J Biol Chem. 2004 Aug 6;279(32):33946-57. Epub 2004 Jun 1. [PubMed Link Image]
  8. Dang L, White DW, Gross S, Bennett BD, Bittinger MA, Driggers EM, Fantin VR, Jang HG, Jin S, Keenan MC, Marks KM, Prins RM, Ward PS, Yen KE, Liau LM, Rabinowitz JD, Cantley LC, Thompson CB, Vander Heiden MG, Su SM: Cancer-associated IDH1 mutations produce 2-hydroxyglutarate. Nature. 2009 Dec 10;462(7274):739-44. Epub . [PubMed Link Image]
  9. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  10. Parsons DW, Jones S, Zhang X, Lin JC, Leary RJ, Angenendt P, Mankoo P, Carter H, Siu IM, Gallia GL, Olivi A, McLendon R, Rasheed BA, Keir S, Nikolskaya T, Nikolsky Y, Busam DA, Tekleab H, Diaz LA Jr, Hartigan J, Smith DR, Strausberg RL, Marie SK, Shinjo SM, Yan H, Riggins GJ, Bigner DD, Karchin R, Papadopoulos N, Parmigiani G, Vogelstein B, Velculescu VE, Kinzler KW: An integrated genomic analysis of human glioblastoma multiforme. Science. 2008 Sep 26;321(5897):1807-12. Epub 2008 Sep 4. [PubMed Link Image]
  11. Bleeker FE, Lamba S, Leenstra S, Troost D, Hulsebos T, Vandertop WP, Frattini M, Molinari F, Knowles M, Cerrato A, Rodolfo M, Scarpa A, Felicioni L, Buttitta F, Malatesta S, Marchetti A, Bardelli A: IDH1 mutations at residue p.R132 (IDH1(R132)) occur frequently in high-grade gliomas but not in other solid tumors. Hum Mutat. 2009 Jan;30(1):7-11. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 6198
Enzyme 79 Name 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Enzyme 79 Synonyms
  1. HMG-CoA reductase
Enzyme 79 Gene Name HMGCR
Enzyme 79 Protein Sequence >3-hydroxy-3-methylglutaryl-coenzyme A reductase 
MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSS
DIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTG
LNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIG
VGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFAR
VLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKR
IEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVT
QKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNS
SLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK
LETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGV
AGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC
DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMI
SKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV
LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITL
MEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR
IVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA
Enzyme 79 Number of Residues 888
Enzyme 79 Molecular Weight 97475.2
Enzyme 79 Theoretical pI 6.72
Enzyme 79 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • hydroxymethylglutaryl-CoA reductase (NADPH) activity
  • hydroxymethylglutaryl-CoA reductase (NADPH) activity
  • hydroxymethylglutaryl-CoA reductase (NADPH) activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular lipid metabolic process
  • cellular metabolic process
  • coenzyme A metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • isoprenoid biosynthetic process
  • isoprenoid metabolic process
  • lipid metabolic process
  • metabolic process
  • oxidation reduction
  • primary metabolic process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 79 General Function Involved in hydroxymethylglutaryl-CoA reductase (NADPH) activity
Enzyme 79 Specific Function This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of sterol biosynthesis
Enzyme 79 Pathways
Enzyme 79 Reactions
  • (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ [RN:R02082]
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • 10-39 57-78 90-114 124-149 160-187 192-220 315-339
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein 306865 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID P04035 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name HMDH_HUMAN Link Image
Enzyme 79 PDB ID 1HWL Link Image
Enzyme 79 PDB File Show
Enzyme 79 3D Structure
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >2667 bp 
ATGTTGTCAAGACTTTTTCGAATGCATGGCCTCTTTGTGGCCTCCCATCCCTGGGAAGTC
ATAGTGGGGACAGTGACACTGACCATCTGCATGATGTCCATGAACATGTTTACTGGTAAC
AATAAGATCTGTGGTTGGAATTATGAATGTCCAAAGTTTGAAGAGGATGTTTTGAGCAGT
GACATTATAATTCTGACAATAACACGATGCATAGCCATCCTGTATATTTACTTCCAGTTC
CAGAATTTACGTCAACTTGGATCAAAATATATTTTGGGTATTGCTGGCCTTTTCACAATT
TTCTCAAGTTTTGTATTCAGTACAGTTGTCATTCACTTCTTAGACAAAGAATTGACAGGC
TTGAATGAAGCTTTGCCCTTTTTCCTACTTTTGATTGACCTTTCCAGAGCAAGCACATTA
GCAAAGTTTGCCCTCAGTTCCAACTCACAGGATGAAGTAAGGGAAAATATTGCTCGTGGA
ATGGCAATTTTAGGTCCTACGTTTACCCTCGATGCTCTTGTTGAATGTCTTGTGATTGGA
GTTGGTACCATGTCAGGGGTACGTCAGCTTGAAATTATGTGCTGCTTTGGCTGCATGTCA
GTTCTTGCCAACTACTTCGTGTTCATGACTTTCTTCCCAGCTTGTGTGTCCTTGGTATTA
GAGCTTTCTCGGGAAAGCCGCGAGGGTCGTCCAATTTGGCAGCTCAGCCATTTTGCCCGA
GTTTTAGAAGAAGAAGAAAATAAGCCGAATCCTGTAACTCAGAGGGTCAAGATGATTATG
TCTCTAGGCTTGGTTCTTGTTCATGCTCACAGTCGCTGGATAGCTGATCCTTCTCCTCAA
AACAGTACAGCAGATACTTCTAAGGTTTCATTAGGACTGGATGAAAATGTGTCCAAGAGA
ATTGAACCAAGTGTTTCCCTCTGGCAGTTTTATCTCTCTAAAATGATCAGCATGGATATT
GAACAAGTTATTACCCTAAGTTTAGCTCTCCTTCTGGCTGTCAAGTACATCTTCTTTGAA
CAAACAGAGACAGAATCTACACTCTCATTAAAAAACCCTATCACATCTCCTGTAGTGACA
CAAAAGAAAGTCCCAGACAATTGTTGTAGACGTGAACCTATGCTGGTCAGAAATAACCAG
AAATGTGATTCAGTAGAGGAAGAGACAGGGATAAACCGAGAAAGAAAAGTTGAGGTTATA
AAACCCTTAGTGGCTGAAACAGATACCCCAAACAGAGCTACATTTGTGGTTGGTAACTCC
TCCTTACTCGATACTTCATCAGTACTGGTGACACAGGAACCTGAAATTGAACTTCCCAGG
GAACCTCGGCCTAATGAAGAATGTCTACAGATACTTGGGAATGCAGAGAAAGGTGCAAAA
TTCCTTAGTGATGCTGAGATCATCCAGTTAGTCAATGCTAAGCATATCCCAGCCTACAAG
TTGGAAACTCTGATGGAAACTCATGAGCGTGGTGTATCTATTCGCCGACAGTTACTTTCC
AAGAAGCTTTCAGAACCTTCTTCTCTCCAGTACCTACCTTACAGGGATTATAATTACTCC
TTGGTGATGGGAGCTTGTTGTGAGAATGTTATTGGATATATGCCCATCCCTGTTGGAGTG
GCAGGACCCCTTTGCTTAGATGAAAAAGAATTTCAGGTTCCAATGGCAACAACAGAAGGT
TGTCTTGTGGCCAGCACCAATAGAGGCTGCAGAGCAATAGGTCTTGGTGGAGGTGCCAGC
AGCCGAGTCCTTGCAGATGGGATGACTCGTGGCCCAGTTGTGCGTCTTCCACGTGCTTGT
GACTCTGCAGAAGTGAAAGCCTGGCTCGAAACATCTGAAGGGTTCGCAGTGATAAAGGAG
GCATTTGACAGCACTAGCAGATTTGCACGTCTACAGAAACTTCATACAAGTATAGCTGGA
CGCAACCTTTATATCCGTTTCCAGTCCAGGTCAGGGGATGCCATGGGGATGAACATGATT
TCAAAGGGTACAGAGAAAGCACTTTCAAAACTTCACGAGTATTTCCCTGAAATGCAGATT
CTAGCCGTTAGTGGTAACTATTGTACTGACAAGAAACCTGCTGCTATAAATTGGATAGAG
GGAAGAGGAAAATCTGTTGTTTGTGAAGCTGTCATTCCAGCCAAGGTTGTCAGAGAAGTA
TTAAAGACTACCACAGAGGCTATGATTGAGGTCAACATTAACAAGAATTTAGTGGGCTCT
GCCATGGCTGGGAGCATAGGAGGCTACAACGCCCATGCAGCAAACATTGTCACCGCCATC
TACATTGCCTGTGGACAGGATGCAGCACAGAATGTTGGTAGTTCAAACTGTATTACTTTA
ATGGAAGCAAGTGGTCCCACAAATGAAGATTTATATATCAGCTGCACCATGCCATCTATA
GAGATAGGAACGGTGGGTGGTGGGACCAACCTACTACCTCAGCAAGCCTGTTTGCAGATG
CTAGGTGTTCAAGGAGCATGCAAAGATAATCCTGGGGAAAATGCCCGGCAGCTTGCCCGA
ATTGTGTGTGGGACCGTAATGGCTGGGGAATTGTCACTTATGGCAGCATTGGCAGCAGGA
CATCTTGTCAAAAGTCACATGATTCACAACAGGTCGAAGATCAATTTACAAGACCTCCAA
GGAGCTTGCACCAAGAAGACAGCCTGA
Enzyme 79 GenBank Gene ID M11058 Link Image
Enzyme 79 GeneCard ID HMGCR Link Image
Enzyme 79 GenAtlas ID HMGCR Link Image
Enzyme 79 HGNC ID HGNC:5006 Link Image
Enzyme 79 Chromosome Location 5
Enzyme 79 Locus 5q13.3-q14
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Luskey KL, Stevens B: Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. J Biol Chem. 1985 Aug 25;260(18):10271-7. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J: Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 2000 Mar 1;19(5):819-30. [PubMed Link Image]
  4. Istvan ES, Deisenhofer J: Structural mechanism for statin inhibition of HMG-CoA reductase. Science. 2001 May 11;292(5519):1160-4. [PubMed Link Image]
  5. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 6199
Enzyme 80 Name NAD(P) transhydrogenase, mitochondrial
Enzyme 80 Synonyms
  1. Nicotinamide nucleotide transhydrogenase
  2. Pyridine nucleotide transhydrogenase
Enzyme 80 Gene Name NNT
Enzyme 80 Protein Sequence >NAD(P) transhydrogenase, mitochondrial 
MANLLKTVVTGCSCPLLSNLGSCKGLRVKKDFLRTFYTHQELWCKAPVKPGIPYKQLTVG
VPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVL
ASDLVVKVRAPMVNPTLGVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQV
PRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFTGQITAAGKVPPAKILIVGGGVAGL
ASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIEAE
MKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPG
ELYIHKGITHIGYTDLPSRMATQASTLYSNNITKLLKAISPDKDNFYFDVKDDFDFGTMG
HVIRGTVVMKDGKVIFPAPTPKNIPQGAPVKQKTVAELEAEKAATITPFRKTMSTASAYT
AGLTGILGLGIAAPNLAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAISGLTAV
GGLALMGGHLYPSTTSQGLAALAAFISSVNIAGGFLVTQRMLDMFKRPTDPPEYNYLYLL
PAGTFVGGYLAALYSGYNIEQIMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLA
ATLGVLKPGPELLAQMSGAMALGGTIGLTIAKRIQISDLPQLVAAFHSLVGLAAVLTCIA
EYIIEYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGRHLL
NAGLLAASVGGIIPFMVDPSFTTGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNS
YSGWALCAEGFLLNNNLLTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGG
KPMEISGTHTEINLDNAIDMIREANSIIITPGYGLCAAKAQYPIADLVKMLTEQGKKVRF
GIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQEDP
NSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAKV
RESYQK
Enzyme 80 Number of Residues 1086
Enzyme 80 Molecular Weight 113894.6
Enzyme 80 Theoretical pI 8.21
Enzyme 80 GO Classification
Function
  • NAD(P)+ transhydrogenase (AB-specific) activity
  • NAD(P)+ transhydrogenase activity
  • NAD(P)+ transhydrogenase activity
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, NAD or NADP as acceptor
Process
  • establishment of localization
  • hydrogen transport
  • metabolic process
  • oxidation reduction
  • proton transport
  • transport
Component
—
Enzyme 80 General Function Involved in oxidoreductase activity
Enzyme 80 Specific Function The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane
Enzyme 80 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 80 Reactions
  • NADPH + NAD+ = NADP+ + NADH [RN:R00112]
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • 475-493 501-521 527-546 558-578 596-616 622-642 646-666 672-691 702-722 740-760 778-797 801-819 833-853 857-879
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein 21732286 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID Q13423 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name NNTM_HUMAN Link Image
Enzyme 80 PDB ID 1PT9 Link Image
Enzyme 80 PDB File Show
Enzyme 80 3D Structure
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >3261 bp 
ATGGCAAACCTATTGAAAACAGTGGTGACTGGCTGCTCGTGTCCTCTACTTAGCAATTTG
GGGTCCTGTAAGGGTCTACGTGTGAAGAAGGATTTTTTACGAACATTTTATACTCACCAA
GAACTGTGGTGTAAAGCGCCTGTAAAACCAGGAATTCCATATAAGCAACTGACTGTTGGA
GTCCCCAAAGAGATATTCCAAAATGAGAAGCGAGTGGCATTGTCTCCTGCTGGTGTTCAG
AACTTGGTCAAGCAGGGTTTTAATGTTGTCGTGGAATCGGGTGCGGGCGAAGCTTCCAAG
TTCTCAGATGATCACTATAGAGTGGCAGGTGCCCAAATCCAAGGGGCAAAGGAAGTGCTG
GCTTCTGATTTGGTGGTCAAAGTGCGAGCCCCTATGGTTAATCCAACATTAGGTGTTCAT
GAAGCTGACCTTTTAAAGACATCAGGAACGCTGATTAGTTTTATTTACCCAGCCCAAAAT
CCAGAGTTGCTAAATAAACTTTCCCAAAGAAAAACTACAGTTCTGGCAATGGACCAGGTT
CCAAGAGTCACAATTGCTCAGGGATATGATGCGCTAAGCTCCATGGCCAACATTGCGGGT
TATAAGGCTGTTGTCCTAGCAGCAAATCATTTTGAACGTTTTTTTACTGGTCAGATCACA
GCTGCTGGAAAAGTTCCTCCAGCTAAGATTCTGATAGTTGGTGGTGGTGTTGCTGGGCTT
GCTTCTGCAGGCGCAGCAAAGTCGATGGGTGCAATTGTTCGAGGATTTGACACAAGAGCT
GCAGCTTTGGAACAGTTCAAGTCTCTTGGTGCTGAGCCCTTGGAGGTGGACTTGAAGGAA
TCTGGTGAGGGACAAGGAGGATATGCAAAAGAGATGTCCAAAGAGTTCATTGAAGCTGAA
ATGAAACTCTTTGCTCAACAATGCAAGGAGGTAGACATCCTTATCAGCACAGCACTTATT
CCAGGTAAAAAAGCTCCAGTTTTATTTAATAAAGAAATGATTGAGTCAATGAAGGAAGGT
TCAGTTGTTGTGGATTTAGCTGCTGAGGCTGGTGGAAACTTTGAAACCACTAAGCCAGGA
GAACTCTACATTCATAAGGGAATTACTCACATAGGCTACACAGACCTGCCCAGCCGAATG
GCCACTCAGGCCAGCACCCTATATTCCAACAACATCACCAAACTCCTGAAGGCCATCAGC
CCGGACAAAGATAATTTTTATTTTGATGTGAAAGATGACTTTGACTTTGGTACGATGGGT
CATGTCATTAGAGGAACTGTAGTGATGAAAGATGGTAAAGTGATTTTCCCAGCTCCCACA
CCGAAAAATATTCCTCAAGGTGCCCCAGTAAAACAGAAGACAGTGGCTGAGCTGGAAGCT
GAAAAAGCAGCTACCATTACACCCTTCAGGAAGACAATGTCAACGGCTTCTGCATATACA
GCAGGTCTCACAGGGATACTGGGTTTGGGCATTGCGGCTCCCAATCTAGCCTTTTCTCAG
ATGGTGACCACTTTTGGCTTGGCTGGCATTGTGGGGTATCATACCGTCTGGGGAGTGACC
CCTGCTCTCCACTCACCACTGATGTCTGTGACAAATGCAATCTCAGGGCTGACTGCAGTT
GGTGGGTTGGCACTGATGGGAGGACATTTGTATCCTTCCACAACTTCTCAGGGCCTTGCT
GCTCTTGCTGCATTCATATCCTCTGTCAACATTGCAGGTGGCTTTCTGGTGACTCAGAGA
ATGCTGGACATGTTCAAGCGTCCCACTGACCCCCCAGAATACAACTACCTGTACCTGCTC
CCTGCCGGCACCTTTGTTGGTGGATATTTAGCTGCCCTCTACAGTGGTTATAACATTGAA
CAGATCATGTACCTAGGCTCGGGTTTGTGCTGTGTCGGTGCCTTGGCTGGCCTCTCCACC
CAGGGAACAGCACGTCTTGGCAATGCACTGGGCATGATTGGGGTTGCTGGAGGACTGGCA
GCCACCCTCGGAGTCCTAAAACCGGGCCCAGAATTACTAGCTCAGATGTCTGGAGCGATG
GCTTTGGGTGGTACCATTGGATTGACAATTGCCAAACGCATCCAGATTTCTGATTTACCT
CAATTAGTTGCTGCTTTTCACAGTTTAGTGGGTTTGGCAGCTGTACTTACTTGCATAGCT
GAGTACATTATAGAATATCCACATTTTGCTACGGACGCAGCAGCAAATCTCACCAAGATT
GTGGCCTACCTCGGCACTTACATTGGTGGCGTCACCTTTAGTGGGTCTCTCATTGCCTAT
GGAAAATTGCAGGGTCTCCTGAAATCTGCCCCTCTCCTACTGCCTGGAAGGCACTTACTC
AATGCAGGCTTACTGGCTGCTAGTGTGGGCGGGATAATCCCATTCATGGTGGACCCAAGC
TTTACTACTGGCATCACCTGTCTGGGTTCAGTGTCTGCTCTCTCTGCTGTCATGGGTGTG
ACTTTGACAGCTGCTATTGGGGGTGCTGACATGCCCGTCGTTATCACTGTGCTGAACAGC
TACTCAGGCTGGGCCCTGTGTGCAGAGGGCTTCCTGCTCAACAACAATCTGCTGACCATC
GTGGGTGCACTCATAGGCTCGTCTGGTGCTATCCTGTCATACATCATGTGTGTGGCAATG
AATCGCTCCCTGGCTAATGTGATTCTTGGAGGCTATGGCACCACTTCAACAGCTGGTGGA
AAACCCATGGAAATTTCTGGCACACATACGGAAATCAACCTTGACAATGCAATTGACATG
ATTCGAGAAGCTAATAGCATTATTATTACACCAGGCTATGGTCTCTGTGCAGCCAAAGCT
CAATACCCCATTGCTGATTTGGTAAAGATGCTCACTGAGCAAGGCAAAAAAGTCAGGTTT
GGAATTCACCCAGTTGCAGGCCGAATGCCTGGTCAGCTTAATGTGCTGCTGGCTGAGGCT
GGTGTGCCATATGACATTGTGTTGGAAATGGATGAGATCAACCATGATTTTCCAGATACT
GATTTGGTCCTTGTAATTGGAGCTAATGACACTGTTAATTCAGCAGCTCAAGAAGATCCC
AACTCTATTATTGCAGGCATGCCAGTCCTTGAGGTCTGGAAATCAAAGCAGGTGATTGTT
ATGAAGAGGTCTTTGGGTGTTGGCTATGCTGCAGTGGACAATCCAATCTTCTACAGACCT
AACACGGCCATGCTTCTAGGTGATGCCAAGAAAACATGTGACGCGCTCCAGGCGAAAGTT
AGAGAATCCTATCAGAAGTAA
Enzyme 80 GenBank Gene ID AL831822 Link Image
Enzyme 80 GeneCard ID NNT Link Image
Enzyme 80 GenAtlas ID NNT Link Image
Enzyme 80 HGNC ID HGNC:7863 Link Image
Enzyme 80 Chromosome Location 5
Enzyme 80 Locus 5p12
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Zieger B, Ware J: Cloning and deduced amino acid sequence of human nicotinamide nucleotide transhydrogenase. DNA Seq. 1997;7(6):369-73. [PubMed Link Image]
  2. Arkblad EL, Betsholtz C, Rydstrom J: The cDNA sequence of proton-pumping nicotinamide nucleotide transhydrogenase from man and mouse. Biochim Biophys Acta. 1996 Mar 28;1273(3):203-5. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. White SA, Peake SJ, McSweeney S, Leonard G, Cotton NP, Jackson JB: The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria. Structure. 2000 Jan 15;8(1):1-12. [PubMed Link Image]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 6211
Enzyme 81 Name C-1-tetrahydrofolate synthase, cytoplasmic
Enzyme 81 Synonyms
  1. C1-THF synthase
  2. Methylenetetrahydrofolate dehydrogenase
  3. Methenyltetrahydrofolate cyclohydrolase
  4. Formyltetrahydrofolate synthetase
Enzyme 81 Gene Name MTHFD1
Enzyme 81 Protein Sequence >C-1-tetrahydrofolate synthase, cytoplasmic 
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAA
EEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAP
EKDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAP
MHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY
VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKP
GKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSAL
ERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGI
KGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLV
PSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRF
LRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPV
SAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVG
PEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLP
KAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAF
DAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIE
LLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFL
YPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Enzyme 81 Number of Residues 935
Enzyme 81 Molecular Weight 101558.4
Enzyme 81 Theoretical pI 7.32
Enzyme 81 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • formate-tetrahydrofolate ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 81 General Function Involved in formate-tetrahydrofolate ligase activity
Enzyme 81 Specific Function 5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Enzyme 81 Pathways
  • Glyoxylate and Dicarboxylate Metabolism (map00630 Link Image)
  • One Carbon Pool By Folate (map00670 Link Image)
Enzyme 81 Reactions
  • ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate [RN:R00943]
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 189065440 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID P11586 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name C1TC_HUMAN Link Image
Enzyme 81 PDB ID 1DIA Link Image
Enzyme 81 PDB File Show
Enzyme 81 3D Structure
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >2808 bp 
ATGGCGCCAGCAGAAATCCTGAACGGGAAGGAGATCTCCGCGCAAATAAGGGCGAGACTG
AAAAATCAAGTCACTCAGTTGAAGGAGCAAGTACCTGGTTTCACACCACGCCTGGCAATA
TTACAGGTTGGCAACAGAGATGATTCCAATCTTTATATAAATGTGAAGCTGAAGGCTGCT
GAAGAGATTGGGATCAAAGCCACTCACATTAAGTTACCAAGAACAACCACAGAATCTGAG
GTGATGAAGTACATTACATCTTTGAATGAAGACTCTACTGTACATGGGTTCTTAGTGCAG
CTACCTTTAGATTCAGAGAATTCCATTAACACTGAAGAAGTGATCAATGCTATTGCACCC
GAGAAGGATGTGGATGGATTGACTAGCATCAATGCTGGGAGACTTGCTAGAGGTGACCTC
AATGACTGTTTCATTCCTTGTACGCCTAAGGGATGCTTGGAACTCATCAAAGAGACAGGG
GTGCCGATTGCCGGAAGGCATGCTGTGGTGGTTGGGCGCAGTAAAATAGTTGGGGCCCCG
ATGCATGACTTGCTTCTGTGGAACAATGCCACAGTGACCACCTGCCACTCCAAGACTGCC
CATCTGGATGAGGAGGTAAATAAAGGTGACATCCTGGTGGTTGCAACTGGTCAGCCTGAA
ATGGTTAAAGGGGAGTGGATCAAACCTGGGGCAATAGTCATCGACTGTGGAATCAATTAT
GTCCCAGATGATAAAAAACCAAATGGGAGAAAAGTTGTGGGTGATGTGGCATACGACGAG
GCCAAAGAGAGGGCGAGCTTCATCACTCCTGTTCCTGGCGGCGTAGGGCCCATGACAGTT
GCAATGCTCATGCAGAGCACAGTAGAGAGTGCCAAGCGTTTCCTGGAGAAATTTAAGCCA
GGAAAGTGGATGATTCAGTATAACAACCTTAACCTCAAGACACCTGTTCCAAGTGACATT
GATATATCACGATCTTGTAAACCGAAGCCCATTGGTAAGCTGGCTCGAGAAATTGGTCTG
CTGTCTGAAGAGGTAGAATTATATGGTGAAACAAAGGCCAAAGTTCTGCTGTCAGCACTA
GAACGCCTGAAGCACCGGCCTGATGGGAAATACGTGGTGGTGACTGGAATAACTCCAACA
CCCCTGGGAGAAGGGAAAAGCACAACTACAATCGGGCTAGTGCAAGCCCTTGGTGCCCAT
CTCTACCAGAATGTCTTTGCGTGTGTGCGACAGCCTTCTCAGGGCCCCACCTTTGGAATA
AAAGGTGGCGCTGCAGGAGGCGGCTACTCCCAGGTCATTCCTATGGAAGAGTTTAATCTC
CACCTCACAGGTGACATCCATGCCATCACTGCAGCTAATAACCTCGTTGCTGCGGCCATT
GATGCTCGGATATTTCATGAACTGACCCAGACAGACAAGGCTCTCTTTAATCGTTTGGTG
CCATCAGTAAATGGAGTGAGAAGGTTCTCTGACATCCAAATCCGAAGGTTAAAGAGACTA
GGCATTGAAAAGACTGACCCTACCACACTGACAGATGAAGAGATAAACAGATTTGCAAGA
TTGGACATTGATCCAGAAACCATAACTTGGCAAAGAGTGTTGGATACCAATGATAGATTC
CTGAGGAAGATCACGATTGGACAGGCTCCAACGGAGAAGGGTCACACACGGACGGCCCAG
TTTGATATCTCTGTGGCCAGTGAAATTATGGCTGTCCTGGCTCTCACCACTTCTCTAGAA
GACATGAGAGAGAGACTGGGCAAAATGGTGGTGGCATCCAGTAAGAAAGGAGAGCCCGTC
AGTGCCGAAGATCTGGGGGTGAGTGGTGCACTGACAGTGCTTATGAAGGACGCAATCAAG
CCCAATCTCATGCAGACACTGGAGGGCACTCCAGTGTTTGTCCATGCTGGCCCGTTTGCC
AACATCGCACATGGCAATTCCTCCATCATTGCAGACCAGATCGCACTCAAGCTTGTTGGC
CCAGAAGGGTTTGTAGTGACGGAAGCAGGATTTGGAGCAGACATTGGAATGGAAAAGTTT
TTTAACATCAAATGCCGGTATTCCGGCCTCTGCCCCCACGTGGTGGTGCTTGTTGCCACT
GTCAGGGCTCTCAAGATGCACGGGGGCGGCCCCACGGTCACTGCTGGACTGCCTCTTCCC
AAGGCTTACATACAGGAGAACCTGGAGCTGGTTGAAAAAGGCTTCAGTAACTTGAAGAAA
CAAATTGAAAATGCCAGAATGTTTGGAATTCCAGTAGTAGTGGCCGTGAATGCATTCAAG
ACGGATACAGAGTCTGAGCTGGACCTCATCAGCCGCCTTTCCAGAGAACATGGGGCTTTT
GATGCCGTGAAGTGCACTCACTGGGCAGAAGGGGGCAAGGGTGCCTTAGCCCTGGCTCAG
GCCGTCCAGAGAGCAGCACAAGCACCCAGCAGCTTCCAGCTCCTTTATGACCTCAAGCTC
CCAGTTGAGGATAAAATCAGGATCATTGCACAGAAGATCTATGGAGCAGATGACATTGAA
TTACTTCCCGAAGCTCAACACAAAGCTGAAGTCTACACGAAGCAGGGCTTTGGGAATCTC
CCCATCTGCATGGCTAAAACACACTTGTCTTTGTCTCACAACCCAGAGCAAAAAGGTGTC
CCTACAGGCTTCATTCTGCCCATTCGCGACATCCGCGCCAGCGTTGGGGCTGGTTTTCTG
TACCCCTTAGTAGGAACGATGAGCACAATGCCTGGACTCCCCACCCGGCCCTGTTTTTAT
GATATTGATTTGGACCCTGAAACAGAACAGGTGAATGGATTATTCTAA
Enzyme 81 GenBank Gene ID AK312361 Link Image
Enzyme 81 GeneCard ID MTHFD1 Link Image
Enzyme 81 GenAtlas ID MTHFD1 Link Image
Enzyme 81 HGNC ID HGNC:7432 Link Image
Enzyme 81 Chromosome Location 1
Enzyme 81 Locus 14q24
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Hum DW, Bell AW, Rozen R, MacKenzie RE: Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. J Biol Chem. 1988 Nov 5;263(31):15946-50. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Allaire M, Li Y, MacKenzie RE, Cygler M: The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. Structure. 1998 Feb 15;6(2):173-82. [PubMed Link Image]
  7. Schmidt A, Wu H, MacKenzie RE, Chen VJ, Bewly JR, Ray JE, Toth JE, Cygler M: Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. Biochemistry. 2000 May 30;39(21):6325-35. [PubMed Link Image]
  8. Hol FA, van der Put NM, Geurds MP, Heil SG, Trijbels FJ, Hamel BC, Mariman EC, Blom HJ: Molecular genetic analysis of the gene encoding the trifunctional enzyme MTHFD (methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, formyltetrahydrofolate synthetase) in patients with neural tube defects. Clin Genet. 1998 Feb;53(2):119-25. [PubMed Link Image]
  9. Brody LC, Conley M, Cox C, Kirke PN, McKeever MP, Mills JL, Molloy AM, O'Leary VB, Parle-McDermott A, Scott JM, Swanson DA: A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group. Am J Hum Genet. 2002 Nov;71(5):1207-15. Epub 2002 Oct 16. [PubMed Link Image]
  10. Parle-McDermott A, Kirke PN, Mills JL, Molloy AM, Cox C, O'Leary VB, Pangilinan F, Conley M, Cleary L, Brody LC, Scott JM: Confirmation of the R653Q polymorphism of the trifunctional C1-synthase enzyme as a maternal risk for neural tube defects in the Irish population. Eur J Hum Genet. 2006 Jun;14(6):768-72. [PubMed Link Image]
  11. Webb EL, Rudd MF, Sellick GS, El Galta R, Bethke L, Wood W, Fletcher O, Penegar S, Withey L, Qureshi M, Johnson N, Tomlinson I, Gray R, Peto J, Houlston RS: Search for low penetrance alleles for colorectal cancer through a scan of 1467 non-synonymous SNPs in 2575 cases and 2707 controls with validation by kin-cohort analysis of 14 704 first-degree relatives. Hum Mol Genet. 2006 Nov 1;15(21):3263-71. Epub 2006 Sep 25. [PubMed Link Image]
  12. Christensen KE, Rohlicek CV, Andelfinger GU, Michaud J, Bigras JL, Richter A, Mackenzie RE, Rozen R: The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects. Hum Mutat. 2009 Feb;30(2):212-20. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 6213
Enzyme 82 Name GDP-L-fucose synthase
Enzyme 82 Synonyms
  1. GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
  2. Protein FX
  3. Red cell NADP(H)-binding protein
  4. Short-chain dehydrogenase/reductase family 4E member 1
Enzyme 82 Gene Name TSTA3
Enzyme 82 Protein Sequence >GDP-L-fucose synthase 
MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEK
VQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPD
KTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNF
NIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPI
ILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTP
FKQAVKETCAWFTDNYEQARK
Enzyme 82 Number of Residues 321
Enzyme 82 Molecular Weight 35892.5
Enzyme 82 Theoretical pI 6.59
Enzyme 82 GO Classification
Function
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolic process
  • metabolic process
Component
—
Enzyme 82 General Function Involved in catalytic activity
Enzyme 82 Specific Function Two step NADP-dependent conversion of GDP-4-dehydro-6- deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction
Enzyme 82 Pathways
Enzyme 82 Reactions
  • GDP-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+ [RN:R05692]
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • None
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein Not Available
Enzyme 82 UniProtKB/Swiss-Prot ID Q13630 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name FCL_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >966 bp 
ATGGGTGAACCCCAGGGATCCATGCGGATTCTAGTGACAGGGGGCTCTGGGCTGGTAGGC
AAAGCCATCCAGAAGGTGGTAGCAGATGGAGCTGGACTTCCTGGAGAGGACTGGGTGTTT
GTCTCCTCTAAAGACGCCGATCTCACGGATACAGCACAGACCCGCGCCCTGTTTGAGAAG
GTCCAACCCACACACGTCATCCATCTTGCTGCAATGGTGGGGGGCCTGTTCCGGAATATC
AAATACAATTTGGACTTCTGGAGGAAAAACGTGCACATGAACGACAACGTCCTGCACTCG
GCCTTTGAGGTGGGGGCCCGCAAGGTGGTGTCCTGCCTGTCCACCTGTATCTTCCCTGAC
AAGACGACCTACCCGATAGATGAGACCATGATCCACAATGGGCCTCCCCACAACAGCAAT
TTTGGGTACTCGTATGCCAAGAGGATGATCGACGTGCAGAACAGGGCCTACTTCCAGCAG
TACGGCTGCACCTTCACCGCTGTCATCCCCACCAACGTTTTCGGGCCCCACGACAACTTC
AACATCGAGGATGGCCACGTGCTGCCTGGCCTCATCCACAAGGTGCACCTGGCCAAGAGC
AGCGGCTCGGCCCTGACGGTGTGGGGTACAGGGAATCCGCGGAGGCAGTTCATATACTCG
CTGGACCTGGCCCAGCTCTTTATCTGGGTCCTGCGGGAGTACAATGAAGTGGAGCCCATC
ATCCTCTCCGTGGGCGAGGAAGATGAGGTCTCCATCAAGGAGGCAGCCGAGGCGGTGGTG
GAGGCCATGGACTTCCATGGGGAAGTCACCTTTGATACAACCAAGTCGGATGGGCAGTTT
AAGAAGACAGCCAGTAACAGCAAGCTGAGGACCTACCTGCCCGACTTCCGGTTCACACCC
TTCAAGCAGGCGGTGAAGGAGACCTGTGCTTGGTTCACTGACAACTACGAGCAGGCCCGG
AAGTGA
Enzyme 82 GenBank Gene ID U58766 Link Image
Enzyme 82 GeneCard ID TSTA3 Link Image
Enzyme 82 GenAtlas ID TSTA3 Link Image
Enzyme 82 HGNC ID HGNC:12390 Link Image
Enzyme 82 Chromosome Location 8
Enzyme 82 Locus 8q24.3
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Tonetti M, Sturla L, Bisso A, Benatti U, De Flora A: Synthesis of GDP-L-fucose by the human FX protein. J Biol Chem. 1996 Nov 1;271(44):27274-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Camardella L, Carratore V, Ciardiello MA, Damonte G, Benatti U, De Flora A: Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum- transplantation antigen P35B. Blood. 1995 Jan 1;85(1):264-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 6214
Enzyme 83 Name Nitric oxide synthase, inducible
Enzyme 83 Synonyms
  1. Hepatocyte NOS
  2. HEP-NOS
  3. Inducible NO synthase
  4. Inducible NOS
  5. iNOS
  6. NOS type II
Enzyme 83 Gene Name NOS2
Enzyme 83 Protein Sequence >Nitric oxide synthase, inducible 
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
Enzyme 83 Number of Residues 1153
Enzyme 83 Molecular Weight 131116.3
Enzyme 83 Theoretical pI 8.01
Enzyme 83 GO Classification
Function
  • FAD or FADH2 binding
  • FMN binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleoside binding
  • transition metal ion binding
Process
  • cellular nitrogen compound biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitric oxide biosynthetic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 83 General Function Involved in oxidoreductase activity
Enzyme 83 Specific Function Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions
Enzyme 83 Pathways
Enzyme 83 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+ [RN:R00557]
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • None
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein Not Available
Enzyme 83 UniProtKB/Swiss-Prot ID P35228 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name NOS2_HUMAN Link Image
Enzyme 83 PDB ID 2NSI Link Image
Enzyme 83 PDB File Show
Enzyme 83 3D Structure
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >3462 bp 
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGCTCCATAGTTTCCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGCCCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTTCCTGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCCGAGATGGCCAGGGTCCCCTGCAC
CACGGCGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGGCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGCGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTTGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
Enzyme 83 GenBank Gene ID L24553 Link Image
Enzyme 83 GeneCard ID NOS2 Link Image
Enzyme 83 GenAtlas ID NOS2 Link Image
Enzyme 83 HGNC ID HGNC:7873 Link Image
Enzyme 83 Chromosome Location 1
Enzyme 83 Locus 17q11.2-q12
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Sherman PA, Laubach VE, Reep BR, Wood ER: Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. Biochemistry. 1993 Nov 2;32(43):11600-5. [PubMed Link Image]
  2. Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR: Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3491-5. [PubMed Link Image]
  3. Charles IG, Palmer RM, Hickery MS, Bayliss MT, Chubb AP, Hall VS, Moss DW, Moncada S: Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11419-23. [PubMed Link Image]
  4. Maier R, Bilbe G, Rediske J, Lotz M: Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. Biochim Biophys Acta. 1994 Sep 21;1208(1):145-50. [PubMed Link Image]
  5. Park CS, Pardhasaradhi K, Gianotti C, Villegas E, Krishna G: Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA. Biochem Biophys Res Commun. 1994 Nov 30;205(1):85-91. [PubMed Link Image]
  6. Hokari A, Zeniya M, Esumi H: Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. J Biochem (Tokyo). 1994 Sep;116(3):575-81. [PubMed Link Image]
  7. Guo FH, De Raeve HR, Rice TW, Stuehr DJ, Thunnissen FB, Erzurum SC: Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7809-13. [PubMed Link Image]
  8. Luss H, Li RK, Shapiro RA, Tzeng E, McGowan FX, Yoneyama T, Hatakeyama K, Geller DA, Mickle DA, Simmons RL, Billiar TR: Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS. J Mol Cell Cardiol. 1997 Apr;29(4):1153-65. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. McLay JS, Chatterjee P, Nicolson AG, Jardine AG, McKay NG, Ralston SH, Grabowski P, Haites NE, MacLeod AM, Hawksworth GM: Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism? Kidney Int. 1994 Oct;46(4):1043-9. [PubMed Link Image]
  11. Fujisawa H, Ogura T, Hokari A, Weisz A, Yamashita J, Esumi H: Inducible nitric oxide synthase in a human glioblastoma cell line. J Neurochem. 1995 Jan;64(1):85-91. [PubMed Link Image]
  12. Bloch KD, Wolfram JR, Brown DM, Roberts JD Jr, Zapol DG, Lepore JJ, Filippov G, Thomas JE, Jacob HJ, Bloch DB: Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17. Genomics. 1995 Jun 10;27(3):526-30. [PubMed Link Image]
  13. Taylor BS, Alarcon LH, Billiar TR: Inducible nitric oxide synthase in the liver: regulation and function. Biochemistry (Mosc). 1998 Jul;63(7):766-81. [PubMed Link Image]
  14. Glynne PA, Darling KE, Picot J, Evans TJ: Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem. 2002 Sep 6;277(36):33132-8. Epub 2002 Jun 21. [PubMed Link Image]
  15. Li H, Raman CS, Glaser CB, Blasko E, Young TA, Parkinson JF, Whitlow M, Poulos TL: Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. J Biol Chem. 1999 Jul 23;274(30):21276-84. [PubMed Link Image]
  16. Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed Link Image]
  17. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 6216
Enzyme 84 Name Nitric oxide synthase, brain
Enzyme 84 Synonyms
  1. Constitutive NOS
  2. NC-NOS
  3. NOS type I
  4. Neuronal NOS
  5. N-NOS
  6. nNOS
  7. bNOS
Enzyme 84 Gene Name NOS1
Enzyme 84 Protein Sequence >Nitric oxide synthase, brain 
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
Enzyme 84 Number of Residues 1434
Enzyme 84 Molecular Weight 160969.1
Enzyme 84 Theoretical pI 7.44
Enzyme 84 GO Classification
Function
  • FAD or FADH2 binding
  • FMN binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleoside binding
  • transition metal ion binding
Process
  • cellular nitrogen compound biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitric oxide biosynthetic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 84 General Function Involved in oxidoreductase activity
Enzyme 84 Specific Function Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter
Enzyme 84 Pathways
Enzyme 84 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+ [RN:R00557]
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein 642526 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID P29475 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name NOS1_HUMAN Link Image
Enzyme 84 PDB ID 1TLL Link Image
Enzyme 84 PDB File Show
Enzyme 84 3D Structure
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >4305 bp 
ATGGAGGATCACATGTTCGGTGTTCAGCAAATCCAGCCCAATGTCATTTCTGTTCGTCTC
TTCAAGCGCAAAGTTGGGGGCCTGGGATTTCTGGTGAAGGAGCGGGTCAGTAAGCCGCCC
GTGATCATCTCTGACCTGATTCGTGGGGGCGCCGCAGAGCAGAGTGGCCTCATCCAGGCC
GGAGACATCATTCTTGCGGTCAACGGCCGGCCCTTGGTGGACCTGAGCTATGACAGCGCC
CTGGAGGTACTCAGAGGCATTGCCTCTGAGACCCACGTGGTCCTCATTCTGAGGGGCCCT
GAAGGTTTCACCACGCACCTGGAGACCACCTTTACAGGTGATGGGACCCCCAAGACCATC
CGGGTGACACAGCCCCTGGGTCCCCCCACCAAAGCCGTGGATCTGTCCCACCAGCCACCG
GCCGGCAAAGAACAGCCCCTGGCAGTGGATGGGGCCTCGGGTCCCGGGAATGGGCCTCAG
CATGCCTACGATGATGGGCAGGAGGCTGGCTCACTCCCCCATGCCAACGGCCTGGCCCCC
AGGCCCCCAGGCCAGGACCCCGCGAAGAAAGCAACCAGAGTCAGCCTCCAAGGCAGAGGG
GAGAACAATGAACTGCTCAAGGAGATAGAGCCTGTGCTGAGCCTTCTCACCAGTGGGAGC
AGAGGGGTCAAGGGAGGGGCACCTGCCAAGGCAGAGATGAAAGATATGGGAATCCAGGTG
GACAGAGATTTGGACGGCAAGTCACACAAACCTCTGCCCCTCGGCGTGGAGAACGACCGA
GTCTTCAATGACCTATGGGGGAAGGGCAATGTGCCTGTCGTCCTCAACAACCCATATTCA
GAGAAGGAGCAGCCCCCCACCTCAGGAAAACAGTCCCCCACAAAGAATGGCAGCCCCTCC
AAGTGTCCACGCTTCCTCAAGGTCAAGAACTGGGAGACTGAGGTGGTTCTCACTGACACC
CTCCACCTTAAGAGCACATTGGAAACGGGATGCACTGAGTACATCTGCATGGGCTCCATC
ATGCATCCTTCTCAGCATGCAAGGAGGCCTGAAGACGTCCGCACAAAAGGACAGCTCTTC
CCTCTCGCCAAAGAGTTTATTGATCAATACTATTCATCAATTAAAAGATTTGGCTCCAAA
GCCCACATGGAAAGGCTGGAAGAGGTGAACAAAGAGATCGACACCACTAGCACTTACCAG
CTCAAGGACACAGAGCTCATCTATGGGGCCAAGCACGCCTGGCGGAATGCCTCGCGCTGT
GTGGGCAGGATCCAGTGGTCCAAGCTGCAGGTATTCGATGCCCGTGACTGCACCACGGCC
CACGGGATGTTCAACTACATCTGTAACCATGTCAAGTATGCCACCAACAAAGGGAACCTC
AGGTCTGCCATCACCATATTCCCCCAGAGGACAGACGGCAAGCACGACTTCCGAGTCTGG
AACTCCCAGCTCATCCGCTACGCTGGCTACAAGCAGCCTGACGGCTCCACCCTGGGGGAC
CCAGCCAATGTGCAGTTCACAGAGATATGCATACAGCAGGGCTGGAAACCGCCTAGAGGC
CGCTTCGATGTCCTGCCGCTCCTGCTTCAGGCCAACGGCAATGACCCTGAGCTCTTCCAG
ATTCCTCCAGAGCTGGTGTTGGAAGTTCCCATCAGGCACCCCAAGTTTGAGTGGTTCAAG
GACCTGGGGCTGAAGTGGTACGGCCTCCCCGCCGTGTCCAACATGCTCCTAGAGATTGGC
GGCCTGGAGTTCAGCGCCTGTCCCTTCAGTGGCTGGTACATGGGCACAGAGATTGGTGTC
CGCGACTACTGTGACAACTCCCGCTACAATATCCTGGAGGAAGTGGCCAAGAAGATGAAC
TTAGACATGAGGAAGACGTCCTCCCTGTGGAAGGACCAGGCGCTGGTGGAGATCAATATC
GCGGTTCTCTATAGCTTCCAGAGTGACAAAGTGACCATTGTTGACCATCACTCCGCCACC
GAGTCCTTCATTAAGCACATGGAGAATGAGTACCGCTGCCGGGGGGGCTGCCCTGCCGAC
TGGGTGTGGATCGTGCCCCCCATGTCCGGAAGCATCACCCCTGTGTTCCACCAGGAGATG
CTCAACTACCGGCTCACCCCCTCCTTCGAATACCAGCCTGATCCCTGGAACACGCATGTC
TGGAAAGGCACCAACGGGACCCCCACAAAGCGGCGAGCCATCGGCTTCAAGAAGCTAGCA
GAAGCTGTCAAGTTCTCGGCCAAGCTGATGGGGCAGGCTATGGCCAAGAGGGTGAAAGCG
ACCATCCTCTATGCCACAGAGACAGGCAAATCGCAAGCTTATGCCAAGACCTTGTGTGAG
ATCTTCAAACACGCCTTTGATGCCAAGGTGATGTCCATGGAAGAATATGACATTGTGCAC
CTGGAACATGAAACTCTGGTCCTTGTGGTCACCAGCACCTTTGGCAATGGAGATCCCCCT
GAGAATGGGGAGAAATTCGGCTGTGCTTTGATGGAAATGAGGCACCCCAACTCTGTGCAG
GAAGAAAGGAAGAGCTACAAGGTCCGATTCAACAGCGTCTCCTCCTACTCTGACTCCCAA
AAATCATCAGGCGATGGGCCCGACCTCAGAGACAACTTTGAGAGTGCTGGACCCCTGGCC
AATGTGAGGTTCTCAGTTTTTGGCCTCGGCTCACGAGCATACCCTCACTTTTGCGCCTTC
GGACACGCTGTGGACACCCTCCTGGAAGAACTGGGAGGGGAGAGGATCCTGAAGATGAGG
GAAGGGGATGAGCTCTGTGGGCAGGAAGAGGCTTTCAGGACCTGGGCCAAGAAGGTCTTC
AAGGCAGCCTGTGATGTCTTCTGTGTGGGAGATGATGTCAACATTGAAAAGGCCAACAAT
TCCCTCATCAGCAATGATCGCAGCTGGAAGAGAAACAAGTTCCGCCTCACCTTTGTGGCC
GAAGCTCCAGAACTCACACAAGGTCTATCCAATGTCCACAAAAAGCGAGTCTCAGCTGCC
CGGCTCCTTAGCCGTCAAAACCTCCAGAGCCCTAAATCCAGTCGGTCAACTATCTTCGTG
CGTCTCCACACCAACGGGAGCCAGGAGCTGCAGTACCAGCCTGGGGACCACCTGGGTGTC
TTCCCTGGCAACCACGAGGACCTCGTGAATGCCCTGATCGAGCGGCTGGAGGACGCGCCG
CCTGTCAACCAGATGGTGAAAGTGGAACTGCTGGAGGAGCGGAACACGGCTTTAGGTGTC
ATCAGTAACTGGACAGACGAGCTCCGCCTCCCGCCCTGCACCATCTTCCAGGCCTTCAAG
TACTACCTGGACATCACCACGCCACCAACGCCTCTGCAGCTGCAGCAGTTTGCCTCCCTA
GCTACCAGCGAGAAGGAGAAGCAGCGTCTGCTGGTCCTCAGCAAGGGTTTGCAGGAGTAC
GAGGAATGGAAATGGGGCAAGAACCCCACCATCGTGGAGGTGCTGGAGGAGTTCCCATCT
ATCCAGATGCCGGCCACCCTGCTCCTGACCCAGCTGTCCCTGCTGCAGCCCCGCTACTAT
TCCATCAGCTCCTCCCCAGACATGTACCCTGATGAAGTGCACCTCACTGTGGCCATCGTT
TCCTACCGCACTCGAGATGGAGAAGGACCAATTCACCACGGCGTATGCTCCTCCTGGCTC
AACCGGATACAGGCTGACGAACTGGTCCCCTGTTTCGTGAGAGGAGCACCCAGCTTCCAC
CTGCCCCGGAACCCCCAAGTCCCCTGCATCCTCGTTGGACCAGGCACCGGCATTGCCCCT
TTCCGAAGCTTCTGGCAACAGCGGCAATTTGATATCCAACACAAAGGAATGAACCCCTGC
CCCATGGTCCTGGTCTTCGGGTGCCGGCAATCCAAGATAGATCATATCTACAGGGAAGAG
ACCCTGCAGGCCAAGAACAAGGGGGTCTTCAGAGAGCTGTACACGGCTTACTCCCGGGAG
CCAGACAAACCAAAGAAGTACGTGCAGGACATCCTGCAGGAGCAGCTGGCGGAGTCTGTG
TACCGAGCCCTGAAGGAGCAAGGGGGCCACATATACGTCTGTGGGGACGTCACCATGGCT
GCTGATGTCCTCAAAGCCATCCAGCGCATCATGACCCAGCAGGGGAAGCTCTCGGCAGAG
GACGCCGGCGTATTCATCAGCCGGATGAGGGATGACAACCGATACCATGAGGATATTTTT
GGAGTCACCCTGCGAACGTACGAAGTGACCAACCGCCTTAGATCTGAGTCCATTGCCTTC
ATTGAAGAGAGCAAAAAAGACACCGATGAGGTTTTCAGCTCCTAA
Enzyme 84 GenBank Gene ID U17327 Link Image
Enzyme 84 GeneCard ID NOS1 Link Image
Enzyme 84 GenAtlas ID NOS1 Link Image
Enzyme 84 HGNC ID HGNC:7872 Link Image
Enzyme 84 Chromosome Location 1
Enzyme 84 Locus 12q24.2-q24.31
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Hall AV, Antoniou H, Wang Y, Cheung AH, Arbus AM, Olson SL, Lu WC, Kau CL, Marsden PA: Structural organization of the human neuronal nitric oxide synthase gene (NOS1). J Biol Chem. 1994 Dec 30;269(52):33082-90. [PubMed Link Image]
  2. Fujisawa H, Ogura T, Kurashima Y, Yokoyama T, Yamashita J, Esumi H: Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines. J Neurochem. 1994 Jul;63(1):140-5. [PubMed Link Image]
  3. Nakane M, Schmidt HH, Pollock JS, Forstermann U, Murad F: Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle. FEBS Lett. 1993 Jan 25;316(2):175-80. [PubMed Link Image]
  4. Park CS, Gianotti C, Park R, Krishna G: Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina. Cell Mol Neurobiol. 1996 Aug;16(4):499-515. [PubMed Link Image]
  5. Wang Y, Goligorsky MS, Lin M, Wilcox JN, Marsden PA: A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase. J Biol Chem. 1997 Apr 25;272(17):11392-401. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 6217
Enzyme 85 Name Nitric oxide synthase, endothelial
Enzyme 85 Synonyms
  1. Constitutive NOS
  2. cNOS
  3. EC-NOS
  4. Endothelial NOS
  5. eNOS
  6. NOS type III
  7. NOSIII
Enzyme 85 Gene Name NOS3
Enzyme 85 Protein Sequence >Nitric oxide synthase, endothelial 
MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLT
QPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAP
EQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGD
FRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPP
ELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMST
EIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDH
HAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW
KGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGR
LFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSS
PRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHF
CAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAA
RDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATIL
VRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGP
PPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRY
EEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVL
AYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAP
FRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSRE
PDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELD
EAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDT
NSP
Enzyme 85 Number of Residues 1203
Enzyme 85 Molecular Weight 133287.6
Enzyme 85 Theoretical pI 7.27
Enzyme 85 GO Classification
Function
  • FAD or FADH2 binding
  • FMN binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleoside binding
  • transition metal ion binding
Process
  • cellular nitrogen compound biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitric oxide biosynthetic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 85 General Function Involved in oxidoreductase activity
Enzyme 85 Specific Function Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets
Enzyme 85 Pathways
Enzyme 85 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+ [RN:R00557]
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein Not Available
Enzyme 85 UniProtKB/Swiss-Prot ID P29474 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name NOS3_HUMAN Link Image
Enzyme 85 PDB ID 3NOS Link Image
Enzyme 85 PDB File Show
Enzyme 85 3D Structure
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >3612 bp 
ATGGGCAACTTGAAGAGCGTGGCCCAGGAGCCTGGGCCACCCTGCGGCCTGGGGCTGGGG
CTGGGCCTTGGGCTGTGCGGCAAGCAGGGCCCAGCCACCCCGGCCCCTGAGCCCAGCCGG
GCCCCAGCATCCCTACTCCCACCAGCGCCAGAACACAGCCCCCCGAGCTCCCCGCTAACC
CAGCCCCCAGAGGGGCCCAAGTTCCCTCGTGTGAAGAACTGGGAGGTGGGGAGCATCACC
TATGACACCCTCAGCGCCCAGGCGCAGCAGGATGGGCCCTGCACCCCAAGACGCTGCCTG
GGCTCCCTGGTATTTCCACGGAAACTACAGGGCCGGCCCTCCCCCGGCCCCCCGGCCCCT
GAGCAGCTGCTGAGTCAGGCCCGGGACTTCATCAACCAGTACTACAGCTCCATTAAGAGG
AGCGGCTCCCAGGCCCACGAACAGCGGCTTCAAGAGGTGGAAGCCGAGGTGGCAGCCACA
GGCACCTACCAGCTTAGGGAGAGCGAGCTGGTGTTCGGGGCTAAGCAGGCCTGGCGCAAC
GCTCCCCGCTGCGTGGGCCGGATCCAGTGGGGGAAGCTGCAGGTGTTCGATGCCCGGGAC
TGCAGGTCTGCACAGGAAATGTTCACCTACATCTGCAACCACATCAAGTATGCCACCAAC
CGGGGCAACCTTCGCTCGGCCATCACAGTGTTCCCGCAGCGCTGCCCTGGCCGAGGAGAC
TTCCGAATCTGGAACAGCCAGCTGGTGCGCTACGCGGGCTACCGGCAGCAGGACGGCTCT
GTGCGGGGGGACCCAGCCAACGTGGAGATCACCGAGCTCTGCATTCAGCACGGCTGGACC
CCAGGAAACGGTCGCTTCGACGTGCTGCCCCTGCTGCTGCAGGCCCCAGATGAGCCCCCA
GAACTCTTCCTTCTGCCCCCCGAGCTGGTCCTTGAGGTGCCCCTGGAGCACCCCACGCTG
GAGTGGTTTGCAGCCCTGGGCCTGCGCTGGTACGCCCTCCCGGCAGTGTCCAACATGCTG
CTGGAAATTGGGGGCCTGGAGTTCCCCGCAGCCCCCTTCAGTGGCTGGTACATGAGCACT
GAGATCGGCACGAGGAACCTGTGTGACCCTCACCGCTACAACATCCTGGAGGATGTGGCT
GTCTGCATGGACCTGGATACCCGGACCACCTCGTCCCTGTGGAAAGACAAGGCAGCAGTG
GAAATCAACGTGGCCGTGCTGCACAGTTACCAGCTAGCCAAAGTCACCATCGTGGACCAC
CACGCCGCCACGGCCTCTTTCATGAAGCACCTGGAGAATGAGCAGAAGGCCAGGGGGGGC
TGCCCTGCAGACTGGGCCTGGATCGTGCCCCCCATCTCGGGCAGCCTCACTCCTGTTTTC
CATCAGGAGATGGTCAACTATTTCCTGTCCCCGGCCTTCCGCTACCAGCCAGACCCCTGG
AAGGGGAGTGCCGCCAAGGGCACCGGCATCACCAGGAAGAAGACCTTTAAAGAAGTGGCC
AACGCCGTGAAGATCTCCGCCTCGCTCATGGGCACGGTGATGGCGAAGCGAGTGAAGGCG
ACAATCCTGTATGGCTCCGAGACCGGCCGGGCCCAGAGCTACGCACAGCAGCTGGGGAGA
CTCTTCCGGAAGGCTTTTGATCCCCGGGTCCTGTGTATGGATGAGTATGACGTGGTGTCC
CTCGAACACGAGACGCTGGTGCTGGTGGTAACCAGCACATTTGGGAATGGGGATCCCCCG
GAGAATGGAGAGAGCTTTGCAGCTGCCCTGATGGAGATGTCCGGCCCCTACAACAGCTCC
CCTCGGCCGGAACAGCACAAGAGTTATAAGATCCGCTTCAACAGCATCTCCTGCTCAGAC
CCACTGGTGTCCTCTTGGCGGCGGAAGAGGAAGGAGTCCAGTAACACAGACAGTGCAGGG
GCCCTGGGCACCCTCAGGTTCTGTGTGTTCGGGCTCGGCTCCCGGGCATACCCCCACTTC
TGCGCCTTTGCTCGTGCCGTGGACACACGGCTGGAGGAACTGGGCGGGGAGCGGCTGCTG
CAGCTGGGCCAGGGCGACGAGCTGTGCGGCCAGGAGGAGGCCTTCCGAGGCTGGGCCCAG
GCTGCCTTCCAGGCCGCCTGTGAGACCTTCTGTGTGGGAGAGGATGCCAAGGCCGCCGCC
CGAGACATCTTCAGCCCCAAACGGAGCTGGAAGCGCCAGAGGTACCGGCTGAGCGCCCAG
GCCGAGGGCCTGCAGTTGCTGCCAGGTCTGATCCACGTGCACAGGCGGAAGATGTTCCAG
GCTACAATCCGCTCAGTGGAAAACCTGCAAAGCAGCAAGTCCACGAGGGCCACCATCCTG
GTGCGCCTGGACACCGGAGGCCAGGAGGGGCTGCAGTACCAGCCGGGGGACCACATAGGT
GTCTGCCCGCCCAACCGGCCCGGCCTTGTGGAGGCGCTGCTGAGCCGCGTGGAGGACCCG
CCGGCGCCCACTGAGCCCGTGGCAGTAGAGCAGCTGGAGAAGGGCAGCCCTGGTGGCCCT
CCCCCCGGCTGGGTGCGGGACCCCCGGCTGCCCCCGTGCACGCTGCGCCAGGCTCTCACC
TTCTTCCTGGACATCACCTCCCCACCCAGCCCTCAGCTCTTGCGGCTGCTCAGCACCTTG
GCAGAAGAGCCCAGGGAACAGCAGGAGCTGGAGGCCCTCAGCCAGGATCCCCGACGCTAC
GAGGAGTGGAAGTGGTTCCGCTGCCCCACGCTGCTGGAGGTGCTGGAGCAGTTCCCGTCG
GTGGCGCTGCCTGCCCCACTGCTCCTCACCCAGCTGCCTCTGCTCCAGCCCCGGTACTAC
TCAGTCAGCTCGGCACCCAGCACCCACCCAGGAGAGATCCACCTCACTGTAGCTGTGCTG
GCATACAGGACTCAGGATGGGCTGGGCCCCCTGCACTATGGAGTCTGCTCCACGTGGCTA
AGCCAGCTCAAGCCCGGAGACCCTGTGCCCTGCTTCATCCGGGGGGCTCCCTCCTTCCGG
CTGCCACCCGATCCCAGCTTGCCCTGCATCCTGGTGGGTCCAGGCACTGGCATTGCCCCC
TTCCGGGGATTCTGGCAGGAGCGGCTGCATGACATTGAGAGCAAAGGGCTGCAGCCCACT
CCCATGACTTTGGTGTTCGGCTGCCGATGCTCCCAACTTGACCATCTCTACCGCGACGAG
GTGCAGAACGCCCAGCAGCGCGGGGTGTTTGGCCGAGTCCTCACCGCCTTCTCCCGGGAA
CCTGACAACCCCAAGACCTACGTGCAGGACATCCTGAGGACGGAGCTGGCTGCGGAGGTG
CACCGCGTGCTGTGCCTCGAGCGGGGCCACATGTTTGTCTGCGGCGATGTTACCATGGCA
ACCAACGTCCTGCAGACCGTGCAGCGCATCCTGGCGACGGAGGGCGACATGGAGCTGGAC
GAGGCCGGCGACGTCATCGGCGTGCTGCGGGATCAGCAACGCTACCACGAAGACATTTTC
GGGCTCACGCTGCGCACCCAGGAGGTGACAAGCCGCATACGCACCCAGAGCTTTTCCTTG
CAGGAGCGTCAGTTGCGGGGCGCAGTGCCCTGGGCGTTCGACCCTCCCGGCTCAGACACC
AACAGCCCCTGA
Enzyme 85 GenBank Gene ID M93718 Link Image
Enzyme 85 GeneCard ID NOS3 Link Image
Enzyme 85 GenAtlas ID NOS3 Link Image
Enzyme 85 HGNC ID HGNC:7876 Link Image
Enzyme 85 Chromosome Location 7
Enzyme 85 Locus 7q36
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Janssens SP, Shimouchi A, Quertermous T, Bloch DB, Bloch KD: Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. J Biol Chem. 1992 Jul 25;267(21):14519-22. [PubMed Link Image]
  2. Marsden PA, Schappert KT, Chen HS, Flowers M, Sundell CL, Wilcox JN, Lamas S, Michel T: Molecular cloning and characterization of human endothelial nitric oxide synthase. FEBS Lett. 1992 Aug 3;307(3):287-93. [PubMed Link Image]
  3. Marsden PA, Heng HH, Scherer SW, Stewart RJ, Hall AV, Shi XM, Tsui LC, Schappert KT: Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene. J Biol Chem. 1993 Aug 15;268(23):17478-88. [PubMed Link Image]
  4. Nadaud S, Bonnardeaux A, Lathrop M, Soubrier F: Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1027-33. [PubMed Link Image]
  5. Miyahara K, Kawamoto T, Sase K, Yui Y, Toda K, Yang LX, Hattori R, Aoyama T, Yamamoto Y, Doi Y, et al.: Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene. Eur J Biochem. 1994 Aug 1;223(3):719-26. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Robinson LJ, Weremowicz S, Morton CC, Michel T: Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene. Genomics. 1994 Jan 15;19(2):350-7. [PubMed Link Image]
  10. Sase K, Michel T: Expression of constitutive endothelial nitric oxide synthase in human blood platelets. Life Sci. 1995;57(22):2049-55. [PubMed Link Image]
  11. Garvey EP, Tuttle JV, Covington K, Merrill BM, Wood ER, Baylis SA, Charles IG: Purification and characterization of the constitutive nitric oxide synthase from human placenta. Arch Biochem Biophys. 1994 Jun;311(2):235-41. [PubMed Link Image]
  12. Dedio J, Konig P, Wohlfart P, Schroeder C, Kummer W, Muller-Esterl W: NOSIP, a novel modulator of endothelial nitric oxide synthase activity. FASEB J. 2001 Jan;15(1):79-89. [PubMed Link Image]
  13. Zimmermann K, Opitz N, Dedio J, Renne C, Muller-Esterl W, Oess S: NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):17167-72. Epub 2002 Nov 21. [PubMed Link Image]
  14. Icking A, Matt S, Opitz N, Wiesenthal A, Muller-Esterl W, Schilling K: NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS. J Cell Sci. 2005 Nov 1;118(Pt 21):5059-69. Epub 2005 Oct 18. [PubMed Link Image]
  15. Schleicher M, Brundin F, Gross S, Muller-Esterl W, Oess S: Cell cycle-regulated inactivation of endothelial NO synthase through NOSIP-dependent targeting to the cytoskeleton. Mol Cell Biol. 2005 Sep;25(18):8251-8. [PubMed Link Image]
  16. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  17. Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed Link Image]
  18. Rosenfeld RJ, Garcin ED, Panda K, Andersson G, Aberg A, Wallace AV, Morris GM, Olson AJ, Stuehr DJ, Tainer JA, Getzoff ED: Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency. Biochemistry. 2002 Nov 26;41(47):13915-25. [PubMed Link Image]
  19. Yoshimura M, Yasue H, Nakayama M, Shimasaki Y, Sumida H, Sugiyama S, Kugiyama K, Ogawa H, Ogawa Y, Saito Y, Miyamoto Y, Nakao K: A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese. Hum Genet. 1998 Jul;103(1):65-9. [PubMed Link Image]
  20. Sofowora G, Dishy V, Xie HG, Imamura H, Nishimi Y, Morales CR, Morrow JD, Kim RB, Stein CM, Wood AJ: In-vivo effects of Glu298Asp endothelial nitric oxide synthase polymorphism. Pharmacogenetics. 2001 Dec;11(9):809-14. [PubMed Link Image]
  21. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 6225
Enzyme 86 Name 10-formyltetrahydrofolate dehydrogenase
Enzyme 86 Synonyms
  1. 10-FTHFDH
  2. Aldehyde dehydrogenase family 1 member L1
Enzyme 86 Gene Name ALDH1L1
Enzyme 86 Protein Sequence >10-formyltetrahydrofolate dehydrogenase 
MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWR
AKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIN
WTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAV
RLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQ
KLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMI
LASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRL
VEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRM
PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKI
SARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKI
QGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ
VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK
SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH
DEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP
RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFT
RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF
EY
Enzyme 86 Number of Residues 902
Enzyme 86 Molecular Weight 98828.5
Enzyme 86 Theoretical pI 5.76
Enzyme 86 GO Classification
Function
  • acyl carrier activity
  • binding
  • catalytic activity
  • cofactor binding
  • formyltetrahydrofolate dehydrogenase activity
  • glycine hydroxymethyltransferase activity
  • hydroxymethyl-, formyl- and related transferase activity
  • methyltransferase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
  • substrate-specific transporter activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transporter activity
Process
  • 10-formyltetrahydrofolate catabolic process
  • 10-formyltetrahydrofolate metabolic process
  • biosynthetic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
  • one-carbon metabolic process
  • oxidation reduction
  • tetrahydrofolate metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 86 General Function Involved in formyltetrahydrofolate dehydrogenase activity
Enzyme 86 Specific Function 10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH
Enzyme 86 Pathways
Enzyme 86 Reactions
  • 10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+ [RN:R00941]
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 3560541 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID O75891 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name FTHFD_HUMAN Link Image
Enzyme 86 PDB ID 1S3I Link Image
Enzyme 86 PDB File Show
Enzyme 86 3D Structure
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >2709 bp 
ATGAAGATTGCAGTGATTGGACAGAGCCTGTTTGGCCAGGAAGTTTACTGCCACCTGAGG
AAGGAGGGCCACGAAGTGGTGGGTGTGTTCACTGTTCCAGACAAGGATGGAAAGGCCGAC
CCCCTGGGTCTGGAAGCTGAGAAGGATGGAGTGCCGGTATTCAAGTACTCCCGGTGGCGT
GCAAAAGCGCAAGCTTTGCCTGATGTGGTGGCAAAATACCAGGCTTTGGGGGCCGAACTC
AACGTCCTGCCCTCCTGCAGCCAATTCATCCCCATGGAGATAATCAGTGCCCCCCGGCAT
GGCTCCATCATCTATCACCCGTCACTGCTCCCTAGGCACCGAGGGGCCTCGGCCATCAAC
TGGACCCTCATTCACGGAGATAAGAAAGGGGGGTTTTCCATCTTCTGGGCGGATGATGGT
CTGGACACCGGAGACCTGCTGCTGCAGAAGGAGTGTGAGGTGCTCCCGGACGACACCGTG
AGCACGCTGTACAACCGCTTCCTCTTCCCTGAAGGCATCAAAGGGGTGGTGCAGGCCGTG
AGGCTGATCGCTGAGGGCAAAGCCCCCAGACTCCCTCAGCCTAAGGAAGGAGCCACCTAT
GAGGGGATTCAGAAGAAGGAGACAGCCAAGATCAACTGGGACCAGCCGGCAGAGGCCATT
CACAACTGGATCCGCGGGAACGACAAGGTGCCGGGAGCCTGGACAGAGGCCTGTGAACAG
AAACTGACATTTTTCAACTCAACGCTGAACACTTCAGGCCTGGTGCCCGAGGGAGACGCT
TTGCCCATCCCAGGAGCCCATCGGCCAGGGGTGGTCACCAAAGCAGGACTCATCCTCTTT
GGGAATGATGACAAAATGCTGCTGGTGAAGAATATTCAGCTGGAGGATGGCAAAATGATC
CTGGCCTCGAACTTCTTTAAGGGGGCAGCCAGCAGTGTCCTTGAGCTGACAGAGGCAGAG
CTGGTTACTGCGGAGGCTGTGCGGAGTGTTTGGCAGCGGATCCTCCCCAAAGTACTGGAG
GTTGAAGACTCCACTGATTTCTTCAAGTCAGGGGCCGCGTCTGTGGACGTTGTGAGGCTG
GTGGAGGAAGTGAAGGAGCTGTGTGATGGCCTGGAGTTAGAAAATGAAGATGTGTACATG
GCATCCACCTTTGGGGACTTCATCCAGCTGTTAGTGAGGAAGCTGCGAGGGGACGATGAG
GAGGGCGAGTGCAGCATTGACTACGTGGAAATGGCAGTGAACAAGCGCACTGTCCGCATG
CCCCACCAGCTCTTCATTGGGGGGGAGTTCGTGGATGCCGAGGGCGCCAAGACCTCTGAG
ACCATCAATCCCACCGATGGAAGTGTCATCTGCCAGGTATCCCTGGCCCAAGTCACCGAC
GTCGACAAGGCAGTGGCCGCNGCCAAGGGTGCCTTTGAGAATGGACGGTGGGGGAAGATC
AGTGCGCGGGACCGGGGCCGGCTGATGTACAGGTTGGCAGATCTCATGGAGCAGCACCAG
GAGGAGCTGGCCACCATTGAGGCCCTGGATGCGGGTGCCGTCTACACGCTGGCCCTGAAG
ACCCACGTGGGCATGTCCATCCAGACCTTCCGATACTTTGCTGGCTGGTGTGACAAGATC
CAGGGCTCCACCATCCCCATCAACCAGGCCAGACCCAACCGCAACCTGACCTTGACCAGG
AAGGAGCCTGTTGGGGTTTGTGGCATCATCATCCCCTGGAACTATCCCCTGATGATGCTG
TCCTGGAAGACAGCTGCCTGCCTGGCTGCCGGGAACACAGTGGTGATCAAGCCTGCTCAG
GTGACCCCACTCACAGCCTTGAAGTTTGCAGAGCTGACATTAAAGGCCGGGATTCCCAAA
GGTGTGGTCAACGTCCTCCCAGGATCTGGCTCCCTGGTCGGCCAGAGACTCTCAGACCAT
CCTGATGTGAGGAAAATCGGGTTCACAGGCTCCACAGAGGTGGGCAAGCACATCATGAAA
AGCTGTGCCATAAGTAACGTGAAGAAGGTGTCCCTGGAACTGGGCGGGGAGTCACCCTTC
ATCATCTTTGCTGACTGTGACCTCAACAAGGCTGTGCAGATGGGGATGAGTTCTGTTTTC
TTCAGCAAAGGAGAGAATTGCATTGCAGCAGGCCGACTCTTTGTGGAGGACTCCATTCAT
GATGAGTTCGTGCGGAGAGTGGTAGAAGAGGTGCGGAAGATGAAGGTGGGCAACCCGCTG
GACAGGGACACCGACCACGGGCCGCAGAATCACCATGCCCACCTTGTGAAGCTGATGGAG
TACTGCCAGCATGGCGTGAAGGAAGGGGCCACACTGGTCTGCGGCGGGAATCAGGTCCCT
CGGCCAGGGTTCTTCTTTGAGCCAACTGTTTTCACAGACGTGGAAGACCACATGTTCATA
GCCAAGGAGGAGTCCTTCGGGCCTGTCATGATCATCTCTCGGTTTGCTGATGGGGACTTG
GATGCCGTGCTGTCTCGGGCCAATGCCACGGAATTTGGCCTGGCTTCTGGTGTCTTCACC
AGGGACATCAACAAGGCCCTGTATGTCAGTGACAAGCTCCAGGCAGGCACTGTGTTTGTC
AACACGTACAACAAGACCGACGTGGCCGCTCCCTTCGGAGGATTCAAACAGTCTGGATTT
GGCAAAGATCTAGGAGAGGCGGCTCTGAACGAGTACCTGCGGGTCAAGACAGTGACCTTC
GAATACTGA
Enzyme 86 GenBank Gene ID AF052732 Link Image
Enzyme 86 GeneCard ID ALDH1L1 Link Image
Enzyme 86 GenAtlas ID ALDH1L1 Link Image
Enzyme 86 HGNC ID HGNC:3978 Link Image
Enzyme 86 Chromosome Location 3
Enzyme 86 Locus 3q21.3
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  2. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 6236
Enzyme 87 Name Cysteine dioxygenase type 1
Enzyme 87 Synonyms
  1. Cysteine dioxygenase type I
  2. CDO
  3. CDO-I
Enzyme 87 Gene Name CDO1
Enzyme 87 Protein Sequence >Cysteine dioxygenase type 1 
MEQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMYAKFDQYRYTR
NLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKK
SERVLRENQCAYINDSIGLHRVENISHTEPAVSLHLYSPPFDTCHAFDQRTGHKNKVTMT
FHSKFGIRTPNATSGSLENN
Enzyme 87 Number of Residues 200
Enzyme 87 Molecular Weight 22971.7
Enzyme 87 Theoretical pI 6.58
Enzyme 87 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cysteine dioxygenase activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • transition metal ion binding
Process
  • L-cysteine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • cysteine metabolic process
  • metabolic process
  • oxidation reduction
  • sulfur amino acid metabolic process
Component
—
Enzyme 87 General Function Involved in iron ion binding
Enzyme 87 Specific Function Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range
Enzyme 87 Pathways
Enzyme 87 Reactions
  • L-cysteine + O2 = 3-sulfinoalanine [RN:R00893]
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • None
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein 467561 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID Q16878 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name CDO1_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >603 bp 
ATGGAACAGACCGAAGTGCTGAAGCCACGGACCCTGGCTGATCTGATCCGCATCCTGCAC
CAGCTCTTTGCCGGCGATGAGGTCAATGTAGAGGAGGTGCAGGCCATCATGGAAGCCTAC
GAGAGCGACCCCATCGAGTGGGCAATGTACGCCAAGTTCGACCAGTACAGGTATACCCGA
AATCTTGTGGATCAAGGAAATGGAAAATTTAATCTGATGATTCTCTGTTGGGGTGAAGGA
CATGGCAGCAGTATTCATGATCATACCAACTCCCACTGCTTTCTGAAGATGCTACAGGGA
AATCTAAAGGAGACATTATTTGCCTGGCCTGACAAAAAATCCAATGAGATGGTCAAGAAG
TCTGAAAGAGTCTTGAGGGAAAACCAGTGTGCCTACATCAATGATTCCATTGGCTTACAT
CGAGTAGAGAACATCAGCCATACGGAACCTGCTGTGAGCCTTCACTTGTACAGTCCACCT
TTTGATACATGCCATGCCTTTGATCAAAGAACAGGACATAAAAACAAAGTCACAATGACA
TTCCATAGTAAATTTGGAATCAGAACTCCAAATGCAACTTCGGGCTCGCTGGAGAACAAC
TAA
Enzyme 87 GenBank Gene ID Z31357 Link Image
Enzyme 87 GeneCard ID CDO1 Link Image
Enzyme 87 GenAtlas ID CDO1 Link Image
Enzyme 87 HGNC ID HGNC:1795 Link Image
Enzyme 87 Chromosome Location 5
Enzyme 87 Locus 5q23.2
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. McCann KP, Akbari MT, Williams AC, Ramsden DB: Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA. Biochim Biophys Acta. 1994 Nov 16;1209(1):107-10. [PubMed Link Image]
  2. Tsuboyama-Kasaoka N, Hosokawa Y, Kodama H, Matsumoto A, Oka J, Totani M: Human cysteine dioxygenase gene: structural organization, tissue-specific expression and downregulation by phorbol 12-myristate 13-acetate. Biosci Biotechnol Biochem. 1999 Jun;63(6):1017-24. [PubMed Link Image]
  3. Ramsden DB, Kapadi A, Fitch NJ, Farmer MJ, Bennett P, Williams AC: Human cysteine dioxygenase type I (CDO-I; EC 1.13.11.20): 5' flanking region and intron-exon structure of the gene. Mol Pathol. 1997 Oct;50(5):269-71. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z: An insight into the mechanism of human cysteine dioxygenase: Key roles of the thioether-bonded tyrosine-cysteine cofactor. J Biol Chem. 2006 Nov 29;. [PubMed Link Image]
  8. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 6298
Enzyme 88 Name Trans-2-enoyl-CoA reductase, mitochondrial
Enzyme 88 Synonyms
  1. Nuclear receptor-binding factor 1
  2. HsNrbf-1
  3. NRBF-1
Enzyme 88 Gene Name MECR
Enzyme 88 Protein Sequence >Trans-2-enoyl-CoA reductase, mitochondrial 
MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVEL
KNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGLLPELPAVGGNEGVAQVVAVGSNVT
GLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ
LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEE
ELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLL
IFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEAS
MKPFISSKQILTM
Enzyme 88 Number of Residues 373
Enzyme 88 Molecular Weight 40427.4
Enzyme 88 Theoretical pI 9.01
Enzyme 88 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 88 General Function Involved in zinc ion binding
Enzyme 88 Specific Function Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids
Enzyme 88 Pathways Not Available
Enzyme 88 Reactions
  • acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R07162]
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • None
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 4929595 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q9BV79 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name MECR_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >1122 bp 
ATGTGGGTCTGCAGTACCCTGTGGCGGGTGCGAACCCCGCCCGGCAGTGGCGGGGGCCTG
CTCCCAGCTTCTGGCTGTCACGGACCTGCCGCCTCCTCCTACTCCGCATCCGCCGAGCCT
GCCCGGGTCCGCGGCGTTGTCTATGGGCACCACGGGGATCCAGCCAAGGTCGTCGAACTC
AAGAACCTGGAGCTAGCTGCTGTGAGAGGATCAGATGTCCGTGTGAAGATGCTGGCGGCC
CCTATCAATCCATCTGACATAAATATGATCCAAGGAAACTACGGACTCCTTCCTGAACTG
CCTGCTGTTGGAGGGAACGAAGGTGTTGCACAGGTGGTAGCGGTGGGCAGCAATGTGACC
GGGCTGAAGCCAGGAGACTGGGTGATTCCAGCAAATGCTGGTTTAGGAACCTGGCGGACC
GAGGCTGTGTTCAGCGAGGAAGCACTGATCCAAGTTCCGAGTGACATCCCTCTTCAGAGC
GCTGCCACCCTGGGTGTCAATCCCTGCACAGCCTACAGGATGTTGATGGACTTCGAGCAA
CTGCAGCCAGGGGATTCTGTCATCCAGAATGCATCCAACAGCGGAGTGGGGCAAGCGGTC
ATCCAGATCGCCGCAGCCCTGGGCCTAAGAACCATCAATGTGGTCCGAGACAGACCTGAT
ATCCAGAAGCTGAGTGACAGACTGAAGAGTCTGGGGGCTGAGCATGTCATCACAGAAGAG
GAGCTAAGAAGGCCCGAAATGAAAAACTTCTTTAAGGACATGCCCCAGCCACGGCTTGCT
CTCAACTGTGTTGGTGGGAAAAGCTCCACAGAGCTGCTGCGCCAGTTAGCGCGTGGAGGA
ACCATGGTAACCTATGGGGGGATGGCCAAGCAGCCCGTCGTAGCCTCTGTGAGCCTGCTC
ATTTTTAAGGATCTCAAACTTCGAGGCTTTTGGTTGTCCCAGTGGAAGAAGGATCACAGT
CCAGACCAGTTCAAGGAGCTGATCCTCACACTGTGCGATCTCATCCGCCGAGGCCAGCTC
ACAGCCCCTGCCTGCTCCCAGGTCCCGCTGCAGGACTACCAGTCTGCCTTGGAAGCCTCC
ATGAAGCCCTTCATATCTTCAAAGCAGATTCTCACCATGTGA
Enzyme 88 GenBank Gene ID AF151821 Link Image
Enzyme 88 GeneCard ID MECR Link Image
Enzyme 88 GenAtlas ID MECR Link Image
Enzyme 88 HGNC ID HGNC:19691 Link Image
Enzyme 88 Chromosome Location 1
Enzyme 88 Locus 1p36.1-p35.1
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Miinalainen IJ, Chen ZJ, Torkko JM, Pirila PL, Sormunen RT, Bergmann U, Qin YM, Hiltunen JK: Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast mitochondrial fatty acid synthesis type II. J Biol Chem. 2003 May 30;278(22):20154-61. Epub 2003 Mar 24. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 6299
Enzyme 89 Name Peroxisomal trans-2-enoyl-CoA reductase
Enzyme 89 Synonyms
  1. TERP
  2. 2,4-dienoyl-CoA reductase-related protein
  3. DCR-RP
  4. HPDHase
  5. pVI-ARL
Enzyme 89 Gene Name PECR
Enzyme 89 Protein Sequence >Peroxisomal trans-2-enoyl-CoA reductase 
MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAD
ELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHIS
SKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYN
LTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVS
SVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEK
AKL
Enzyme 89 Number of Residues 303
Enzyme 89 Molecular Weight 32544.1
Enzyme 89 Theoretical pI 9.12
Enzyme 89 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • biological regulation
  • metabolic process
  • oxidation reduction
  • regulation of apoptosis
  • regulation of biological process
  • regulation of cell death
  • regulation of cellular process
  • regulation of programmed cell death
Component
—
Enzyme 89 General Function Involved in regulation of apoptosis
Enzyme 89 Specific Function Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity
Enzyme 89 Pathways Not Available
Enzyme 89 Reactions
  • acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R07162]
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein Not Available
Enzyme 89 UniProtKB/Swiss-Prot ID Q9BY49 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name PECR_HUMAN Link Image
Enzyme 89 PDB ID 1YXM Link Image
Enzyme 89 PDB File Show
Enzyme 89 3D Structure
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >912 bp 
ATGGCCTCCTGGGCTAAGGGCAGGAGCTACCTGGCGCCTGGTTTGCTGCAGGGCCAAGTG
GCCATCGTCACCGGCGGGGCCACGGGCATCGGAAAAGCCATCGTGAAGGAGCTCCTGGAG
CTGGGGAGTAATGTGGTCATTGCATCCCGTAAGTTGGAGAGATTGAAGTCTGCGGCAGAT
GAACTGCAGGCCAACCTACCTCCCACAAAGCAGGCACGAGTCATTCCCATACAATGCAAC
ATCCGGAATGAGGAGGAGGTGAATAATTTGGTCAAATCTACCTTAGATACTTTTGGTAAG
ATCAATTTCTTGGTGAACAATGGAGGAGGCCAGTTTCTTTCCCCTGCTGAACACATCAGT
TCTAAGGGATGGCACGCTGTGCTTGAGACCAACCTGACGGGTACCTTCTACATGTGCAAA
GCAGTTTACAGCTCCTGGATGAAAGAGCATGGAGGATCTATCGTCAATATCATTGTCCCT
ACTAAAGCTGGATTTCCATTAGCTGTGCATTCTGGAGCTGCAAGAGCAGGTGTTTACAAC
CTCACCAAATCTTTAGCTTTGGAATGGGCCTGCAGTGGAATACGGATCAATTGTGTTGCC
CCTGGAGTTATTTATTCCCAGACTGCTGTGGAGAACTATGGTTCCTGGGGACAAAGCTTC
TTTGAAGGGTCTTTTCAGAAAATCCCCGCTAAACGAATTGGTGTTCCTGAGGAGGTCTCC
TCTGTGGTCTGCTTCCTACTGTCTCCTGCAGCTTCCTTCATCACTGGACAGTCAGTGGAT
GTGGATGGGGGCCGGAGTCTCTATACTCACTCGTATGAGGTACCAGATCATGACAACTGG
CCCAAGGGAGCAGGGGACCTTTCTGTTGTCAAAAAGATGAAGGAGACCTTTAAGGAGAAA
GCTAAGCTCTGA
Enzyme 89 GenBank Gene ID AF232009 Link Image
Enzyme 89 GeneCard ID PECR Link Image
Enzyme 89 GenAtlas ID PECR Link Image
Enzyme 89 HGNC ID HGNC:18281 Link Image
Enzyme 89 Chromosome Location 2
Enzyme 89 Locus 2q35
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Das AK, Uhler MD, Hajra AK: Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs. J Biol Chem. 2000 Aug 11;275(32):24333-40. [PubMed Link Image]
  2. Amery L, Mannaerts GP, Subramani S, Van Veldhoven PP, Fransen M: Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology. Comb Chem High Throughput Screen. 2001 Nov;4(7):545-52. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Braastad CD, Leguia M, Hendrickson EA: Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element. Nucleic Acids Res. 2002 Apr 15;30(8):1713-24. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 6301
Enzyme 90 Name Leukotriene-B(4) omega-hydroxylase 1
Enzyme 90 Synonyms
  1. CYPIVF2
  2. Cytochrome P450 4F2
  3. Cytochrome P450-LTB-omega
  4. Leukotriene-B(4) 20-monooxygenase 1
Enzyme 90 Gene Name CYP4F2
Enzyme 90 Protein Sequence >Leukotriene-B(4) omega-hydroxylase 1 
MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWF
WGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPK
DKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQL
LASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEIL
LHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFID
VLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQE
LLKDREPKEIEWDDLAHLPFLTMCMKESLRLHPPVPVISRHVTQDIVLPDGRVIPKGIIC
LISVFGTHHNPAVWPDPEVYDPFRFDPENIKERSPLAFIPFSAGPRNCIGQTFAMAEMKV
VLALTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS
Enzyme 90 Number of Residues 520
Enzyme 90 Molecular Weight 59852.8
Enzyme 90 Theoretical pI 7.08
Enzyme 90 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 90 General Function Involved in monooxygenase activity
Enzyme 90 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 90 Pathways
Enzyme 90 Reactions
  • (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H+ + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14- tetraenoate + NADP+ + H2O [RN:R03866]
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 4519535 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID P78329 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name CP4F2_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >1563 bp 
ATGTCCCAGCTGAGCCTGTCCTGGCTGGGCCTCGGGCCAGTGGCAGCATCCCCTTGGCTG
CTCCTCCTGCTGGTCGGGGCCTCCTGGCTCCTGGCCCATGTCCTGGCCTGGACCTACGCC
TTCTATGACAACTGCCGCCGCCTTCGGTGTTTCCCACAACCCCCGAGACGGAACTGGTTT
TGGGGACACCAGGGCATGGTCAACCCCACAGAGGAGGGCATGAGAGTTCTGACTCAGCTG
GTGGCCACCTACCCCCAGGGCTTTAAGGTCTGGATGGGACCCATCTCCCCCCTCCTCAGT
TTGTGCCACCCCGACATCATCCGGTCTGTCATCAACGCCTCAGCTGCCATTGCACCAAAG
GACAAGTTCTTCTACAGCTTCCTGGAGCCCTGGCTGGGGGATGGGCTCCTGCTGAGTGCT
GGTGACAAGTGGAGCCGCCACCGTCGGATGCTGACGCCTGCCTTCCATTTCAACATCCTG
AAGCCCTATATGAAGATTTTCAATGAGAGTGTGAACATCATGCACGCCAAGTGGCAGCTC
CTGGCCTCAGAGGGTAGTGCCTGTTTGGATATGTTTGAGCACATCAGCCTCATGACCTTG
GACAGTCTACAGAAATGTGTCTTCAGCTTTGACAGCCATTGTCAGGAGAAACCCAGTGAA
TATATTGCCGCCATCTTGGAGCTCAGTGCCCTTGTATCAAAAAGACACCATGAGATCCTC
CTGCATATTGACTTCCTGTATTATCTCACCCCTGATGGGCAGCGTTTCCGCAGGGCCTGC
CGCCTGGTGCACGACTTCACAGATGCCGTCATCCAGGAGCGGCGCCGCACTCTCCCTAGC
CAGGGTGTTGATGACTTCCTCCAAGCCAAGGCCAAATCCAAGACTTTGGACTTCATTGAT
GTACTCCTGCTGAGCAAGGATGAAGACGGGAAGAAGTTATCTGATGAGGACATAAGAGCA
GAAGCTGACACCTTTATGTTTGAGGGCCATGACACCACGGCCAGTGGTCTCTCCTGGGTC
CTGTACCACCTTGCAAAGCACCCAGAATACCAGGAGCGCTGCCGGCAGGAGGTGCAAGAA
CTTCTGAAGGACCGTGAGCCTAAAGAGATTGAATGGGACGACCTGGCCCATTTGCCCTTC
CTGACCATGTGCATGAAGGAGAGCCTGCGGCTGCATCCCCCAGTCCCGGTCATCTCCCGC
CATGTCACCCAGGACATTGTGCTCCCAGACGGCCGGGTCATCCCCAAAGGCATTATCTGC
CTCATCAGTGTTTTCGGAACCCATCACAACCCAGCTATGTGGCCGGACCCTGAGGTCTAC
GACCCCTTTCGCTTTGACCCAGAGAACATCAAGGAGAGGTCACCTCTGGCTTTTATTCCC
TTCTCGGCAGGGCCCAGGAACTGCATCGGGCAGACGTTCGCGATGGCGGAGATGAAGGTG
GTCCTGGCGCTCACGCTGCTGCGCTTCCGCGTCCTGCCTGACCACACCGAGCCCCGCAGG
AAGCCGGAGCTGGTCCTGCGCGCAGAGGGCGGACTTTGGCTGCGGGTGGAGCCCCTGAGC
TGA
Enzyme 90 GenBank Gene ID AB015306 Link Image
Enzyme 90 GeneCard ID CYP4F2 Link Image
Enzyme 90 GenAtlas ID CYP4F2 Link Image
Enzyme 90 HGNC ID HGNC:2645 Link Image
Enzyme 90 Chromosome Location 1
Enzyme 90 Locus 19pter-p13.11
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. Kikuta Y, Kusunose E, Kondo T, Yamamoto S, Kinoshita H, Kusunose M: Cloning and expression of a novel form of leukotriene B4 omega-hydroxylase from human liver. FEBS Lett. 1994 Jul 4;348(1):70-4. [PubMed Link Image]
  2. Kikuta Y, Miyauchi Y, Kusunose E, Kusunose M: Expression and molecular cloning of human liver leukotriene B4 omega-hydroxylase (CYP4F2) gene. DNA Cell Biol. 1999 Sep;18(9):723-30. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Zhang X, Chen L, Hardwick JP: Promoter activity and regulation of the CYP4F2 leukotriene B(4) omega-hydroxylase gene by peroxisomal proliferators and retinoic acid in HepG2 cells. Arch Biochem Biophys. 2000 Jun 15;378(2):364-76. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 6302
Enzyme 91 Name Leukotriene-B(4) omega-hydroxylase 2
Enzyme 91 Synonyms
  1. CYPIVF3
  2. Cytochrome P450 4F3
  3. Cytochrome P450-LTB-omega
  4. Leukotriene-B(4) 20-monooxygenase 2
Enzyme 91 Gene Name CYP4F3
Enzyme 91 Protein Sequence >Leukotriene-B(4) omega-hydroxylase 2 
MPQLSLSSLGLWPMAASPWLLLLLVGASWLLARILAWTYTFYDNCCRLRCFPQPPKRNWF
LGHLGLIHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAPAAIVPK
DKVFYSFLKPWLGDGLLLSAGEKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQL
LASEGSARLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVTKRHQQIL
LYIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFID
VLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQE
LLKDREPKEIEWDDLAQLPFLTMCIKESLRLHPPVPAVSRCCTQDIVLPDGRVIPKGIIC
LISVFGTHHNPAVWPDPEVYDPFRFDPKNIKERSPLAFIPFSAGPRNCIGQAFAMAEMKV
VLGLTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS
Enzyme 91 Number of Residues 520
Enzyme 91 Molecular Weight 59846.1
Enzyme 91 Theoretical pI 7.68
Enzyme 91 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 91 General Function Involved in monooxygenase activity
Enzyme 91 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. This enzyme requires molecular oxygen and NADPH for the omega-hydroxylation of LTB4, a potent chemoattractant for polymorphonuclear leukocytes
Enzyme 91 Pathways
Enzyme 91 Reactions
  • (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H+ + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14- tetraenoate + NADP+ + H2O [RN:R03866]
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • 11-31
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 3123723 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID Q08477 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name CP4F3_HUMAN Link Image
Enzyme 91 PDB ID Not Available
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >1563 bp 
ATGCCACAGCTGAGCCTGTCCTCGCTGGGCCTTTGGCCAATGGCAGCATCCCCGTGGCTG
CTCCTGCTGCTGGTTGGGGCCTCCTGGCTCCTGGCCCGCATCCTGGCCTGGACCTATACC
TTCTATGACAACTGCTGCCGCCTCCGGTGTTTCCCGCAACCCCCGAAACGGAATTGGTTC
TTGGGTCACCTGGGCCTGATTCACAGCTCGGAGGAAGGTCTCCTATACACACAAAGCCTG
GCATGCACCTTCGGTGATATGTGCTGCTGGTGGGTGGGGCCCTGGCACGCAATCGTCCGC
ATCTTCCACCCCACCTACATCAAGCCTGTGCTCTTTGCTCCAGCTGCCATTGTACCAAAG
GACAAGGTCTTCTACAGCTTCCTGAAGCCCTGGCTGGGGGATGGGCTCCTGCTGAGTGCT
GGTGAAAAGTGGAGCCGCCACCGTCGGATGCTGACGCCTGCCTTCCATTTCAACATCCTG
AAGCCCTATATGAAGATTTTCAATGAGAGTGTGAACATCATGCATGCCAAGTGGCAGCTC
CTGGCCTCAGAGGGTAGTGCCCGTCTGGACATGTTTGAGCACATCAGCCTCATGACCTTG
GACAGTCTGCAGAAATGTGTCTTCAGCTTTGACAGCCATTGCCAGGAGAAGCCCAGTGAA
TATATTGCCGCCATCTTGGAGCTCAGTGCCCTTGTGACAAAAAGACACCAGCAGATCCTC
CTGTACATAGACTTCCTGTATTATCTCACCCCTGATGGGCAGCGTTTCCGCAGGGCCTGC
CGCCTGGTGCACGACTTCACAGATGACGTCATCCAGGAGCGGCGCCGCACCCTCCCTAGC
CAGGGTGTTGATGACTTCCTCCAAGCCAAGGCCAAATCCAAGACTTTGGACTTCATTGAT
GTACTCCTGCTGAGCAAGGATGAAGATGGGAAGAAGTTGTCCGATGAGGACATAAGAGCA
GAAGCTGACACCTTTATGTTTGAGGGCCATGACACCACAGCCAGTGGTCTCTCCTGGGTC
CTGTACCACCTTGCAAAGCACCCGGAATACCAGGAGCGCTGTCGGCAGGAGGTACAAGAG
CTTCTGAAGGACCGTGAGCCTAAAGAGATTGAATGGGACGACCTGGCCCAGCTGCCCTTC
CTGACCATGTGCATTAAGGAGAGCCTGAGGCTGCATCCCCCAGTCCCTGCCGTCTCTCGC
TGCTGCACCCAAGACATTGTGCTCCCAGACGGCCGGGTCATCCCCAAAGGCATTATCTGC
CTCATCAGTGTTTTTGGAACCCATCACAACCCAGCCGTGTGGCCGGACCCTGAGGTCTAT
GACCCCTTTCGCTTTGACCCAAAGAACATCAAGGAGAGGTCACCTCTGGCTTTTATTCCC
TTCTCAGCAGGGCCCAGGAACTGCATCGGGCAGGCGTTCGCGATGGCGGAGATGAAGGTG
GTCCTGGGGCTCACGCTGCTGGCCTTCCGCGTCCTGCCTGACCACACCGAGCCCCGCAGG
AAGCCGGAGCTGGTCCTGCGCGCAGAGGGCGGACTTTGGCTGCGGGTGGAGCCCCTGAGC
TGA
Enzyme 91 GenBank Gene ID AB002454 Link Image
Enzyme 91 GeneCard ID CYP4F3 Link Image
Enzyme 91 GenAtlas ID CYP4F3 Link Image
Enzyme 91 HGNC ID HGNC:2646 Link Image
Enzyme 91 Chromosome Location 1
Enzyme 91 Locus 19p13.2
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Kikuta Y, Kusunose E, Endo K, Yamamoto S, Sogawa K, Fujii-Kuriyama Y, Kusunose M: A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 omega-hydroxylase. J Biol Chem. 1993 May 5;268(13):9376-80. [PubMed Link Image]
  2. Kikuta Y, Kato M, Yamashita Y, Miyauchi Y, Tanaka K, Kamada N, Kusunose M: Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular cloning and chromosomal localization. DNA Cell Biol. 1998 Mar;17(3):221-30. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 6306
Enzyme 92 Name Cytochrome P450 3A4
Enzyme 92 Synonyms
  1. Albendazole monooxygenase
  2. Albendazole sulfoxidase
  3. CYPIIIA3
  4. CYPIIIA4
  5. Cytochrome P450 3A3
  6. Cytochrome P450 HLp
  7. Cytochrome P450 NF-25
  8. Cytochrome P450-PCN1
  9. Nifedipine oxidase
  10. Quinine 3-monooxygenase
  11. Taurochenodeoxycholate 6-alpha-hydroxylase
Enzyme 92 Gene Name CYP3A4
Enzyme 92 Protein Sequence >Cytochrome P450 3A4 
MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMF
DMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISI
AEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSI
IFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVV
NETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
Enzyme 92 Number of Residues 503
Enzyme 92 Molecular Weight 57342.7
Enzyme 92 Theoretical pI 8.25
Enzyme 92 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 92 General Function Involved in monooxygenase activity
Enzyme 92 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4- hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. The enzyme also hydroxylates etoposide
Enzyme 92 Pathways Not Available
Enzyme 92 Reactions
  • (1) taurochenodeoxycholate + NADPH + H+ + O2 = taurohyocholate + NADP+ + H2O [RN:R07205]
  • (2) lithocholate + NADPH + H+ + O2 = hyodeoxycholate + NADP+ + H2O [RN:R07206]
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • 2-22
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 6470135 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID P08684 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name CP3A4_HUMAN Link Image
Enzyme 92 PDB ID 1TQN Link Image
Enzyme 92 PDB File Show
Enzyme 92 3D Structure
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >1512 bp 
ATGGCTCTCATCCCAGACTTGGCCATGGAAACCCGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGAACTCATTCACATGGACTTTTTAAGAAGCTTGGAATTCCAGGG
CCCACACCTCTGCCTTTTTTGGGAAATATTTTGTCCTACCATAAGGGCTTTTGTATGTTT
GACATGGAATGTCATAAAAAGTATGGAAAAGTGTGGGGCTTTTATGATGGTCAACAGCCT
GTGCTGGCTATCACAGATCCTGACATGATCAAAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAACCGGAGGCCTTTTGGTCCAGTGGGATTTATGAAAAGTGCCATCTCTATA
GCTGAGGATGAAGAATGGAAGAGATTACGATCATTGCTGTCTCCAACCTTCACCAGTGGA
AAACTCAAGGAGATGGTCCCTATCATTGCCCAGTATGGAGATGTGTTGGTGAGAAATCTG
AGGCGGGAAGCAGAGACAGGCAAGCCTGTCACCTTGAAAGACGTCTTTGGGGCCTACAGC
ATGGATGTGATCACTAGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAAAACACCAAGAAGCTTTTAAGATTTGATTTTTTGGATCCATTCTTT
CTCTCAATAACAGTCTTTCCATTCCTCATCCCAATTCTTGAAGTATTAAATATCTGTGTG
TTTCCAAGAGAAGTTACAAATTTTTTAAGAAAATCTGTAAAAAGGATGAAAGAAAGTCGC
CTCGAAGATACACAAAAGCACCGAGTGGATTTCCTTCAGCTGATGATTGACTCTCAGAAT
TCAAAAGAAACTGAGTCCCACAAAGCTCTGTCCGATCTGGAGCTCGTGGCCCAATCAATT
ATCTTTATTTTTGCTGGCTGTGAAACCACGAGCAGTGTTCTCTCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAAATTGATGCAGTTTTACCC
AATAAGGCACCACCCACCTATGATACTGTGCTACAGATGGAGTATCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAATTGCTATGAGACTTGAGAGGGTCTGCAAAAAAGAT
GTTGAGATCAATGGGATGTTCATTCCCAAAGGGGTGGTGGTGATGATTCCAAGCTATGCT
CTTCACCGTGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCCTCCCTGAAAGATTCAGC
AAGAAGAACAAGGACAACATAGATCCTTACATATACACACCCTTTGGAAGTGGACCCAGA
AACTGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTT
CAGAACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCCTGAAATTAAGCTTAGGA
GGACTTCTTCAACCAGAAAAACCCGTTGTTCTAAAGGTTGAGTCAAGGGATGGCACCGTA
AGTGGAGCCTGA
Enzyme 92 GenBank Gene ID AF182273 Link Image
Enzyme 92 GeneCard ID CYP3A4 Link Image
Enzyme 92 GenAtlas ID CYP3A4 Link Image
Enzyme 92 HGNC ID HGNC:2637 Link Image
Enzyme 92 Chromosome Location 7
Enzyme 92 Locus 7q21.1
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Molowa DT, Schuetz EG, Wrighton SA, Watkins PB, Kremers P, Mendez-Picon G, Parker GA, Guzelian PS: Complete cDNA sequence of a cytochrome P-450 inducible by glucocorticoids in human liver. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5311-5. [PubMed Link Image]
  2. Gonzalez FJ, Schmid BJ, Umeno M, Mcbride OW, Hardwick JP, Meyer UA, Gelboin HV, Idle JR: Human P450PCN1: sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase. DNA. 1988 Mar;7(2):79-86. [PubMed Link Image]
  3. Beaune PH, Umbenhauer DR, Bork RW, Lloyd RS, Guengerich FP: Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8064-8. [PubMed Link Image]
  4. Spurr NK, Gough AC, Stevenson K, Wolf CR: The human cytochrome P450 CYP3 locus: assignment to chromosome 7q22-qter. Hum Genet. 1989 Jan;81(2):171-4. [PubMed Link Image]
  5. Bork RW, Muto T, Beaune PH, Srivastava PK, Lloyd RS, Guengerich FP: Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity. J Biol Chem. 1989 Jan 15;264(2):910-9. [PubMed Link Image]
  6. Chen Q, Wu J, Yu Y: [Establishment of transgenic cell line CHL-3A4 and its metabolic activation] Zhonghua Yu Fang Yi Xue Za Zhi. 1998 Sep;32(5):281-4. [PubMed Link Image]
  7. Gellner K, Eiselt R, Hustert E, Arnold H, Koch I, Haberl M, Deglmann CJ, Burk O, Buntefuss D, Escher S, Bishop C, Koebe HG, Brinkmann U, Klenk HP, Kleine K, Meyer UA, Wojnowski L: Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics. 2001 Mar;11(2):111-21. [PubMed Link Image]
  8. Hsieh KP, Lin YY, Cheng CL, Lai ML, Lin MS, Siest JP, Huang JD: Novel mutations of CYP3A4 in Chinese. Drug Metab Dispos. 2001 Mar;29(3):268-73. [PubMed Link Image]
  9. Komori M, Hashizume T, Ohi H, Miura T, Kitada M, Nagashima K, Kamataki T: Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization. J Biochem. 1988 Dec;104(6):912-6. [PubMed Link Image]
  10. Watkins PB, Wrighton SA, Maurel P, Schuetz EG, Mendez-Picon G, Parker GA, Guzelian PS: Identification of an inducible form of cytochrome P-450 in human liver. Proc Natl Acad Sci U S A. 1985 Sep;82(18):6310-4. [PubMed Link Image]
  11. Zhang H, Coville PF, Walker RJ, Miners JO, Birkett DJ, Wanwimolruk S: Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine. Br J Clin Pharmacol. 1997 Mar;43(3):245-52. [PubMed Link Image]
  12. Zhao XJ, Kawashiro T, Ishizaki T: Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways. Drug Metab Dispos. 1998 Feb;26(2):188-91. [PubMed Link Image]
  13. Pabarcus MK, Hoe N, Sadeghi S, Patterson C, Wiertz E, Correia MA: CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases. Arch Biochem Biophys. 2009 Mar 1;483(1):66-74. Epub 2008 Dec 10. [PubMed Link Image]
  14. Yano JK, Wester MR, Schoch GA, Griffin KJ, Stout CD, Johnson EF: The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem. 2004 Sep 10;279(37):38091-4. Epub 2004 Jul 16. [PubMed Link Image]
  15. Williams PA, Cosme J, Vinkovic DM, Ward A, Angove HC, Day PJ, Vonrhein C, Tickle IJ, Jhoti H: Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Science. 2004 Jul 30;305(5684):683-6. Epub 2004 Jul 15. [PubMed Link Image]
  16. Sata F, Sapone A, Elizondo G, Stocker P, Miller VP, Zheng W, Raunio H, Crespi CL, Gonzalez FJ: CYP3A4 allelic variants with amino acid substitutions in exons 7 and 12: evidence for an allelic variant with altered catalytic activity. Clin Pharmacol Ther. 2000 Jan;67(1):48-56. [PubMed Link Image]
  17. Dai D, Tang J, Rose R, Hodgson E, Bienstock RJ, Mohrenweiser HW, Goldstein JA: Identification of variants of CYP3A4 and characterization of their abilities to metabolize testosterone and chlorpyrifos. J Pharmacol Exp Ther. 2001 Dec;299(3):825-31. [PubMed Link Image]
  18. Eiselt R, Domanski TL, Zibat A, Mueller R, Presecan-Siedel E, Hustert E, Zanger UM, Brockmoller J, Klenk HP, Meyer UA, Khan KK, He YA, Halpert JR, Wojnowski L: Identification and functional characterization of eight CYP3A4 protein variants. Pharmacogenetics. 2001 Jul;11(5):447-58. [PubMed Link Image]
  19. Lamba JK, Lin YS, Thummel K, Daly A, Watkins PB, Strom S, Zhang J, Schuetz EG: Common allelic variants of cytochrome P4503A4 and their prevalence in different populations. Pharmacogenetics. 2002 Mar;12(2):121-32. [PubMed Link Image]
  20. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 6324
Enzyme 93 Name Cytochrome P450 2C9
Enzyme 93 Synonyms
  1. (R)-limonene 6-monooxygenase
  2. (S)-limonene 6-monooxygenase
  3. (S)-limonene 7-monooxygenase
  4. CYPIIC9
  5. Cytochrome P-450MP
  6. Cytochrome P450 MP-4
  7. Cytochrome P450 MP-8
  8. Cytochrome P450 PB-1
  9. S-mephenytoin 4-hydroxylase
Enzyme 93 Gene Name CYP2C9
Enzyme 93 Protein Sequence >Cytochrome P450 2C9 
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKV
YGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFM
KSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYID
LLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFK
KSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVP
PFYQLCFIPV
Enzyme 93 Number of Residues 490
Enzyme 93 Molecular Weight 55627.4
Enzyme 93 Theoretical pI 7.99
Enzyme 93 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 93 General Function Involved in monooxygenase activity
Enzyme 93 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan
Enzyme 93 Pathways
Enzyme 93 Reactions
  • (R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O [RN:R06119]
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • None
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 32891803 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID P11712 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name CP2C9_HUMAN Link Image
Enzyme 93 PDB ID 1R9O Link Image
Enzyme 93 PDB File Show
Enzyme 93 3D Structure
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >1473 bp 
ATGGATTCTCTTGTGGTCCTTGTGCTCTGTCTCTCATGTTTGCTTCTCCTTTCACTCTGG
AGACAGAGCTCTGGGAGAGGAAAACTCCCTCCTGGCCCCACTCCTCTCCCAGTGATTGGA
AATATCCTACAGATAGGTATTAAGGACATCAGCAAATCCTTAACCAATCTCTCAAAGGTC
TATGGCCCTGTGTTCACTCTGTATTTTGGCCTGAAACCCATAGTGGTGCTGCATGGATAT
GAAGCAGTGAAGGAAGCCCTGATTGATCTTGGAGAGGAGTTTTCTGGAAGAGGCATTTTC
CCACTGGCTGAAAGAGCTAACAGAGGATTTGGAATTGTTTTCAGCAATGGAAAGAAATGG
AAGGAGATCCGGCGTTTCTCCCTCATGACGCTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCCTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
ATTATTTTCCATAAACGTTTTGATTATAAAGATCAGCAATTTCTTAACTTAATGGAAAAG
TTGAATGAAAACATCAAGATTTTGAGCAGCCCCTGGATCCAGATCTGCAATAATTTTTCT
CCTATCATTGATTACTTCCCGGGAACTCACAACAAATTACTTAAAAACGTTGCTTTTATG
AAAAGTTATATTTTGGAAAAAGTAAAAGAACACCAAGAATCAATGGACATGAACAACCCT
CAGGACTTTATTGATTGCTTCCTGATGAAAATGGAGAAGGAAAAGCACAACCAACCATCT
GAATTTACTATTGAAAGCTTGGAAAACACTGCAGTTGACTTGTTTGGAGCTGGGACAGAG
ACGACAAGCACAACCCTGAGATATGCTCTCCTTCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGAACGTGTGATTGGCAGAAACCGGAGCCCCTGCATGCAA
GACAGGAGCCACATGCCCTACACAGATGCTGTGGTGCACGAGGTCCAGAGATACATTGAC
CTTCTCCCCACCAGCCTGCCCCATGCAGTGACCTGTGACATTAAATTCAGAAACTATCTC
ATTCCCAAGGGCACAACCATATTAATTTCCCTGACTTCTGTGCTACATGACAACAAAGAA
TTTCCCAACCCAGAGATGTTTGACCCTCATCACTTTCTGGATGAAGGTGGCAATTTTAAG
AAAAGTAAATACTTCATGCCTTTCTCAGCAGGAAAACGGATTTGTGTGGGAGAAGCCCTG
GCCGGCATGGAGCTGTTTTTATTCCTGACCTCCATTTTACAGAACTTTAACCTGAAATCT
CTGGTTGACCCAAAGAACCTTGACACCACTCCAGTTGTCAATGGATTTGCCTCTGTGCCG
CCCTTCTACCAGCTGTGCTTCATTCCTGTCTGA
Enzyme 93 GenBank Gene ID AY341248 Link Image
Enzyme 93 GeneCard ID CYP2C9 Link Image
Enzyme 93 GenAtlas ID CYP2C9 Link Image
Enzyme 93 HGNC ID HGNC:2623 Link Image
Enzyme 93 Chromosome Location 1
Enzyme 93 Locus 10q24
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Meehan RR, Gosden JR, Rout D, Hastie ND, Friedberg T, Adesnik M, Buckland R, van Heyningen V, Fletcher J, Spurr NK, et al.: Human cytochrome P-450 PB-1: a multigene family involved in mephenytoin and steroid oxidations that maps to chromosome 10. Am J Hum Genet. 1988 Jan;42(1):26-37. [PubMed Link Image]
  2. Kimura S, Pastewka J, Gelboin HV, Gonzalez FJ: cDNA and amino acid sequences of two members of the human P450IIC gene subfamily. Nucleic Acids Res. 1987 Dec 10;15(23):10053-4. [PubMed Link Image]
  3. Yasumori T, Kawano S, Nagata K, Shimada M, Yamazoe Y, Kato R: Nucleotide sequence of a human liver cytochrome P-450 related to the rat male specific form. J Biochem (Tokyo). 1987 Nov;102(5):1075-82. [PubMed Link Image]
  4. Umbenhauer DR, Martin MV, Lloyd RS, Guengerich FP: Cloning and sequence determination of a complementary DNA related to human liver microsomal cytochrome P-450 S-mephenytoin 4-hydroxylase. Biochemistry. 1987 Feb 24;26(4):1094-9. [PubMed Link Image]
  5. Ged C, Umbenhauer DR, Bellew TM, Bork RW, Srivastava PK, Shinriki N, Lloyd RS, Guengerich FP: Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase. Biochemistry. 1988 Sep 6;27(18):6929-40. [PubMed Link Image]
  6. Ohgiya S, Komori M, Ohi H, Shiramatsu K, Shinriki N, Kamataki T: Six-base deletion occurring in messages of human cytochrome P-450 in the CYP2C subfamily results in reduction of tolbutamide hydroxylase activity. Biochem Int. 1992 Sep;27(6):1073-81. [PubMed Link Image]
  7. Shimada T, Misono KS, Guengerich FP: Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction. J Biol Chem. 1986 Jan 15;261(2):909-21. [PubMed Link Image]
  8. Komori M, Hashizume T, Ohi H, Miura T, Kitada M, Nagashima K, Kamataki T: Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization. J Biochem. 1988 Dec;104(6):912-6. [PubMed Link Image]
  9. Srivastava PK, Yun CH, Beaune PH, Ged C, Guengerich FP: Separation of human liver microsomal tolbutamide hydroxylase and (S)-mephenytoin 4'-hydroxylase cytochrome P-450 enzymes. Mol Pharmacol. 1991 Jul;40(1):69-79. [PubMed Link Image]
  10. Haining RL, Hunter AP, Veronese ME, Trager WF, Rettie AE: Allelic variants of human cytochrome P450 2C9: baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity, and prochiral selectivity of the wild-type and I359L mutant forms. Arch Biochem Biophys. 1996 Sep 15;333(2):447-58. [PubMed Link Image]
  11. Sandhu P, Baba T, Guengerich FP: Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity. Arch Biochem Biophys. 1993 Nov 1;306(2):443-50. [PubMed Link Image]
  12. Miyazawa M, Shindo M, Shimada T: Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes. Drug Metab Dispos. 2002 May;30(5):602-7. [PubMed Link Image]
  13. Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H: Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. [PubMed Link Image]
  14. Stubbins MJ, Harries LW, Smith G, Tarbit MH, Wolf CR: Genetic analysis of the human cytochrome P450 CYP2C9 locus. Pharmacogenetics. 1996 Oct;6(5):429-39. [PubMed Link Image]
  15. Bhasker CR, Miners JO, Coulter S, Birkett DJ: Allelic and functional variability of cytochrome P4502C9. Pharmacogenetics. 1997 Feb;7(1):51-8. [PubMed Link Image]
  16. Imai J, Ieiri I, Mamiya K, Miyahara S, Furuumi H, Nanba E, Yamane M, Fukumaki Y, Ninomiya H, Tashiro N, Otsubo K, Higuchi S: Polymorphism of the cytochrome P450 (CYP) 2C9 gene in Japanese epileptic patients: genetic analysis of the CYP2C9 locus. Pharmacogenetics. 2000 Feb;10(1):85-9. [PubMed Link Image]
  17. Dickmann LJ, Rettie AE, Kneller MB, Kim RB, Wood AJ, Stein CM, Wilkinson GR, Schwarz UI: Identification and functional characterization of a new CYP2C9 variant (CYP2C9*5) expressed among African Americans. Mol Pharmacol. 2001 Aug;60(2):382-7. [PubMed Link Image]
  18. Higashi MK, Veenstra DL, Kondo LM, Wittkowsky AK, Srinouanprachanh SL, Farin FM, Rettie AE: Association between CYP2C9 genetic variants and anticoagulation-related outcomes during warfarin therapy. JAMA. 2002 Apr 3;287(13):1690-8. [PubMed Link Image]
  19. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 6325
Enzyme 94 Name Sterol 26-hydroxylase, mitochondrial
Enzyme 94 Synonyms
  1. 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase
  2. Cytochrome P-450C27/25
  3. Cytochrome P450 27
  4. Sterol 27-hydroxylase
  5. Vitamin D(3) 25-hydroxylase
Enzyme 94 Gene Name CYP27A1
Enzyme 94 Protein Sequence >Sterol 26-hydroxylase, mitochondrial 
MAALGCARLRWALRGAGRGLCPHGARAKAAIPAALPSDKATGAPGAGPGVRRRQRSLEEI
PRLGQLRFFFQLFVQGYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQ
EGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAALYTDAFNE
VIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTF
VRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAA
GPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEA
LHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPK
NTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSVPFGYGVRACLGRR
IAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQFLQRQC
Enzyme 94 Number of Residues 531
Enzyme 94 Molecular Weight 60234.3
Enzyme 94 Theoretical pI 9.16
Enzyme 94 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 94 General Function Involved in monooxygenase activity
Enzyme 94 Specific Function Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta- cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3- 25-hydroxylase activity
Enzyme 94 Pathways
Enzyme 94 Reactions
  • 5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ + H2O [RN:R04807]
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • None
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein Not Available
Enzyme 94 UniProtKB/Swiss-Prot ID Q02318 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name CP27A_HUMAN Link Image
Enzyme 94 PDB ID Not Available
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >1596 bp 
ATGGCTGCGCTGGGCTGCGCGAGGCTGAGGTGGGCGCTGCGAGGGGCCGGCCGTGGCCTC
TGCCCCCACGGGGCCAGAGCCAAGGCCGCGATCCCTGCCGCCCTCCCCTCGGACAAGGCC
ACCGGAGCTCCCGGAGCCGGGCCTGGTGTCCGGCGGCGGCAACGGAGCTTAGAGGAGATT
CCACGTCTAGGACAGCTGCGCTTCTTCTTTCAGCTGTTCGTTCAAGGCTATGCCCTGCAA
CTGCACCAGTTACAGGTGCTTTACAAGGCCAAGTACGGTCCAATGTGGATGTCCTACTTA
GGGCCTCAGATGCACGTGAACCTGGCCAGTGCCCCGCTCTTGGAGCAAGTGATGCGGCAA
GAGGGAAAGTACCCAGTACGGAACGACATGGAGCTATGGAAGGAGCACCGGGACCAGCAC
GACCTGACCTATGGGCCGTTCACCACGGAAGGACACCACTGGTACCAGCTGCGCCAGGCT
CTGAACCAGCGGTTGCTGAAGCCAGCGGAAGCAGCGCTCTATACGGATGCTTTCAATGAG
GTGATTGATGACTTTATGACTCGACTGGACCAGCTGCGGGCAGAGAGTGCTTCGGGGAAC
CAGGTGTCGGACATGGCTCAACTCTTCTACTACTTTGCCTTGGAAGCTATTTGCTACATC
CTGTTCGAGAAACGCATTGGCTGCCTGCAGCGATCCATCCCCGAGGACACCGTGACCTTC
GTCAGATCCATCGGGTTAATGTTCCAGAACTCACTCTATGCCACCTTCCTCCCCAAGTGG
ACTCGCCCCGTGCTGCCTTTCTGGAAGCGATACCTGGATGGTTGGAATGCCATCTTTTCC
TTTGGGAAGAAGCTGATTGATGAGAAGCTCGAAGATATGGAGGCCCAACTGCAGGCAGCA
GGGCCAGATGGCATCCAGGTGTCTGGCTACCTGCACTTCTTACTGGCCAGTGGACAGCTC
AGTCCTCGGGAGGCCATGGGCAGCCTGCCTGAGCTGCTCATGGCTGGAGTGGACACGACA
TCCAACACGCTGACATGGGCCCTGTACCACCTCTCAAAGGACCCTGAGATCCAGGAGGCC
TTGCACGAGGAAGTGGTGGGTGTGGTGCCAGCCGGGCAAGTGCCCCAGCACAAGGACTTT
GCCCACATGCCGTTGCTCAAAGCTGTGCTTAAGGAGACTCTGCGTCTCTACCCTGTGGTC
CCCACAAACTCCCGGATCATAGAAAAGGAAATTGAAGTTGATGGCTTCCTCTTCCCCAAG
AACACCCAGTTTGTGTTCTGCCACTATGTGGTGTCCCGGGACCCCACTGCCTTCTCTGAG
CCTGAAAGCTTCCAGCCCCACCGCTGGCTGAGAAACAGCCAGCCTGCTACCCCCAGGATC
CAGCACCCATTTGGCTCTGTGCCCTTTGGCTATGGGGTCCGGGCCTGCCTGGGCCGCAGG
ATTGCAGAGCTGGAGATGCAGCTACTCCTCGCAAGGCTGATCCAGAAGTACAAGGTGGTC
CTGGCCCCGGAGACGGGGGAGTTGAAGAGTGTGGCCCGCATTGTCCTGGTTCCCAATAAG
AAAGTGGGCCTGCAGTTCCTGCAGAGACAGTGCTGA
Enzyme 94 GenBank Gene ID M62401 Link Image
Enzyme 94 GeneCard ID CYP27A1 Link Image
Enzyme 94 GenAtlas ID CYP27A1 Link Image
Enzyme 94 HGNC ID HGNC:2605 Link Image
Enzyme 94 Chromosome Location 2
Enzyme 94 Locus 2q33-qter
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Cali JJ, Russell DW: Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. J Biol Chem. 1991 Apr 25;266(12):7774-8. [PubMed Link Image]
  2. Guo YD, Strugnell S, Back DW, Jones G: Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8668-72. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Leitersdorf E, Reshef A, Meiner V, Levitzki R, Schwartz SP, Dann EJ, Berkman N, Cali JJ, Klapholz L, Berginer VM: Frameshift and splice-junction mutations in the sterol 27-hydroxylase gene cause cerebrotendinous xanthomatosis in Jews or Moroccan origin. J Clin Invest. 1993 Jun;91(6):2488-96. [PubMed Link Image]
  6. Cali JJ, Hsieh CL, Francke U, Russell DW: Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis. J Biol Chem. 1991 Apr 25;266(12):7779-83. [PubMed Link Image]
  7. Kim KS, Kubota S, Kuriyama M, Fujiyama J, Bjorkhem I, Eggertsen G, Seyama Y: Identification of new mutations in sterol 27-hydroxylase gene in Japanese patients with cerebrotendinous xanthomatosis (CTX). J Lipid Res. 1994 Jun;35(6):1031-9. [PubMed Link Image]
  8. Chen W, Kubota S, Kim KS, Cheng J, Kuriyama M, Eggertsen G, Bjorkhem I, Seyama Y: Novel homozygous and compound heterozygous mutations of sterol 27-hydroxylase gene (CYP27) cause cerebrotendinous xanthomatosis in three Japanese patients from two unrelated families. J Lipid Res. 1997 May;38(5):870-9. [PubMed Link Image]
  9. Chen W, Kubota S, Ujike H, Ishihara T, Seyama Y: A novel Arg362Ser mutation in the sterol 27-hydroxylase gene (CYP27): its effects on pre-mRNA splicing and enzyme activity. Biochemistry. 1998 Oct 27;37(43):15050-6. [PubMed Link Image]
  10. Lamon-Fava S, Schaefer EJ, Garuti R, Salen G, Calandra S: Two novel mutations in the sterol 27-hydroxylase gene causing cerebrotendinous xanthomatosis. Clin Genet. 2002 Mar;61(3):185-91. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 6326
Enzyme 95 Name Cytochrome P450 2C19
Enzyme 95 Synonyms
  1. (R)-limonene 6-monooxygenase
  2. (S)-limonene 6-monooxygenase
  3. (S)-limonene 7-monooxygenase
  4. CYPIIC17
  5. CYPIIC19
  6. Cytochrome P450-11A
  7. Cytochrome P450-254C
  8. Mephenytoin 4-hydroxylase
Enzyme 95 Gene Name CYP2C19
Enzyme 95 Protein Sequence >Cytochrome P450 2C19 
MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKI
YGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFM
ESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYID
LIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFK
KSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVP
PFYQLCFIPV
Enzyme 95 Number of Residues 490
Enzyme 95 Molecular Weight 55930.5
Enzyme 95 Theoretical pI 7.42
Enzyme 95 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 95 General Function Involved in monooxygenase activity
Enzyme 95 Specific Function Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine
Enzyme 95 Pathways
Enzyme 95 Reactions
  • (R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O [RN:R06119]
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 181344 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID P33261 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name CP2CJ_HUMAN Link Image
Enzyme 95 PDB ID 1R9O Link Image
Enzyme 95 PDB File Show
Enzyme 95 3D Structure
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >1473 bp 
ATGGATCCTTTTGTGGTCCTTGTGCTCTGTCTCTCATGTTTGCTTCTCCTTTCAATCTGG
AGACAGAGCTCTGGGAGAGGAAAACTCCCTCCTGGCCCCACTCCTCTCCCAGTGATTGGA
AATATCCTACAGATAGATATTAAGGATGTCAGCAAATCCTTAACCAATCTCTCAAAAATC
TATGGCCCTGTGTTCACTCTGTATTTTGGCCTGGAACGCATGGTGGTGCTGCATGGATAT
GAAGTGGTGAAGGAAGCCCTGATTGATCTTGGAGAGGAGTTTTCTGGAAGAGGCCATTTC
CCACTGGCTGAAAGAGCTAACAGAGGATTTGGAATCGTTTTCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCATGACGCTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
ATTATTTTCCAGAAACGTTTCGATTATAAAGATCAGCAATTTCTTAACTTGATGGAAAAA
TTGAATGAAAACATCAGGATTGTAAGCACCCCCTGGATCCAGATATGCAATAATTTTCCC
ACTATCATTGATTATTTCCCGGGAACCCATAACAAATTACTTAAAAACCTTGCTTTTATG
GAAAGTGATATTTTGGAGAAAGTAAAAGAACACCAAGAATCGATGGACATCAACAACCCT
CGGGACTTTATTGATTGCTTCCTGATCAAAATGGAGAAGGAAAAGCAAAACCAACAGTCT
GAATTCACTATTGAAAACTTGGTAATCACTGCAGCTGACTTACTTGGAGCTGGGACAGAG
ACAACAAGCACAACCCTGAGATATGCTCTCCTTCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGAACGTGTCATTGGCAGAAACCGGAGCCCCTGCATGCAG
GACAGGGGCCACATGCCCTACACAGATGCTGTGGTGCACGAGGTCCAGAGATACATCGAC
CTCATCCCCACCAGCCTGCCCCATGCAGTGACCTGTGACGTTAAATTCAGAAACTACCTC
ATTCCCAAGGGCACAACCATATTAACTTCCCTCACTTCTGTGCTACATGACAACAAAGAA
TTTCCCAACCCAGAGATGTTTGACCCTCGTCACTTTCTGGATGAAGGTGGAAATTTTAAG
AAAAGTAACTACTTCATGCCTTTCTCAGCAGGAAAACGGATTTGTGTGGGAGAGGGCCTG
GCCCGCATGGAGCTGTTTTTATTCCTGACCTTCATTTTACAGAACTTTAACCTGAAATCT
CTGATTGACCCAAAGGACCTTGACACAACTCCTGTTGTCAATGGATTTGCTTCTGTCCCG
CCCTTCTATCAGCTGTGCTTCATTCCTGTCTGA
Enzyme 95 GenBank Gene ID M61854 Link Image
Enzyme 95 GeneCard ID CYP2C19 Link Image
Enzyme 95 GenAtlas ID CYP2C19 Link Image
Enzyme 95 HGNC ID HGNC:2621 Link Image
Enzyme 95 Chromosome Location 1
Enzyme 95 Locus 10q24.1-q24.3
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed Link Image]
  2. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome PH50IIC subfamily. Biochemistry. 1993 Feb 9;32(5):1390. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Wrighton SA, Stevens JC, Becker GW, VandenBranden M: Isolation and characterization of human liver cytochrome P450 2C19: correlation between 2C19 and S-mephenytoin 4'-hydroxylation. Arch Biochem Biophys. 1993 Oct;306(1):240-5. [PubMed Link Image]
  5. Miyazawa M, Shindo M, Shimada T: Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes. Drug Metab Dispos. 2002 May;30(5):602-7. [PubMed Link Image]
  6. de Morais SM, Wilkinson GR, Blaisdell J, Nakamura K, Meyer UA, Goldstein JA: The major genetic defect responsible for the polymorphism of S-mephenytoin metabolism in humans. J Biol Chem. 1994 Jun 3;269(22):15419-22. [PubMed Link Image]
  7. De Morais SM, Wilkinson GR, Blaisdell J, Meyer UA, Nakamura K, Goldstein JA: Identification of a new genetic defect responsible for the polymorphism of (S)-mephenytoin metabolism in Japanese. Mol Pharmacol. 1994 Oct;46(4):594-8. [PubMed Link Image]
  8. Xiao ZS, Goldstein JA, Xie HG, Blaisdell J, Wang W, Jiang CH, Yan FX, He N, Huang SL, Xu ZH, Zhou HH: Differences in the incidence of the CYP2C19 polymorphism affecting the S-mephenytoin phenotype in Chinese Han and Bai populations and identification of a new rare CYP2C19 mutant allele. J Pharmacol Exp Ther. 1997 Apr;281(1):604-9. [PubMed Link Image]
  9. Ibeanu GC, Goldstein JA, Meyer U, Benhamou S, Bouchardy C, Dayer P, Ghanayem BI, Blaisdell J: Identification of new human CYP2C19 alleles (CYP2C19*6 and CYP2C19*2B) in a Caucasian poor metabolizer of mephenytoin. J Pharmacol Exp Ther. 1998 Sep;286(3):1490-5. [PubMed Link Image]
  10. Ibeanu GC, Blaisdell J, Ghanayem BI, Beyeler C, Benhamou S, Bouchardy C, Wilkinson GR, Dayer P, Daly AK, Goldstein JA: An additional defective allele, CYP2C19*5, contributes to the S-mephenytoin poor metabolizer phenotype in Caucasians. Pharmacogenetics. 1998 Apr;8(2):129-35. [PubMed Link Image]
  11. Ibeanu GC, Blaisdell J, Ferguson RJ, Ghanayem BI, Brosen K, Benhamou S, Bouchardy C, Wilkinson GR, Dayer P, Goldstein JA: A novel transversion in the intron 5 donor splice junction of CYP2C19 and a sequence polymorphism in exon 3 contribute to the poor metabolizer phenotype for the anticonvulsant drug S-mephenytoin. J Pharmacol Exp Ther. 1999 Aug;290(2):635-40. [PubMed Link Image]
  12. Blaisdell J, Mohrenweiser H, Jackson J, Ferguson S, Coulter S, Chanas B, Xi T, Ghanayem B, Goldstein JA: Identification and functional characterization of new potentially defective alleles of human CYP2C19. Pharmacogenetics. 2002 Dec;12(9):703-11. [PubMed Link Image]
  13. Morita J, Kobayashi K, Wanibuchi A, Kimura M, Irie S, Ishizaki T, Chiba K: A novel single nucleotide polymorphism (SNP) of the CYP2C19 gene in a Japanese subject with lowered capacity of mephobarbital 4'-hydroxylation. Drug Metab Pharmacokinet. 2004 Jun;19(3):236-8. [PubMed Link Image]
  14. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  15. Fukushima-Uesaka H, Saito Y, Maekawa K, Ozawa S, Hasegawa R, Kajio H, Kuzuya N, Yasuda K, Kawamoto M, Kamatani N, Suzuki K, Yanagawa T, Tohkin M, Sawada J: Genetic variations and haplotypes of CYP2C19 in a Japanese population. Drug Metab Pharmacokinet. 2005 Aug;20(4):300-7. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 6328
Enzyme 96 Name 6-phosphogluconate dehydrogenase, decarboxylating
Enzyme 96 Synonyms Not Available
Enzyme 96 Gene Name PGD
Enzyme 96 Protein Sequence >6-phosphogluconate dehydrogenase, decarboxylating 
MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKE
MVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKG
ILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAG
HFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANIL
KFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQA
SKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIAL
MWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPM
PCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSS
YNA
Enzyme 96 Number of Residues 483
Enzyme 96 Molecular Weight 53139.6
Enzyme 96 Theoretical pI 7.25
Enzyme 96 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphogluconate dehydrogenase (decarboxylating) activity
  • phosphogluconate dehydrogenase (decarboxylating) activity
  • phosphogluconate dehydrogenase (decarboxylating) activity
  • phosphogluconate dehydrogenase (decarboxylating) activity
  • phosphogluconate dehydrogenase (decarboxylating) activity
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • oxidation reduction
  • pentose-phosphate shunt
  • small molecule metabolic process
Component
—
Enzyme 96 General Function Involved in oxidoreductase activity
Enzyme 96 Specific Function Catalyzes the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH
Enzyme 96 Pathways
Enzyme 96 Reactions
  • 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH [RN:R01528]
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 12653201 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID P52209 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name 6PGD_HUMAN Link Image
Enzyme 96 PDB ID 2PGD Link Image
Enzyme 96 PDB File Show
Enzyme 96 3D Structure
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >1452 bp 
ATGGCCCAAGCTGACATCGCGCTGATCGGATTGGCCGTCATGGGCCAGAACTTAATTCTG
AACATGAATGACCACGGCTTTGTGGTCTGTGCTTTTAATAGGACTGTCTCCAAAGTTGAT
GATTTCTTGGCCAATGAGGCAAAGGGAACCAAAGTGGTGGGTGCCCAGTCCCTGAAAGAG
ATGGTCTCCAAGCTGAAGAAGCCCCGGCGGATCATCCTCCTGGTGAAGGCTGGGCAAGCT
GTGGATGATTTCATCGAGAAATTGGTACCATTGTTGGATACTGGTGACATCATCATTGAC
GGAGGAAATTCTGAATATAGGGACACCACAAGACGGTGCCGAGACCTCAAGGCCAAGGGA
ATTTTATTTGTGGGGAGCGGAGTCAGTGGTGGAGAGGAAGGGGCCCGGTATGGCCCATCG
CTCATGCCAGGAGGGAACAAAGAAGCGTGGCCCCACATCAAGACCATCTTCCAAGGCATT
GCTGCAAAAGTGGGAACTGGAGAACCCTGCTGTGACTGGGTGGGAGATGAGGGAGCAGGC
CACTTCGTGAAGATGGTGCACAACGGGATAGAGTATGGGGACATGCAGCTGATCTGTGAG
GCATACCACCTGATGAAAGACGTGCTGGGCATGGCGCAGGACGAGATGGCCCAGGCCTTT
GAGGATTGGAATAAGACAGAGCTAGACTCATTCCTGATTGAAATCACAGCCAATATTCTC
AAGTTCCAAGACACCGATGGCAAACACCTGCTGCCAAAGATCAGGGACAGCGCGGGGCAG
AAGGGCACAGGGAAGTGGACCGCCATCTCCGCCCTGGAATACGGCGTACCCGTCACCCTC
ATTGGAGAAGCTGTCTTTGCTCGGTGCTTATCATCTCTGAAGGATGAGAGAATTCAAGCT
AGCAAAAAGCTGAAGGGTCCCCAGAAGTTCCAGTTTGATGGTGATAAGAAATCATTCCTG
GAGGACATTCGGAAGGCACTCTACGCTTCCAAGATCATCTCTTACGCTCAAGGCTTTATG
CTGCTAAGGCAGGCAGCCACCGAGTTTGGCTGGACTCTCAATTATGGTGGCATCGCCCTG
ATGTGGAGAGGGGGCTGCATCATTAGAAGTGTATTCCTAGGAAAGATAAAGGATGCATTT
GATCGAAACCCGGAACTTCAGAACCTCCTACTGGACGACTTCTTTAAGTCAGCTGTTGAA
AACTGCCAGGACTCCTGGCGGCGGGCAGTCAGCACTGGGGTCCAGGCTGGCATTCCCATG
CCCTGTTTTACCACTGCCCTCTCCTTCTATGACGGGTACAGACATGAGATGCTTCCAGCC
AGCCTCATCCAGGCTCAGCGGGATTACTTCGGGGCTCACACCTATGAACTCTTGGCCAAA
CCAGGGCAGTTTATCCACACCAACTGGACAGGCCATGGTGGCACCGTGTCATCCTCGTCA
TACAATGCCTGA
Enzyme 96 GenBank Gene ID BC000368 Link Image
Enzyme 96 GeneCard ID PGD Link Image
Enzyme 96 GenAtlas ID PGD Link Image
Enzyme 96 HGNC ID HGNC:8891 Link Image
Enzyme 96 Chromosome Location 1
Enzyme 96 Locus 1p36.3-p36.13
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Tsui SK, Chan JY, Waye MM, Fung KP, Lee CY: Identification of a cDNA encoding 6-phosphogluconate dehydrogenase from a human heart cDNA library. Biochem Genet. 1996 Oct;34(9-10):367-73. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 6329
Enzyme 97 Name 2,4-dienoyl-CoA reductase, mitochondrial
Enzyme 97 Synonyms
  1. 2,4-dienoyl-CoA reductase [NADPH]
  2. 4-enoyl-CoA reductase [NADPH]
Enzyme 97 Gene Name DECR1
Enzyme 97 Protein Sequence >2,4-dienoyl-CoA reductase, mitochondrial 
MKLPARVFFTLGSRLPCGLAPRRFFSYGTKILYQNTEALQSKFFSPLQKAMLPPNSFQGK
VAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRD
PDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIG
KQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQP
GPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFD
GGEEVLISGEFNDLRKVTKEQWDTIEELIRKTKGS
Enzyme 97 Number of Residues 335
Enzyme 97 Molecular Weight 36067.4
Enzyme 97 Theoretical pI 9.84
Enzyme 97 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 97 General Function Involved in oxidoreductase activity
Enzyme 97 Specific Function Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3- enoyl-CoA
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions
  • trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+ [RN:R04319]
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein Not Available
Enzyme 97 UniProtKB/Swiss-Prot ID Q16698 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name DECR_HUMAN Link Image
Enzyme 97 PDB ID 1W6U Link Image
Enzyme 97 PDB File Show
Enzyme 97 3D Structure
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >1008 bp 
ATGAAGCTACCGGCCAGGGTTTTCTTTACTCTGGGGTCCCGGCTGCCCTGTGGCCTCGCT
CCTCGGAGGTTTTTCAGTTATGGGACAAAAATATTATATCAAAACACTGAAGCTTTGCAA
TCTAAATTCTTTTCACCTCTTCAAAAAGCGATGCTACCACCTAATAGTTTTCAAGGAAAA
GTGGCATTCATTACTGGGGGAGGTACTGGCCTTGGTAAAGGAATGACAACTCTTCTGTCC
AGCCTAGGTGCTCAGTGCGTGATAGCCAGCCGGAAGATGGATGTTTTGAAAGCTACCGCA
GAACAAATTTCTTCTCAAACTGGAAATAAGGTTCATGCAATTCAGTGTGATGTGAGGGAT
CCTGATATGGTTCAAAACACTGTGTCAGAACTGATCAAAGTTGCAGGACATCCTAATATT
GTGATAAACAATGCAGCAGGGAATTTTATTTCTCCTACTGAAAGACTTTCTCCTAATGCT
TGGAAAACCATAACTGACATAGTTCTAAATGGCACAGCCTTCGTGACACTAGAAATTGGA
AAACAACTAATTAAAGCACAGAAAGGAGCAGCATTTCTTTCTATTACTACTATCTATGCT
GAGACTGGTTCAGGTTTTGTAGTACCAAGTGCTTCTGCCAAAGCAGGTGTGGAAGCCATG
AGCAAGTCTCTTGCAGCTGAATGGGGTAAATATGGAATGCGATTCAATGTGATTCAACCA
GGGCCTATAAAAACCAAAGGTGCCTTTAGCCGTCTGGACCCAACTGGAACATTTGAGAAA
GAAATGATTGGCAGAATTCCCTGTGGTCGCCTGGGGACTGTAGAAGAACTCGCAAATCTT
GCTGCTTTCCTTTGTAGTGATTATGCTTCTTGGATTAATGGAGCAGTCATTAAATTTGAC
GGTGGAGAGGAAGTACTTATTTCAGGGGAATTCAACGACCTGAGAAAGGTCACCAAGGAG
CAGTGGGACACCATAGAAGAACTCATCAGGAAGACAAAAGGTTCCTAA
Enzyme 97 GenBank Gene ID L26050 Link Image
Enzyme 97 GeneCard ID DECR1 Link Image
Enzyme 97 GenAtlas ID DECR1 Link Image
Enzyme 97 HGNC ID HGNC:2753 Link Image
Enzyme 97 Chromosome Location 8
Enzyme 97 Locus 8q21.3
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Koivuranta KT, Hakkola EH, Hiltunen JK: Isolation and characterization of cDNA for human 120 kDa mitochondrial 2,4-dienoyl-coenzyme A reductase. Biochem J. 1994 Dec 15;304 ( Pt 3):787-92. [PubMed Link Image]
  2. Helander HM, Koivuranta KT, Horelli-Kuitunen N, Palvimo JJ, Palotie A, Hiltunen JK: Molecular cloning and characterization of the human mitochondrial 2,4-dienoyl-CoA reductase gene (DECR). Genomics. 1997 Nov 15;46(1):112-9. [PubMed Link Image]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Alphey MS, Yu W, Byres E, Li D, Hunter WN: Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site. J Biol Chem. 2005 Jan 28;280(4):3068-77. Epub 2004 Nov 6. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 6330
Enzyme 98 Name Quinone oxidoreductase
Enzyme 98 Synonyms
  1. NADPH:quinone reductase
  2. Zeta-crystallin
Enzyme 98 Gene Name CRYZ
Enzyme 98 Protein Sequence >Quinone oxidoreductase 
MATGQKLMRAVRVFEFGGPEVLKLRSDIAVPIPKDHQVLIKVHACGVNPVETYIRSGTYS
RKPLLPYTPGSDVAGVIEAVGDNASAFKKGDRVFTSSTISGGYAEYALAADHTVYKLPEK
LDFKQGAAIGIPYFTAYRALIHSACVKAGESVLVHGASGGVGLAACQIARAYGLKILGTA
GTEEGQKIVLQNGAHEVFNHREVNYIDKIKKYVGEKGIDIIIEMLANVNLSKDLSLLSHG
GRVIVVGSRGTIEINPRDTMAKESSIIGVTLFSSTKEEFQQYAAALQAGMEIGWLKPVIG
SQYPLEKVAEAHENIIHGSGATGKMILLL
Enzyme 98 Number of Residues 329
Enzyme 98 Molecular Weight 35206.4
Enzyme 98 Theoretical pI 8.70
Enzyme 98 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 98 General Function Involved in zinc ion binding
Enzyme 98 Specific Function Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding
Enzyme 98 Pathways Not Available
Enzyme 98 Reactions
  • NADPH + H+ + 2 quinone = NADP+ + 2 semiquinone [RN:R02364]
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein Not Available
Enzyme 98 UniProtKB/Swiss-Prot ID Q08257 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name QOR_HUMAN Link Image
Enzyme 98 PDB ID 1YB5 Link Image
Enzyme 98 PDB File Show
Enzyme 98 3D Structure
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >990 bp 
ATGGCGACTGGACAGAAGTTGATGAGAGCTGTTAGAGTTTTTGAATTTGGTGGGCCAGAA
GTCCTGAAATTGCGATCAGATATTGCAGTACCGATTCCAAAAGACCATCAGGTTCTAATC
AAGGTCCATGCATGTGGTGTCAACCCCGTGGAGACATACATTCGCTCTGGTACTTATAGT
AGAAAACCACTCTTACCCTATACTCCTGGCTCAGATGTGGCTGGGGTGATAGAAGCTGTT
GGAGATAATGCATCTGCTTTCAAGAAAGGTGACAGAGTTTTCACTAGCAGCACGATCTCT
GGGGGTTATGCAGAGTATGCTCTTGCAGCAGACCACACTGTTTACAAACTACCTGAAAAA
CTGGACTTTAAACAAGGAGCTGCCATCGGCATTCCATATTTTACTGCTTATCGAGCTCTG
ATCCACAGTGCCTGTGTGAAAGCTGGAGAGAGTGTTCTGGTTCATGGGGCAAGTGGAGGA
GTTGGATTAGCAGCATGCCAAATTGCTAGAGCTTATGGCTTAAAGATTTTGGGCACTGCT
GGTACTGAGGAAGGACAAAAGATTGTTTTGCAAAATGGAGCCCATGAAGTGTTCAATCAC
AGAGAAGTGAATTACATTGATAAAATTAAGAAGTATGTTGGTGAGAAAGGAATTGATATA
ATTATTGAAATGTTAGCTAATGTAAATCTTAGTAAAGACTTGAGTCTTCTGTCACATGGA
GGACGAGTGATAGTTGTTGGCAGCAGAGGTACTATTGAAATAAACCCACGAGACACCATG
GCAAAGGAGTCGAGTATAATTGGAGTTACTCTCTTTTCCTCAACCAAGGAGGAATTTCAG
CAATATGCAGCAGCCCTTCAAGCTGGAATGGAAATTGGCTGGTTGAAACCTGTGATAGGT
TCTCAATATCCATTGGAGAAGGTGGCCGAGGCTCATGAAAATATCATTCATGGTAGTGGG
GCTACTGGAAAAATGATTCTTCTCTTATGA
Enzyme 98 GenBank Gene ID L13278 Link Image
Enzyme 98 GeneCard ID CRYZ Link Image
Enzyme 98 GenAtlas ID CRYZ Link Image
Enzyme 98 HGNC ID HGNC:2419 Link Image
Enzyme 98 Chromosome Location 1
Enzyme 98 Locus 1p31-p22
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Gonzalez P, Rao PV, Zigler JS Jr: Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver. Biochem Biophys Res Commun. 1993 Mar 31;191(3):902-7. [PubMed Link Image]
  2. Gonzalez P, Rao PV, Zigler JS Jr: Organization of the human zeta-crystallin/quinone reductase gene (CRYZ). Genomics. 1994 May 15;21(2):317-24. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Fernandez MR, Porte S, Crosas E, Barbera N, Farres J, Biosca JA, Pares X: Human and yeast zeta-crystallins bind AU-rich elements in RNA. Cell Mol Life Sci. 2007 Jun;64(11):1419-27. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Lapucci A, Lulli M, Amedei A, Papucci L, Witort E, Di Gesualdo F, Bertolini F, Brewer G, Nicolin A, Bevilacqua A, Schiavone N, Morello D, Donnini M, Capaccioli S: zeta-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2 overexpression in T-cell acute lymphocytic leukemia. FASEB J. 2010 Jun;24(6):1852-65. Epub 2010 Jan 26. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 6331
Enzyme 99 Name 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
Enzyme 99 Synonyms
  1. 25-OHD-1 alpha-hydroxylase
  2. 25-hydroxyvitamin D(3) 1-alpha-hydroxylase
  3. VD3 1A hydroxylase
  4. Calcidiol 1-monooxygenase
  5. Cytochrome P450 subfamily XXVIIB polypeptide 1
  6. Cytochrome P450C1 alpha
  7. Cytochrome P450VD1-alpha
  8. Cytochrome p450 27B1
Enzyme 99 Gene Name CYP27B1
Enzyme 99 Protein Sequence >25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial 
MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSR
LHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCR
QRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPP
ALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPH
WLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFRE
ELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPS
ATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPA
QFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQP
EPGAAPVRPKTRTVLVPERSINLQFLDR
Enzyme 99 Number of Residues 508
Enzyme 99 Molecular Weight 56503.5
Enzyme 99 Theoretical pI 9.39
Enzyme 99 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 99 General Function Involved in monooxygenase activity
Enzyme 99 Specific Function Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation
Enzyme 99 Pathways
Enzyme 99 Reactions
  • calcidiol + NADPH + H+ + O2 = calcitriol + NADP+ + H2O [RN:R03610]
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein Not Available
Enzyme 99 UniProtKB/Swiss-Prot ID O15528 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name CP27B_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >1527 bp 
ATGACCCAGACCCTCAAGTACGCCTCCAGAGTGTTCCATCGCGTCCGCTGGGCGCCCGAG
TTGGGCGCCTCCCTAGGCTACCGAGAGTACCACTCAGCACGCCGGAGCTTGGCAGACATC
CCAGGCCCCTCTACGCCCAGCTTTCTGGCCGAACTTTTCTGCAAGGGGGGGCTGTCGAGG
CTACACGAGCTGCAGGTGCAGGGCGCCGCGCACTTCGGGCCGGTGTGGCTAGCCAGCTTT
GGGACAGTGCGCACCGTGTACGTGGCTGCCCCTGCACTCGTCGAGGAGCTGCTGCGACAG
GAGGGACCCCGGCCCGAGCGCTGCAGCTTCTCGCCCTGGACGGAGCACCGCCGCTGCCGC
CAGCGGGCTTGCGGACTGCTCACTGCGGAAGGCGAAGAATGGCAAAGGCTCCGCAGTCTC
CTGGCCCCGCTCCTCCTCCGGCCTCAAGCGGCCGCCCGCTACGCCGGAACCCTGAACAAC
GTAGTCTGCGACCTTGTGCGGCGTCTGAGGCGCCAGCGGGGACGTGGCACGGGGCCGCCC
GCCCTGGTTCGGGACGTGGCGGGGGAATTTTACAAGTTCGGACTGGAAGGCATCGCCGCG
GTTCTGCTCGGCTCGCGCTTGGGCTGCCTGGAGGCTCAAGTGCCACCCGACACGGAGACC
TTCATCCGCGCTGTGGGCTCGGTGTTTGTGTCCACGCTGTTGACCATGGCGATGCCCCAC
TGGCTGCGCCACCTTGTGCCTGGGCCCTGGGGCCGCCTCTGCCGAGACTGGGACCAGATG
TTTGCATTTGCTCAGAGGCACGTGGAGCGGCGAGAGGCAGAGGCAGCCATGAGGAACGGA
GGACAGCCCGAGAAGGACCTGGAGTCTGGGGCGCACCTGACCCACTTCCTGTTCCGGGAA
GAGTTGCCTGCCCAGTCCATCCTGGGAAATGTGACAGAGTTGCTATTGGCGGGAGTGGAC
ACGGTGTCCAACACGCTCTCTTGGGCTCTGTATGAGCTCTCCCGGCACCCCGAAGTCCAG
ACAGCACTCCACTCAGAGATCACAGCTGCCCTGAGCCCTGGCTCCAGTGCCTACCCCTCA
GCCACTGTTCTGTCCCAGCTGCCCCTGCTGAAGGCGGTGGTCAAGGAAGTGCTAAGACTG
TACCCTGTGGTACCTGGAAATTCTCGTGTCCCAGACAAAGACATTCATGTGGGTGACTAT
ATTATCCCCAAAAATACGCTGGTCACTCTGTGTCACTATGCCACTTCAAGGGACCCTGCC
CAGTTCCCAGAGCCAAATTCTTTTCGTCCAGCTCGCTGGCTGGGGGAGGGTCCCACCCCC
CACCCATTTGCATCTCTTCCCTTTGGCTTTGGCAAGCGCAGCTGTATGGGGAGACGCCTG
GCAGAGCTTGAATTGCAAATGGCTTTGGCCCAGATCCTAACACATTTTGAGGTGCAGCCT
GAGCCAGGTGCGGCCCCAGTTAGACCCAAGACCCGGACTGTCCTGGTACCTGAAAGGAGC
ATCAACCTACAGTTTTTGGACAGATAG
Enzyme 99 GenBank Gene ID AB005038 Link Image
Enzyme 99 GeneCard ID CYP27B1 Link Image
Enzyme 99 GenAtlas ID CYP27B1 Link Image
Enzyme 99 HGNC ID HGNC:2606 Link Image
Enzyme 99 Chromosome Location 1
Enzyme 99 Locus 12q13.1-q13.3
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References
  1. Fu GK, Portale AA, Miller WL: Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha. DNA Cell Biol. 1997 Dec;16(12):1499-507. [PubMed Link Image]
  2. Monkawa T, Yoshida T, Wakino S, Shinki T, Anazawa H, Deluca HF, Suda T, Hayashi M, Saruta T: Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase. Biochem Biophys Res Commun. 1997 Oct 20;239(2):527-33. [PubMed Link Image]
  3. Fu GK, Lin D, Zhang MY, Bikle DD, Shackleton CH, Miller WL, Portale AA: Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1. Mol Endocrinol. 1997 Dec;11(13):1961-70. [PubMed Link Image]
  4. Kitanaka S, Takeyama K, Murayama A, Sato T, Okumura K, Nogami M, Hasegawa Y, Niimi H, Yanagisawa J, Tanaka T, Kato S: Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets. N Engl J Med. 1998 Mar 5;338(10):653-61. [PubMed Link Image]
  5. Wang JT, Lin CJ, Burridge SM, Fu GK, Labuda M, Portale AA, Miller WL: Genetics of vitamin D 1alpha-hydroxylase deficiency in 17 families. Am J Hum Genet. 1998 Dec;63(6):1694-702. [PubMed Link Image]
  6. Smith SJ, Rucka AK, Berry JL, Davies M, Mylchreest S, Paterson CR, Heath DA, Tassabehji M, Read AP, Mee AP, Mawer EB: Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages. J Bone Miner Res. 1999 May;14(5):730-9. [PubMed Link Image]
  7. Kitanaka S, Murayama A, Sakaki T, Inouye K, Seino Y, Fukumoto S, Shima M, Yukizane S, Takayanagi M, Niimi H, Takeyama K, Kato S: No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene product in pseudovitamin D deficiency rickets, including that with mild clinical manifestation. J Clin Endocrinol Metab. 1999 Nov;84(11):4111-7. [PubMed Link Image]
  8. Wang X, Zhang MY, Miller WL, Portale AA: Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro. J Clin Endocrinol Metab. 2002 Jun;87(6):2424-30. [PubMed Link Image]
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 6332
Enzyme 100 Name Steroid 17-alpha-hydroxylase/17,20 lyase
Enzyme 100 Synonyms
  1. CYPXVII
  2. Cytochrome P450 17A1
  3. Cytochrome P450-C17
  4. Cytochrome P450c17
  5. Steroid 17-alpha-monooxygenase
Enzyme 100 Gene Name CYP17A1
Enzyme 100 Protein Sequence >Steroid 17-alpha-hydroxylase/17,20 lyase 
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
Enzyme 100 Number of Residues 508
Enzyme 100 Molecular Weight 57370.0
Enzyme 100 Theoretical pI 8.87
Enzyme 100 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 100 General Function Involved in monooxygenase activity
Enzyme 100 Specific Function Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty
Enzyme 100 Pathways
Enzyme 100 Reactions
  • a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O [RN:R02131]
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein Not Available
Enzyme 100 UniProtKB/Swiss-Prot ID P05093 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name CP17A_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >1527 bp 
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
Enzyme 100 GenBank Gene ID M14564 Link Image
Enzyme 100 GeneCard ID CYP17A1 Link Image
Enzyme 100 GenAtlas ID CYP17A1 Link Image
Enzyme 100 HGNC ID HGNC:2593 Link Image
Enzyme 100 Chromosome Location 1
Enzyme 100 Locus 10q24.3
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed Link Image]
  2. Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed Link Image]
  3. Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed Link Image]
  4. Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed Link Image]
  5. Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed Link Image]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed Link Image]
  9. Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed Link Image]
  10. Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed Link Image]
  11. Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed Link Image]
  12. Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed Link Image]
  13. Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed Link Image]
  14. Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed Link Image]
  15. Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed Link Image]
  16. Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed Link Image]
  17. Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed Link Image]
  18. Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed Link Image]
  19. Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed Link Image]
  20. Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed Link Image]
  21. Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed Link Image]
  22. Martin RM, Lin CJ, Costa EM, de Oliveira ML, Carrilho A, Villar H, Longui CA, Mendonca BB: P450c17 deficiency in Brazilian patients: biochemical diagnosis through progesterone levels confirmed by CYP17 genotyping. J Clin Endocrinol Metab. 2003 Dec;88(12):5739-46. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 6333
Enzyme 101 Name Peroxisomal 2,4-dienoyl-CoA reductase
Enzyme 101 Synonyms
  1. pDCR
  2. 2,4-dienoyl-CoA reductase 2
Enzyme 101 Gene Name DECR2
Enzyme 101 Protein Sequence >Peroxisomal 2,4-dienoyl-CoA reductase 
MAQPPPDVEGDDCLPAYRHLFCPDLLRDKVAFITGGGSGIGFRIAEIFMRHGCHTVIASR
SLPRVLTAARKLAGATGRRCLPLSMDVRAPPAVMAAVDQALKEFGRIDILINCAAGNFLC
PAGALSFNAFKTVMDIDTSGTFNVSRVLYEKFFRDHGGVIVNITATLGNRGQALQVHAGS
AKAAVDAMTRHLAVEWGPQNIRVNSLAPGPISGTEGLRRLGGPQASLSTKVTASPLQRLG
NKTEIAHSVLYLASPLASYVTGAVLVADGGAWLTFPNGVKGLPDFASFSAKL
Enzyme 101 Number of Residues 292
Enzyme 101 Molecular Weight 30777.2
Enzyme 101 Theoretical pI 9.59
Enzyme 101 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 101 General Function Involved in oxidoreductase activity
Enzyme 101 Specific Function Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19- docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions
  • trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+ [RN:R04319]
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 14336698 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q9NUI1 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name DECR2_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >879 bp 
ATGGCCCAGCCGCCGCCCGACGTGGAGGGGGACGACTGTCTCCCCGCGTACCGCCACCTC
TTCTGCCCGGACCTGCTGCGGGACAAAGTGGCCTTCATCACAGGAGGCGGCTCTGGGATT
GGGTTCCGGATTGCTGAGATTTTCATGCGGCACGGCTGCCATACGGTGATTGCCAGTAGG
AGCCTGCCGCGAGTGCTGACGGCCGCCAGGAAGCTGGCTGGGGCCACCGGCCGGCGCTGC
CTCCCTCTCTCTATGGACGTCCGAGCGCCCCCAGCTGTCATGGCCGCCGTGGACCAGGCT
CTGAAGGAGTTTGGCAGAATCGACATTCTCATTAACTGTGCGGCCGGGAACTTCCTGTGC
CCCGCTGGCGCCTTGTCCTTCAACGCCTTCAAGACCGTGATGGACATCGATACCAGCGGC
ACCTTCAATGTGTCTCGTGTGCTCTATGAGAAGTTCTTCCGGGACCACGGAGGGGTGATC
GTGAACATCACTGCCACCCTGGGGAACCGGGGGCAGGCGCTCCAGGTGCATGCAGGCTCC
GCCAAGGCCGCTGTGGACGCGATGACGCGGCACTTGGCTGTGGAGTGGGGTCCCCAAAAC
ATCCGCGTCAACAGCCTCGCCCCTGGCCCCATCAGTGGCACAGAGGGGCTCCGGCGACTG
GGTGGCCCTCAGGCCAGCCTGAGCACCAAGGTCACTGCCAGCCCGCTGCAGAGGCTGGGG
AACAAGACCGAGATCGCCCACAGCGTGCTCTACCTGGCCAGCCCTCTGGCTTCCTACGTG
ACGGGGGCCGTGCTGGTGGCCGATGGCGGGGCATGGTTGACGTTCCCAAACGGTGTCAAA
GGGCTGCCGGATTTCGCATCCTTCTCTGCTAAGCTCTAG
Enzyme 101 GenBank Gene ID AE006463 Link Image
Enzyme 101 GeneCard ID DECR2 Link Image
Enzyme 101 GenAtlas ID DECR2 Link Image
Enzyme 101 HGNC ID HGNC:2754 Link Image
Enzyme 101 Chromosome Location 1
Enzyme 101 Locus 16p13.3
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. De Nys K, Meyhi E, Mannaerts GP, Fransen M, Van Veldhoven PP: Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase. Biochim Biophys Acta. 2001 Aug 29;1533(1):66-72. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 6840
Enzyme 102 Name Cytochrome P450 2E1
Enzyme 102 Synonyms
  1. 4-nitrophenol 2-hydroxylase
  2. CYPIIE1
  3. Cytochrome P450-J
Enzyme 102 Gene Name CYP2E1
Enzyme 102 Protein Sequence >Cytochrome P450 2E1 
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
Enzyme 102 Number of Residues 493
Enzyme 102 Molecular Weight 56848.4
Enzyme 102 Theoretical pI 8.22
Enzyme 102 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 102 General Function Involved in monooxygenase activity
Enzyme 102 Specific Function Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Inactivates a number of drugs and xenobiotics and also bioactivates many xenobiotic substrates to their hepatotoxic or carcinogenic forms
Enzyme 102 Pathways
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • None
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein Not Available
Enzyme 102 UniProtKB/Swiss-Prot ID P05181 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name CP2E1_HUMAN Link Image
Enzyme 102 PDB ID Not Available
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >1482 bp 
ATGTCTGCCCTCGGAGTGACCGTGGCCCTGCTGGTGTGGGCGGCCTTCCTCCTGCTGGTG
TCCATGTGGAGGCAGGTGCACAGCAGCTGGAATCTGCCCCCAGGTCCTTTCCCGCTTCCC
ATCATCGGGAACCTCTTCCAGTTGGAATTGAAGAATATTCCCAAGTCCTTCACCCGGTTG
GCCCAGCGCTTCGGGCCGGTGTTCACGCTGTACGTGGGCTCGCAGCGCATGGTGGTGATG
CACGGCTACAAGGCGGTGAAGGAAGCGCTGCTGGACTACAAGGACGAGTTCTCGGGCAGA
GGCGACCTCCCCGCGTTCCATGCGCACAGGGACAGGGGAATCATTTTTAATAATGGACCT
ACCTGGAAGGACATCCGGCGGTTTTCCCTGACCACCCTCCGGAACTATGGGATGGGGAAA
CAGGGCAATGAGAGCCGGATCCAGAGGGAGGCCCACTTCCTGCTGGAAGCACTCAGGAAG
ACCCAAGGCCAGCCTTTCGACCCCACCTTCCTCATCGGCTGCGCGCCCTGCAACGTCATA
GCCGACATCCTCTTCCGCAAGCATTTTGACTACAATGATGAGAAGTTTCTAAGGCTGATG
TATTTGTTTAATGAGAACTTCCACCTACTCAGCACTCCCTGGCTCCAGCTTTACAATAAT
TTTCCCAGCTTTCTACACTACTTGCCTGGAAGCCACAGAAAAGTCATAAAAAATGTGGCT
GAAGTAAAAGAGTATGTGTCTGAAAGGGTGAAGGAGCACCATCAATCTCTGGACCCCAAC
TGTCCCCGGGACCTCACCGACTGCCTGCTCGTGGAAATGGAGAAGGAAAAGCACAGTGCA
GAGCGCTTGTACACAATGGACGGTATCACCGTGACTGTGGCCGACCTGTTCTTTGCGGGG
ACAGAGACCACCAGCACAACTCTGAGATATGGGCTCCTGATTCTCATGAAATACCCTGAG
ATCGAAGAGAAGCTCCATGAAGAAATTGACAGGGTGATTGGGCCAAGCCGAATCCCTGCC
ATCAAGGATAGGCAAGAGATGCCCTACATGGATGCTGTGGTGCATGAGATTCAGCGGTTC
ATCACCCTCGTGCCCTCCAACCTGCCCCATGAAGCAACCCGAGACACCATTTTCAGAGGA
TACCTCATCCCCAAGGGCACAGTCGTAGTGCCAACTCTGGACTCTGTTTTGTATGACAAC
CAAGAATTTCCTGATCCAGAAAAGTTTAAGCCAGAACACTTCCTGAATGAAAATGGAAAG
TTCAAGTACAGTGACTATTTCAAGCCATTTTCCACAGGAAAACGAGTGTGTGCTGGAGAA
GGCCTGGCTCGCATGGAGTTGTTTCTTTTGTTGTGTGCCATTTTGCAGCATTTTAATTTG
AAGCCTCTCGTTGACCCAAAGGATATCGACCTCAGCCCTATACATATTGGGTTTGGCTGT
ATCCCACCACGTTACAAACTCTGTGTCATTCCCCGCTCATGA
Enzyme 102 GenBank Gene ID J02625 Link Image
Enzyme 102 GeneCard ID CYP2E1 Link Image
Enzyme 102 GenAtlas ID CYP2E1 Link Image
Enzyme 102 HGNC ID HGNC:2631 Link Image
Enzyme 102 Chromosome Location 1
Enzyme 102 Locus 10q24.3-qter
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Song BJ, Gelboin HV, Park SS, Yang CS, Gonzalez FJ: Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme. J Biol Chem. 1986 Dec 15;261(35):16689-97. [PubMed Link Image]
  2. Umeno M, McBride OW, Yang CS, Gelboin HV, Gonzalez FJ: Human ethanol-inducible P450IIE1: complete gene sequence, promoter characterization, chromosome mapping, and cDNA-directed expression. Biochemistry. 1988 Dec 13;27(25):9006-13. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Lasker JM, Raucy J, Kubota S, Bloswick BP, Black M, Lieber CS: Purification and characterization of human liver cytochrome P-450-ALC. Biochem Biophys Res Commun. 1987 Oct 14;148(1):232-8. [PubMed Link Image]
  5. Robinson RC, Shorr RG, Varrichio A, Park SS, Gelboin HV, Miller H, Friedman FK: Human liver cytochrome P-450 related to a rat acetone-inducible, nitrosamine-metabolizing cytochrome P-450: identification and isolation. Pharmacology. 1989;39(3):137-44. [PubMed Link Image]
  6. Gillam EM, Guo Z, Guengerich FP: Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties. Arch Biochem Biophys. 1994 Jul;312(1):59-66. [PubMed Link Image]
  7. Zerilli A, Ratanasavanh D, Lucas D, Goasduff T, Dreano Y, Menard C, Picart D, Berthou F: Both cytochromes P450 2E1 and 3A are involved in the O-hydroxylation of p-nitrophenol, a catalytic activity known to be specific for P450 2E1. Chem Res Toxicol. 1997 Oct;10(10):1205-12. [PubMed Link Image]
  8. Porubsky PR, Meneely KM, Scott EE: Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates. J Biol Chem. 2008 Nov 28;283(48):33698-707. Epub 2008 Sep 24. [PubMed Link Image]
  9. Hu Y, Oscarson M, Johansson I, Yue QY, Dahl ML, Tabone M, Arinco S, Albano E, Ingelman-Sundberg M: Genetic polymorphism of human CYP2E1: characterization of two variant alleles. Mol Pharmacol. 1997 Mar;51(3):370-6. [PubMed Link Image]
  10. Fairbrother KS, Grove J, de Waziers I, Steimel DT, Day CP, Crespi CL, Daly AK: Detection and characterization of novel polymorphisms in the CYP2E1 gene. Pharmacogenetics. 1998 Dec;8(6):543-52. [PubMed Link Image]
  11. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 6843
Enzyme 103 Name Cytochrome P450 1B1
Enzyme 103 Synonyms
  1. CYPIB1
Enzyme 103 Gene Name CYP1B1
Enzyme 103 Protein Sequence >Cytochrome P450 1B1 
MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLI
GNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAF
ASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVAL
LVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSL
VDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSA
EKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAEL
DQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVV
FVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQL
FLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKE
TCQ
Enzyme 103 Number of Residues 543
Enzyme 103 Molecular Weight 60845.3
Enzyme 103 Theoretical pI 9.23
Enzyme 103 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 103 General Function Involved in monooxygenase activity
Enzyme 103 Specific Function Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development
Enzyme 103 Pathways
Enzyme 103 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • None
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 501031 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID Q16678 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name CP1B1_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >1632 bp 
ATGGGCACCAGCCTCAGCCCGAACGACCCTTGGCCGCTAAACCCGCTGTCCATCCAGCAG
ACCACGCTCCTGCTACTCCTGTCGGTGCTGGCCACTGTGCATGTGGGCCAGCGGCTGCTG
AGGCAACGGAGGCGGCAGCTCCGGTCCGCGCCCCCGGGCCCGTTTGCGTGGCCACTGATC
GGAAACGCGGCGGCGGTGGGCCAGGCGGCTCACCTCTCGTTCGCTCGCCTGGCGCGGCGC
TACGGCGACGTTTTCCAGATCCGCCTGGGCAGCTGCCCCATAGTGGTGCTGAATGGCGAG
CGCGCCATCCACCAGGCCCTGGTGCAGCAGGGCTCGGCCTTCGCCGACCGGCCGGCCTTC
GCCTCCTTCCGTGTGGTGTCCGGCGGCCGCAGCATGGCTTTCGGCCACTACTCGGAGCAC
TGGAAGGTGCAGCGGCGCGCAGCCCACAGCATGATGCGCAACTTCTTCACGCGCCAGCCG
CGCAGCCGCCAAGTCCTCGAGGGCCACGTGCTGAGCGAGGCGCGCGAGCTGGTGGCGCTG
CTGGTGCGCGGCAGCGCGGACGGCGCCTTCCTCGACCCGAGGCCGCTGACCGTCGTGGCC
GTGGCCAACGTCATGAGTGCCGTGTGTTTCGGCTGCCGCTACAGCCACGACGACCCCGAG
TTCCGTGAGCTGCTCAGCCACAACGAAGAGTTCGGGCGCACGGTGGGCGCGGGCAGCCTG
GTGGACGTGATGCCCTGGCTGCAGTACTTCCCCAACCCGGTGCGCACCGTTTTCCGCGAA
TTCGAGCAGCTCAACCGCAACTTCAGCAACTTCATCCTGGACAAGTTCTTGAGGCACTGC
GAAAGCCTTCGGCCCGGGGCCGCCCCCCGCGACATGATGGACGCCTTTATCCTCTCTGCG
GAAAAGAAGGCGGCCGGGGACTCGCACGGTGGTGGCGCGCGGCTGGATTTGGAGAACGTA
CCGGCCACTATCACTGACATCTTCGGCGCCAGCCAGGACACCCTGTCCACCGCGCTGCAG
TGGCTGCTCCTCCTCTTCACCAGGTATCCTGATGTGCAGACTCGAGTGCAGGCAGAATTG
GATCAGGTCGTGGGGAGGGACCGTCTGCCTTGTATGGGTGACCAGCCCAACCTGCCCTAT
GTCCTGGCCTTCCTTTATGAAGCCATGCGCTTCTCCAGCTTTGTGCCTGTCACTATTCCT
CATGCCACCACTGCCAACACCTCTGTCTTGGGCTACCACATTCCCAAGGACACTGTGGTT
TTTGTCAACCAGTGGTCTGTGAATCATGACCCAGTGAAGTGGCCTAACCCGGAGAACTTT
GATCCAGCTCGATTCTTGGACAAGGATGGCCTCATCAACAAGGACCTGACCAGCAGAGTG
ATGATTTTTTCAGTGGGCAAAAGGCGGTGCATTGGCGAAGAACTTTCTAAGATGCAGCTT
TTTCTCTTCATCTCCATCCTGGCTCACCAGTGCGATTTCAGGGCCAACCCAAATGAGCCT
GCGAAAATGAATTTCAGTTATGGTCTAACCATTAAACCCAAGTCATTTAAAGTCAATGTC
ACTCTCAGAGAGTCCATGGAGCTCCTTGATAGTGCTGTCCAAAATTTACAAGCCAAGGAA
ACTTGCCAATAA
Enzyme 103 GenBank Gene ID U03688 Link Image
Enzyme 103 GeneCard ID CYP1B1 Link Image
Enzyme 103 GenAtlas ID CYP1B1 Link Image
Enzyme 103 HGNC ID HGNC:2597 Link Image
Enzyme 103 Chromosome Location 2
Enzyme 103 Locus 2p21
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References
  1. Sutter TR, Tang YM, Hayes CL, Wo YY, Jabs EW, Li X, Yin H, Cody CW, Greenlee WF: Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. J Biol Chem. 1994 May 6;269(18):13092-9. [PubMed Link Image]
  2. Tang YM, Wo YY, Stewart J, Hawkins AL, Griffin CA, Sutter TR, Greenlee WF: Isolation and characterization of the human cytochrome P450 CYP1B1 gene. J Biol Chem. 1996 Nov 8;271(45):28324-30. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bejjani BA, Lewis RA, Tomey KF, Anderson KL, Dueker DK, Jabak M, Astle WF, Otterud B, Leppert M, Lupski JR: Mutations in CYP1B1, the gene for cytochrome P4501B1, are the predominant cause of primary congenital glaucoma in Saudi Arabia. Am J Hum Genet. 1998 Feb;62(2):325-33. [PubMed Link Image]
  5. Stoilov I, Akarsu AN, Alozie I, Child A, Barsoum-Homsy M, Turacli ME, Or M, Lewis RA, Ozdemir N, Brice G, Aktan SG, Chevrette L, Coca-Prados M, Sarfarazi M: Sequence analysis and homology modeling suggest that primary congenital glaucoma on 2p21 results from mutations disrupting either the hinge region or the conserved core structures of cytochrome P4501B1. Am J Hum Genet. 1998 Mar;62(3):573-84. [PubMed Link Image]
  6. Bailey LR, Roodi N, Dupont WD, Parl FF: Association of cytochrome P450 1B1 (CYP1B1) polymorphism with steroid receptor status in breast cancer. Cancer Res. 1998 Nov 15;58(22):5038-41. [PubMed Link Image]
  7. Shimada T, Watanabe J, Kawajiri K, Sutter TR, Guengerich FP, Gillam EM, Inoue K: Catalytic properties of polymorphic human cytochrome P450 1B1 variants. Carcinogenesis. 1999 Aug;20(8):1607-13. [PubMed Link Image]
  8. Plasilova M, Stoilov I, Sarfarazi M, Kadasi L, Ferakova E, Ferak V: Identification of a single ancestral CYP1B1 mutation in Slovak Gypsies (Roms) affected with primary congenital glaucoma. J Med Genet. 1999 Apr;36(4):290-4. [PubMed Link Image]
  9. Bejjani BA, Stockton DW, Lewis RA, Tomey KF, Dueker DK, Jabak M, Astle WF, Lupski JR: Multiple CYP1B1 mutations and incomplete penetrance in an inbred population segregating primary congenital glaucoma suggest frequent de novo events and a dominant modifier locus. Hum Mol Genet. 2000 Feb 12;9(3):367-74. [PubMed Link Image]
  10. Ohtake Y, Kubota R, Tanino T, Miyata H, Mashima Y: Novel compound heterozygous mutations in the cytochrome P4501B1 gene (CYP1B1) in a Japanese patient with primary congenital glaucoma. Ophthalmic Genet. 2000 Sep;21(3):191-3. [PubMed Link Image]
  11. Watanabe J, Shimada T, Gillam EM, Ikuta T, Suemasu K, Higashi Y, Gotoh O, Kawajiri K: Association of CYP1B1 genetic polymorphism with incidence to breast and lung cancer. Pharmacogenetics. 2000 Feb;10(1):25-33. [PubMed Link Image]
  12. Mashima Y, Suzuki Y, Sergeev Y, Ohtake Y, Tanino T, Kimura I, Miyata H, Aihara M, Tanihara H, Inatani M, Azuma N, Iwata T, Araie M: Novel cytochrome P4501B1 (CYP1B1) gene mutations in Japanese patients with primary congenital glaucoma. Invest Ophthalmol Vis Sci. 2001 Sep;42(10):2211-6. [PubMed Link Image]
  13. Vincent AL, Billingsley G, Buys Y, Levin AV, Priston M, Trope G, Williams-Lyn D, Heon E: Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene. Am J Hum Genet. 2002 Feb;70(2):448-60. Epub 2002 Jan 3. [PubMed Link Image]
  14. Panicker SG, Reddy AB, Mandal AK, Ahmed N, Nagarajaram HA, Hasnain SE, Balasubramanian D: Identification of novel mutations causing familial primary congenital glaucoma in Indian pedigrees. Invest Ophthalmol Vis Sci. 2002 May;43(5):1358-66. [PubMed Link Image]
  15. Stoilov IR, Costa VP, Vasconcellos JP, Melo MB, Betinjane AJ, Carani JC, Oltrogge EV, Sarfarazi M: Molecular genetics of primary congenital glaucoma in Brazil. Invest Ophthalmol Vis Sci. 2002 Jun;43(6):1820-7. [PubMed Link Image]
  16. Aklillu E, Oscarson M, Hidestrand M, Leidvik B, Otter C, Ingelman-Sundberg M: Functional analysis of six different polymorphic CYP1B1 enzyme variants found in an Ethiopian population. Mol Pharmacol. 2002 Mar;61(3):586-94. [PubMed Link Image]
  17. Chakrabarti S, Komatireddy S, Mandal AK, Balasubramanian D: Gene symbol: CYP1B1. Disease: glaucoma, primary congenital. Hum Genet. 2003 Nov;113(6):556. [PubMed Link Image]
  18. Colomb E, Kaplan J, Garchon HJ: Novel cytochrome P450 1B1 (CYP1B1) mutations in patients with primary congenital glaucoma in France. Hum Mutat. 2003 Dec;22(6):496. [PubMed Link Image]
  19. Sitorus R, Ardjo SM, Lorenz B, Preising M: CYP1B1 gene analysis in primary congenital glaucoma in Indonesian and European patients. J Med Genet. 2003 Jan;40(1):e9. [PubMed Link Image]
  20. Melki R, Colomb E, Lefort N, Brezin AP, Garchon HJ: CYP1B1 mutations in French patients with early-onset primary open-angle glaucoma. J Med Genet. 2004 Sep;41(9):647-51. [PubMed Link Image]
  21. Reddy AB, Kaur K, Mandal AK, Panicker SG, Thomas R, Hasnain SE, Balasubramanian D, Chakrabarti S: Mutation spectrum of the CYP1B1 gene in Indian primary congenital glaucoma patients. Mol Vis. 2004 Sep 30;10:696-702. [PubMed Link Image]
  22. Curry SM, Daou AG, Hermanns P, Molinari A, Lewis RA, Bejjani BA: Cytochrome P4501B1 mutations cause only part of primary congenital glaucoma in Ecuador. Ophthalmic Genet. 2004 Mar;25(1):3-9. [PubMed Link Image]
  23. Alfadhli S, Behbehani A, Elshafey A, Abdelmoaty S, Al-Awadi S: Molecular and clinical evaluation of primary congenital glaucoma in Kuwait. Am J Ophthalmol. 2006 Mar;141(3):512-6. [PubMed Link Image]
  24. Acharya M, Mookherjee S, Bhattacharjee A, Bandyopadhyay AK, Daulat Thakur SK, Bhaduri G, Sen A, Ray K: Primary role of CYP1B1 in Indian juvenile-onset POAG patients. Mol Vis. 2006 Apr 20;12:399-404. [PubMed Link Image]
  25. Chavarria-Soley G, Michels-Rautenstrauss K, Pasutto F, Flikier D, Flikier P, Cirak S, Bejjani B, Winters DL, Lewis RA, Mardin C, Reis A, Rautenstrauss B: Primary congenital glaucoma and Rieger's anomaly: extended haplotypes reveal founder effects for eight distinct CYP1B1 mutations. Mol Vis. 2006 May 22;12:523-31. [PubMed Link Image]
  26. Lopez-Garrido MP, Sanchez-Sanchez F, Lopez-Martinez F, Aroca-Aguilar JD, Blanco-Marchite C, Coca-Prados M, Escribano J: Heterozygous CYP1B1 gene mutations in Spanish patients with primary open-angle glaucoma. Mol Vis. 2006 Jul 11;12:748-55. [PubMed Link Image]
  27. Chavarria-Soley G, Sticht H, Aklillu E, Ingelman-Sundberg M, Pasutto F, Reis A, Rautenstrauss B: Mutations in CYP1B1 cause primary congenital glaucoma by reduction of either activity or abundance of the enzyme. Hum Mutat. 2008 Sep;29(9):1147-53. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 6845
Enzyme 104 Name Cytochrome P450 2C18
Enzyme 104 Synonyms
  1. CYPIIC18
  2. Cytochrome P450-6b/29c
Enzyme 104 Gene Name CYP2C18
Enzyme 104 Protein Sequence >Cytochrome P450 2C18 
MDPAVALVLCLSCLFLLSLWRQSSGRGRLPSGPTPLPIIGNILQLDVKDMSKSLTNFSKV
YGPVFTVYFGLKPIVVLHGYEAVKEALIDHGEEFSGRGSFPVAEKVNKGLGILFSNGKRW
KEIRRFCLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNASPCDPTFILGCAPCNVICS
VIFHDRFDYKDQRFLNLMEKFNENLRILSSPWIQVCNNFPALIDYLPGSHNKIAENFAYI
KSYVLERIKEHQESLDMNSARDFIDCFLIKMEQEKHNQQSEFTVESLIATVTDMFGAGTE
TTSTTLRYGLLLLLKYPEVTAKVQEEIECVVGRNRSPCMQDRSHMPYTDAVVHEIQRYID
LLPTNLPHAVTCDVKFKNYLIPKGTTIITSLTSVLHNDKEFPNPEMFDPGHFLDKSGNFK
KSDYFMPFSAGKRMCMGEGLARMELFLFLTTILQNFNLKSQVDPKDIDITPIANAFGRVP
PLYQLCFIPV
Enzyme 104 Number of Residues 490
Enzyme 104 Molecular Weight 55710.1
Enzyme 104 Theoretical pI 7.22
Enzyme 104 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 104 General Function Involved in monooxygenase activity
Enzyme 104 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 104 Pathways
Enzyme 104 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein 189066652 Link Image
Enzyme 104 UniProtKB/Swiss-Prot ID P33260 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name CP2CI_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >1473 bp 
ATGGATCCAGCTGTGGCTCTGGTGCTCTGTCTCTCCTGTTTGTTTCTCCTTTCACTCTGG
AGGCAGAGCTCTGGAAGAGGGAGGCTCCCGTCTGGCCCCACTCCTCTCCCGATTATTGGA
AATATCCTGCAGTTAGATGTTAAGGACATGAGCAAATCCTTAACCAATTTCTCAAAAGTC
TATGGCCCTGTGTTCACTGTGTATTTTGGCCTGAAGCCCATTGTGGTGTTGCATGGATAT
GAAGCAGTGAAGGAGGCCCTGATTGATCATGGAGAGGAGTTTTCTGGAAGAGGAAGTTTT
CCAGTGGCTGAAAAAGTTAACAAAGGACTTGGAATCCTTTTCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTGCCTCATGACTCTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATCGAGGACCGTGTTCAAGAGGAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAT
GCCTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCT
GTTATTTTCCATGATCGATTTGATTATAAAGATCAGAGGTTTCTTAACTTGATGGAAAAA
TTCAATGAAAACCTCAGGATTCTGAGCTCTCCATGGATCCAGGTCTGCAATAATTTCCCT
GCTCTCATCGATTATCTCCCAGGAAGTCATAATAAAATAGCTGAAAATTTTGCTTACATT
AAAAGTTATGTATTGGAGAGAATAAAAGAACATCAAGAATCCCTGGACATGAACAGTGCT
CGGGACTTTATTGATTGTTTCCTGATCAAAATGGAACAGGAAAAGCACAATCAACAGTCT
GAATTTACTGTTGAAAGCTTGATAGCCACTGTAACTGATATGTTTGGGGCTGGAACAGAG
ACAACGAGCACCACTCTGAGATATGGACTCCTGCTCCTGCTGAAGTACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGAATGTGTAGTTGGCAGAAACCGGAGCCCCTGTATGCAG
GACAGGAGTCACATGCCCTACACAGATGCTGTGGTGCACGAGATCCAGAGATACATTGAC
CTCCTCCCCACCAACCTGCCCCATGCAGTGACCTGTGATGTTAAATTCAAAAACTACCTC
ATCCCCAAGGGCACGACCATAATAACATCCCTGACTTCTGTGCTGCACAATGACAAAGAA
TTCCCCAACCCAGAGATGTTTGACCCTGGCCACTTTCTGGATAAGAGTGGCAACTTTAAG
AAAAGTGACTACTTCATGCCTTTCTCAGCAGGAAAACGGATGTGTATGGGAGAGGGCCTG
GCCCGCATGGAGCTGTTTTTATTCCTGACCACCATTTTGCAGAACTTTAACCTGAAATCT
CAGGTTGACCCAAAGGATATTGACATCACCCCCATTGCCAATGCATTTGGTCGTGTGCCA
CCCTTGTACCAGCTCTGCTTCATTCCTGTCTGA
Enzyme 104 GenBank Gene ID AK313403 Link Image
Enzyme 104 GeneCard ID CYP2C18 Link Image
Enzyme 104 GenAtlas ID CYP2C18 Link Image
Enzyme 104 HGNC ID HGNC:2620 Link Image
Enzyme 104 Chromosome Location 1
Enzyme 104 Locus 10q24
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 General References
  1. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed Link Image]
  2. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome PH50IIC subfamily. Biochemistry. 1993 Feb 9;32(5):1390. [PubMed Link Image]
  3. de Morais SM, Schweikl H, Blaisdell J, Goldstein JA: Gene structure and upstream regulatory regions of human CYP2C9 and CYP2C18. Biochem Biophys Res Commun. 1993 Jul 15;194(1):194-201. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Archbold JK, Macdonald WA, Miles JJ, Brennan RM, Kjer-Nielsen L, McCluskey J, Burrows SR, Rossjohn J: Alloreactivity between disparate cognate and allogeneic pMHC-I complexes is the result of highly focused, peptide-dependent structural mimicry. J Biol Chem. 2006 Nov 10;281(45):34324-32. Epub 2006 Sep 8. [PubMed Link Image]
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 6847
Enzyme 105 Name Cytochrome P450 2F1
Enzyme 105 Synonyms
  1. CYPIIF1
Enzyme 105 Gene Name CYP2F1
Enzyme 105 Protein Sequence >Cytochrome P450 2F1 
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSK
EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDR
WKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIIC
SVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKC
LRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGT
KTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFA
DIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSF
KKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNL
PRPFQLCLRPR
Enzyme 105 Number of Residues 491
Enzyme 105 Molecular Weight 55500.6
Enzyme 105 Theoretical pI 7.40
Enzyme 105 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxygen binding
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 105 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 105 Specific Function May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3- methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine
Enzyme 105 Pathways
Enzyme 105 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • None
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 19743565 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID P24903 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name CP2F1_HUMAN Link Image
Enzyme 105 PDB ID Not Available
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >1476 bp 
ATGGACAGCATAAGCACAGCCATCTTACTCCTGCTCCTGGCTCTCGTCTGTCTGCTCCTG
ACCCTAAGCTCAAGAGATAAGGGAAAGCTGCCTCCGGGACCCAGACCCCTCTCAATCCTG
GGAAACCTGCTGCTGCTTTGCTCCCAAGACATGCTGACTTCTCTCACTAAGCTGAGCAAG
GAGTATGGCTCCATGTACACAGTGCACCTGGGACCCAGGCGGGTGGTGGTCCTCAGCGGG
TACCAAGCTGTGAAGGAGGCCCTGGTGGACCAGGGAGAGGAGTTTAGTGGCCGCGGTGAC
TACCCTGCCTTTTTCAACTTTACCAAGGGCAATGGCATCGCCTTCTCCAGTGGGGATCGA
TGGAAGGTCCTGAGACAGTTCTCTATCCAGATTCTACGGAATTTCGGGATGGGGAAGAGA
AGCATTGAGGAGCGAATCCTAGAGGAGGGCAGCTTCCTGCTGGCGGAGCTGCGGAAAACT
GAAGGCGAGCCCTTTGACCCCACGTTTGTGCTGAGTCGCTCAGTGTCCAACATTATCTGT
TCCGTGCTCTTCGGCAGCCGCTTCGACTATGATGATGAGCGTCTGCTCACCATTATCCGC
CTTATCAATGACAACTTCCAAATCATGAGCAGCCCCTGGGGCGAGTTGTACGACATCTTC
CCGAGCCTCCTGGACTGGGTGCCTGGGCCGCACCAACGCATCTTCCAGAACTTCAAGTGC
CTGAGAGACCTCATCGCCCACAGCGTCCACGACCACCAGGCCTCGCTAGACCCCAGATCT
CCCCGGGACTTCATCCAGTGCTTCCTCACCAAGATGGCAGAGGAGAAGGAGGACCCACTG
AGCCACTTCCACATGGATACCCTGCTGATGACCACACATAACCTGCTCTTTGGCGGCACC
AAGACGGTGAGCACCACGCTGCACCACGCCTTCCTGGCACTCATGAAGTACCCAAAAGTT
CAAGCCCGCGTGCAGGAGGAGATCGACCTCGTGGTGGGACGCGCGCGGCTGCCGGCGCTG
AAGGACCGCGCGGCCATGCCTTACACAGACGCGGTGATCCACGAGGTGCAGCGCTTTGCA
GACATCATCCCCATGAACTTGCCGCACCGCGTCACTAGGGACACGGCCTTTCGCGGCTTC
CTGATACCCAAGGGCACCGATGTCATCACCCTCCTTAACACCGTCCACTACGACCCCAGC
CAGTTCCTGACGCCCCAGGAGTTCAACCCCGAGCATTTTTTGGATGCCAATCAGTCCTTC
AAGAAGAGTCCAGCCTTCATGCCCTTCTCAGCTGGGCGCCGTCTGTGCCTGGGAGAGTCG
CTGGCGCGCATGGAGCTCTTTCTGTACCTCACCGCCATCCTGCAGAGCTTTTCGCTGCAG
CCGCTGGGTGCGCCCGAGGACATCGACCTGACCCCACTCAGCTCAGGTCTTGGCAATTTG
CCGCGGCCTTTCCAGCTGTGCCTGCGCCCGCGCTAA
Enzyme 105 GenBank Gene ID NM_000774.3 Link Image
Enzyme 105 GeneCard ID CYP2F1 Link Image
Enzyme 105 GenAtlas ID Not Available
Enzyme 105 HGNC ID Not Available
Enzyme 105 Chromosome Location 1
Enzyme 105 Locus 19q13.2
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Nhamburo PT, Kimura S, McBride OW, Kozak CA, Gelboin HV, Gonzalez FJ: The human CYP2F gene subfamily: identification of a cDNA encoding a new cytochrome P450, cDNA-directed expression, and chromosome mapping. Biochemistry. 1990 Jun 12;29(23):5491-9. [PubMed Link Image]
  2. Chen N, Whitehead SE, Caillat AW, Gavit K, Isphording DR, Kovacevic D, McCreary MB, Hoffman SM: Identification and cross-species comparisons of CYP2F subfamily genes in mammals. Mutat Res. 2002 Feb 20;499(2):155-61. [PubMed Link Image]
  3. Tournel G, Cauffiez C, Billaut-Laden I, Allorge D, Chevalier D, Bonnifet F, Mensier E, Lafitte JJ, Lhermitte M, Broly F, Lo-Guidice JM: Molecular analysis of the CYP2F1 gene: identification of a frequent non-functional allelic variant. Mutat Res. 2007 Apr 1;617(1-2):79-89. Epub 2007 Jan 25. [PubMed Link Image]
  4. Hakkola J, Pasanen M, Hukkanen J, Pelkonen O, Maenpaa J, Edwards RJ, Boobis AR, Raunio H: Expression of xenobiotic-metabolizing cytochrome P450 forms in human full-term placenta. Biochem Pharmacol. 1996 Feb 23;51(4):403-11. [PubMed Link Image]
  5. Thornton-Manning J, Appleton ML, Gonzalez FJ, Yost GS: Metabolism of 3-methylindole by vaccinia-expressed P450 enzymes: correlation of 3-methyleneindolenine formation and protein-binding. J Pharmacol Exp Ther. 1996 Jan;276(1):21-9. [PubMed Link Image]
  6. Lanza DL, Code E, Crespi CL, Gonzalez FJ, Yost GS: Specific dehydrogenation of 3-methylindole and epoxidation of naphthalene by recombinant human CYP2F1 expressed in lymphoblastoid cells. Drug Metab Dispos. 1999 Jul;27(7):798-803. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 6849
Enzyme 106 Name Cytochrome P450 2B6
Enzyme 106 Synonyms
  1. CYPIIB6
  2. Cytochrome P450 IIB1
Enzyme 106 Gene Name CYP2B6
Enzyme 106 Protein Sequence >Cytochrome P450 2B6 
MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFRE
KYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNR
WKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIIC
SIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQE
INAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGT
ETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFS
DLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGAL
KKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKI
PPTYQIRFLPR
Enzyme 106 Number of Residues 491
Enzyme 106 Molecular Weight 56277.8
Enzyme 106 Theoretical pI 8.44
Enzyme 106 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 106 General Function Involved in monooxygenase activity
Enzyme 106 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 106 Pathways
Enzyme 106 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • None
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein Not Available
Enzyme 106 UniProtKB/Swiss-Prot ID P20813 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name CP2B6_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >1476 bp 
ATGGAACTCAGCGTCCTCCTCTTCCTTGCACTCCTCACAGGACTCTTGCTACTCCTGGTT
CAGCGCCACCCTAACACCCATGACCGCCTCCCACCAGGGCCCCGCCCTCTGCCCCTTTTG
GGAAACCTTCTGCAGATGGATAGAAGAGGCCTACTCAAATCCTTTCTGAGGTTCCGAGAG
AAATATGGGGACGTCTTCACGGTACACCTGGGACCGAGGCCCGTGGTCATGCTGTGTGGA
GTAGAGGCCATACGGGAGGCCCTTGTGGACAAGGCTGAGGCCTTCTCTGGCCGGGGAAAA
ATCGCCATGGTCGACCCATTCTTCCGGGGATATGGTGTGATCTTTGCCAATGGAAACCGC
TGGAAGGTGCTTCGGCGATTCTCTGTGACCACTATGAGGGACTTCGGGATGGGAAAGCGG
AGTGTGGAGGAGCGGATTCAGGAGGAGGCTCAGTGTCTGATAGAGGAGCTTCGGAAATCC
AAGGGGGCCCTCATGGACCCCACCTTCCTCTTCCAGTCCATTACCGCCAACATCATCTGC
TCCATCGTCTTTGGAAAACGATTCCACTACCAAGATCAAGAGTTCCTGAAGATGCTGAAC
TTGTTCTACCAGACTTTTTCACTCATCAGCTCTGTATTCGGCCAGCTGTTTGAGCTCTTC
TCTGGCTTCTTGAAATACTTTCCTGGGGCACACAGGCAAGTTTACAAAAACCTGCAGGAA
ATCAATGCTTACATTGGCCACAGTGTGGAGAAGCACCGTGAAACCCTGGACCCCAGCGCC
CCCAAGGACCTCATCGACACCTACCTGCTCCACATGGAAAAAGAGAAATCCAACGCACAC
AGTGAATTCAGCCACCAGAACCTCAACCTCAACACGCTCTCGCTCTTCTTTGCTGGCACT
GAGACCACCAGCACCACTCTCCGCTACGGCTTCCTGCTCATGCTCAAATACCCTCATGTT
GCAGAGAGAGTCTACAGGGAGATTGAACAGGTGATTGGCCCACATCGCCCTCCAGAGCTT
CATGACCGAGCCAAAATGCCATACACAGAGGCAGTCATCTATGAGATTCAGAGATTTTCC
GACCTTCTCCCCATGGGTGTGCCCCACATTGTCACCCAACACACCAGCTTCCGAGGGTAC
ATCATCCCCAAGGACACAGAAGTATTTCTCATCCTGAGCACTGCTCTCCATGACCCACAC
TACTTTGAAAAACCAGACGCCTTCAATCCTGACCACTTTCTGGATGCCAATGGGGCACTG
AAAAAGACTGAAGCTTTTATCCCCTTCTCCTTAGGGAAGCGGATTTGTCTTGGTGAAGGC
ATCGCCCGTGCGGAATTGTTCCTCTTCTTCACCACCATCCTCCAGAACTTCTCCATGGCC
AGCCCCGTGGCCCCAGAAGACATCGATCTGACACCCCAGGAGTGTGGTGTGGGCAAAATA
CCCCCAACATACCAGATCCGCTTCCTGCCCCGCTGA
Enzyme 106 GenBank Gene ID M29874 Link Image
Enzyme 106 GeneCard ID CYP2B6 Link Image
Enzyme 106 GenAtlas ID CYP2B6 Link Image
Enzyme 106 HGNC ID HGNC:2615 Link Image
Enzyme 106 Chromosome Location 1
Enzyme 106 Locus 19q13.2
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Yamano S, Nhamburo PT, Aoyama T, Meyer UA, Inaba T, Kalow W, Gelboin HV, McBride OW, Gonzalez FJ: cDNA cloning and sequence and cDNA-directed expression of human P450 IIB1: identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver. Biochemistry. 1989 Sep 5;28(18):7340-8. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Miles JS, McLaren AW, Wolf CR: Alternative splicing in the human cytochrome P450IIB6 gene generates a high level of aberrant messages. Nucleic Acids Res. 1989 Oct 25;17(20):8241-55. [PubMed Link Image]
  4. Thum T, Borlak J: Gene expression in distinct regions of the heart. Lancet. 2000 Mar 18;355(9208):979-83. [PubMed Link Image]
  5. Ariyoshi N, Miyazaki M, Toide K, Sawamura Yi, Kamataki T: A single nucleotide polymorphism of CYP2b6 found in Japanese enhances catalytic activity by autoactivation. Biochem Biophys Res Commun. 2001 Mar;281(5):1256-60. [PubMed Link Image]
  6. Lang T, Klein K, Fischer J, Nussler AK, Neuhaus P, Hofmann U, Eichelbaum M, Schwab M, Zanger UM: Extensive genetic polymorphism in the human CYP2B6 gene with impact on expression and function in human liver. Pharmacogenetics. 2001 Jul;11(5):399-415. [PubMed Link Image]
  7. Jinno H, Tanaka-Kagawa T, Ohno A, Makino Y, Matsushima E, Hanioka N, Ando M: Functional characterization of cytochrome P450 2B6 allelic variants. Drug Metab Dispos. 2003 Apr;31(4):398-403. [PubMed Link Image]
  8. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
  9. Lamba V, Lamba J, Yasuda K, Strom S, Davila J, Hancock ML, Fackenthal JD, Rogan PK, Ring B, Wrighton SA, Schuetz EG: Hepatic CYP2B6 expression: gender and ethnic differences and relationship to CYP2B6 genotype and CAR (constitutive androstane receptor) expression. J Pharmacol Exp Ther. 2003 Dec;307(3):906-22. Epub 2003 Oct 9. [PubMed Link Image]
  10. Lang T, Klein K, Richter T, Zibat A, Kerb R, Eichelbaum M, Schwab M, Zanger UM: Multiple novel nonsynonymous CYP2B6 gene polymorphisms in Caucasians: demonstration of phenotypic null alleles. J Pharmacol Exp Ther. 2004 Oct;311(1):34-43. Epub 2004 Jun 9. [PubMed Link Image]
  11. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 6850
Enzyme 107 Name Cytochrome P450 3A5
Enzyme 107 Synonyms
  1. CYPIIIA5
  2. Cytochrome P450 HLp2
  3. Cytochrome P450-PCN3
Enzyme 107 Gene Name CYP3A5
Enzyme 107 Protein Sequence >Cytochrome P450 3A5 
MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKF
DTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISL
AEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYS
MDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSL
FPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSI
IFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVV
NETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFS
KKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQG
LLQPEKPIVLKVDSRDGTLSGE
Enzyme 107 Number of Residues 502
Enzyme 107 Molecular Weight 57108.1
Enzyme 107 Theoretical pI 9.09
Enzyme 107 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 107 General Function Involved in monooxygenase activity
Enzyme 107 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 107 Pathways
Enzyme 107 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 41393491 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID P20815 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name CP3A5_HUMAN Link Image
Enzyme 107 PDB ID Not Available
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >1509 bp 
ATGGACCTCATCCCAAATTTGGCGGTGGAAACCTGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGGACCCGTACACATGGACTTTTTAAGAGACTGGGAATTCCAGGG
CCCACACCTCTGCCTTTGTTGGGAAATGTTTTGTCCTATCGTCAGGGTCTCTGGAAATTT
GACACAGAGTGCTATAAAAAGTATGGAAAAATGTGGGGAACGTATGAAGGTCAACTCCCT
GTGCTGGCCATCACAGATCCCGACGTGATCAGAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAATCGAAGGTCTTTAGGCCCAGTGGGATTTATGAAAAGTGCCATCTCTTTA
GCTGAGGATGAAGAATGGAAGAGAATACGGTCATTGCTGTCTCCAACCTTCACCAGCGGA
AAACTCAAGGAGATGTTCCCCATCATTGCCCAGTATGGAGATGTATTGGTGAGAAACTTG
AGGCGGGAAGCAGAGAAAGGCAAGCCTGTCACCTTGAAAGACATCTTTGGGGCCTACAGC
ATGGATGTGATTACTGGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAGAGCACTAAGAAGTTCCTAAAATTTGGTTTCTTAGATCCATTATTT
CTCTCAATAATACTCTTTCCATTCCTTACCCCAGTTTTTGAAGCATTAAATGTCTCTCTG
TTTCCAAAAGATACCATAAATTTTTTAAGTAAATCTGTAAACAGAATGAAGAAAAGTCGC
CTCAACGACAAACAAAAGCACCGACTAGATTTCCTTCAGCTGATGATTGACTCCCAGAAT
TCGAAAGAAACTGAGTCCCACAAAGCTCTGTCTGATCTGGAGCTCGCAGCCCAGTCAATA
ATCTTCATTTTTGCTGGCTATGAAACCACCAGCAGTGTTCTTTCCTTCACTTTATATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAAAAGGAGATTGATGCAGTTTTGCCC
AATAAGGCACCACCTACCTATGATGCCGTGGTACAGATGGAGTACCTTGACATGGTGGTG
AATGAAACACTCAGATTATTCCCAGTTGCTATTAGACTTGAGAGGACTTGCAAGAAAGAT
GTTGAAATCAATGGGGTATTCATTCCCAAAGGGTCAATGGTGGTGATTCCAACTTATGCT
CTTCACCATGACCCAAAGTACTGGACAGAGCCTGAGGAGTTCCGCCCTGAAAGGTTCAGT
AAGAAGAAGGACAGCATAGATCCTTACATATACACACCCTTTGGAACTGGACCCAGAAAC
TGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTTCAG
AACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCTTGAAATTAGACACGCAAGGA
CTTCTTCAACCAGAAAAACCCATTGTTCTAAAGGTGGATTCAAGAGATGGAACCCTAAGT
GGAGAATGA
Enzyme 107 GenBank Gene ID AC005020 Link Image
Enzyme 107 GeneCard ID CYP3A5 Link Image
Enzyme 107 GenAtlas ID CYP3A5 Link Image
Enzyme 107 HGNC ID HGNC:2638 Link Image
Enzyme 107 Chromosome Location 7
Enzyme 107 Locus 7q21.1
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 General References
  1. Aoyama T, Yamano S, Waxman DJ, Lapenson DP, Meyer UA, Fischer V, Tyndale R, Inaba T, Kalow W, Gelboin HV, et al.: Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine. J Biol Chem. 1989 Jun 25;264(18):10388-95. [PubMed Link Image]
  2. Schuetz JD, Molowa DT, Guzelian PS: Characterization of a cDNA encoding a new member of the glucocorticoid-responsive cytochromes P450 in human liver. Arch Biochem Biophys. 1989 Nov 1;274(2):355-65. [PubMed Link Image]
  3. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gellner K, Eiselt R, Hustert E, Arnold H, Koch I, Haberl M, Deglmann CJ, Burk O, Buntefuss D, Escher S, Bishop C, Koebe HG, Brinkmann U, Klenk HP, Kleine K, Meyer UA, Wojnowski L: Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics. 2001 Mar;11(2):111-21. [PubMed Link Image]
  7. Schuetz JD, Schuetz EG, Thottassery JV, Guzelian PS, Strom S, Sun D: Identification of a novel dexamethasone responsive enhancer in the human CYP3A5 gene and its activation in human and rat liver cells. Mol Pharmacol. 1996 Jan;49(1):63-72. [PubMed Link Image]
  8. Jounaidi Y, Guzelian PS, Maurel P, Vilarem MJ: Sequence of the 5'-flanking region of CYP3A5: comparative analysis with CYP3A4 and CYP3A7. Biochem Biophys Res Commun. 1994 Dec 30;205(3):1741-7. [PubMed Link Image]
  9. Jounaidi Y, Hyrailles V, Gervot L, Maurel P: Detection of CYP3A5 allelic variant: a candidate for the polymorphic expression of the protein? Biochem Biophys Res Commun. 1996 Apr 16;221(2):466-70. [PubMed Link Image]
  10. Chou FC, Tzeng SJ, Huang JD: Genetic polymorphism of cytochrome P450 3A5 in Chinese. Drug Metab Dispos. 2001 Sep;29(9):1205-9. [PubMed Link Image]
  11. Lee SJ, Usmani KA, Chanas B, Ghanayem B, Xi T, Hodgson E, Mohrenweiser HW, Goldstein JA: Genetic findings and functional studies of human CYP3A5 single nucleotide polymorphisms in different ethnic groups. Pharmacogenetics. 2003 Aug;13(8):461-72. [PubMed Link Image]
  12. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 6851
Enzyme 108 Name Cytochrome P450 1A1
Enzyme 108 Synonyms
  1. CYPIA1
  2. Cytochrome P450 form 6
  3. Cytochrome P450-C
  4. Cytochrome P450-P1
Enzyme 108 Gene Name CYP1A1
Enzyme 108 Protein Sequence >Cytochrome P450 1A1 
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
Enzyme 108 Number of Residues 512
Enzyme 108 Molecular Weight 58164.8
Enzyme 108 Theoretical pI 8.47
Enzyme 108 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 108 General Function Involved in monooxygenase activity
Enzyme 108 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 108 Pathways
Enzyme 108 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 181276 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID P04798 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name CP1A1_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >1539 bp 
ATGCTTTTCCCAATCTCCATGTCGGCCACGGAGTTTCTTCTGGCCTCTGTCATCTTCTGT
CTGGTATTCTGGGTAATGAGGGCCTCAAGACCTCAGGTCCCCAAAGGCCTGAAGAATCCA
CCAGGGCCATGGGGCTGGCCTCTGATTGGGCACATGCTGACCCTGGGAAAGAACCCGCAC
CTGGCACTGTCAAGGATGAGCCAGCAGTATGGGGACGTGCTGCAGATCCGAATTGGCTCC
ACACCCGTGGTGGTGCTGAGCGGCCTGGACACCATCCGGCAGGCCCTGGTGCGGCAGGGC
GATGATTTCAAGGGCCGGCCCGACCTCTACACCTTCACCCTCATCAGTAATGGTCAGAGC
ATGTCCTTCAGCCCAGACTCTGGACCAGTGTGGGCTGCCCGCCGGCGCCTGGCCCAGAAT
GGCCTGAAAAGTTTCTCCATTGCCTCTGACCCAGCCTCCTCAACCTCCTGCTACCTGGAA
GAGCATGTGAGCAAGGAGGCTGAGGTCCTGATAAGCACGTTGCAGGAGCTGATGGCAGGG
CCTGGGCACTTTAACCCCTACAGGTATGTGGTGGTATCAGTGACCAATGTCATCTGTGCC
ATTTGCTTTGGCCGGCGCTATGACCACAACCACCAAGAACTGCTTAGCCTAGTCAACCTG
AATAATAATTTCGGGGAGGTGGTTGGCTCTGGAAACCCAGCTGAGTTCATCCCTATTCTT
CGCTACCTACCCAACCCTTCCCTGAATGCCTTCAAGGACCTGAATGAGAAGTTCTACAGC
TTCATGCAGAAGATGGTCAAGGAGCACTACAAAACCTTTGAGAAGGGCCACATCCGGGAC
ATCACAGACAGCCTGATTGAGCACTGTCAGGAGAAGCAGCTGGATGAGAACGCCAATGTC
CAGCTGTCAGATGAGAAGATCATTAACATCGTCTTGGACCTCTTTGGAGCTGGGTTTGAC
ACAGTCACAACTGCTATCTCCTGGAGCCTCATGTATTTGGTGATGAACCCCAGGGTACAG
AGAAAGATCCAAGAGGAGCTAGACACAGTGATTGGCAGGTCACGGCGGCCCCGGCTCTCT
GACAGATCCCATCTGCCCTATATGGAGGCCTTCATCCTGGAGACCTTCCGACACTCTTCC
TTCGTCCCCTTCACCATCCCCCACAGCACAACAAGAGACACAAGTTTGAAAGGCTTTTAC
ATCCCCAAGGGGCGTTGTGTCTTTGTAAACCAGTGGCAGATCAACCATGACCAGAAGCTA
TGGGTCAACCCATCTGAGTTCCTACCTGAACGGTTTCTCACCCCTGATGGTGCTATCGAC
AAGGTGTTAAGTGAGAAGGTGATTATCTTTGGCATGGGCAAGCGGAAGTGTATCGGTGAG
ACCGTTGCCCGCTGGGAGGTCTTTCTCTTCCTGGCTATCCTGCTGCAACGGGTGGAATTC
AGCGTGCCACTGGGCGTGAAGGTGGACATGACCCCCATCTATGGGCTAACCATGAAGCAT
GCCTGCTGTGAGCACTTCCAAATGCAGCTGCGCTCTTAG
Enzyme 108 GenBank Gene ID K03191 Link Image
Enzyme 108 GeneCard ID CYP1A1 Link Image
Enzyme 108 GenAtlas ID CYP1A1 Link Image
Enzyme 108 HGNC ID HGNC:2595 Link Image
Enzyme 108 Chromosome Location 1
Enzyme 108 Locus 15q24.1
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. Jaiswal AK, Gonzalez FJ, Nebert DW: Human P1-450 gene sequence and correlation of mRNA with genetic differences in benzo[a]pyrene metabolism. Nucleic Acids Res. 1985 Jun 25;13(12):4503-20. [PubMed Link Image]
  2. Jaiswal AK, Gonzalez FJ, Nebert DW: Human dioxin-inducible cytochrome P1-450: complementary DNA and amino acid sequence. Science. 1985 Apr 5;228(4695):80-3. [PubMed Link Image]
  3. Kawajiri K, Watanabe J, Gotoh O, Tagashira Y, Sogawa K, Fujii-Kuriyama Y: Structure and drug inducibility of the human cytochrome P-450c gene. Eur J Biochem. 1986 Sep 1;159(2):219-25. [PubMed Link Image]
  4. Corchero J, Pimprale S, Kimura S, Gonzalez FJ: Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation. Pharmacogenetics. 2001 Feb;11(1):1-6. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yun CH, Park HJ, Kim SJ, Kim HK: Identification of cytochrome P450 1A1 in human brain. Biochem Biophys Res Commun. 1998 Feb 24;243(3):808-10. [PubMed Link Image]
  7. Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH: Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. DNA. 1985 Oct;4(5):395-400. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Hayashi S, Watanabe J, Nakachi K, Kawajiri K: Genetic linkage of lung cancer-associated MspI polymorphisms with amino acid replacement in the heme binding region of the human cytochrome P450IA1 gene. J Biochem (Tokyo). 1991 Sep;110(3):407-11. [PubMed Link Image]
  10. Cascorbi I, Brockmoller J, Roots I: A C4887A polymorphism in exon 7 of human CYP1A1: population frequency, mutation linkages, and impact on lung cancer susceptibility. Cancer Res. 1996 Nov 1;56(21):4965-9. [PubMed Link Image]
  11. Smart J, Daly AK: Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor and GSTM1 polymorphisms. Pharmacogenetics. 2000 Feb;10(1):11-24. [PubMed Link Image]
  12. Chevalier D, Allorge D, Lo-Guidice JM, Cauffiez C, Lhermitte M, Lafitte JJ, Broly F: Detection of known and two novel (M331I and R464S) missense mutations in the human CYP1A1 gene in a French Caucasian population. Hum Mutat. 2001 Apr;17(4):355. [PubMed Link Image]
  13. Saito T, Egashira M, Kiyotani K, Fujieda M, Yamazaki H, Kiyohara C, Kunitoh H, Kamataki T: Novel nonsynonymous polymorphisms of the CYP1A1 gene in Japanese. Drug Metab Pharmacokinet. 2003;18(3):218-21. [PubMed Link Image]
  14. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  15. Jiang Z, Dalton TP, Jin L, Wang B, Tsuneoka Y, Shertzer HG, Deka R, Nebert DW: Toward the evaluation of function in genetic variability: characterizing human SNP frequencies and establishing BAC-transgenic mice carrying the human CYP1A1_CYP1A2 locus. Hum Mutat. 2005 Feb;25(2):196-206. [PubMed Link Image]
  16. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 6852
Enzyme 109 Name Cytochrome P450 2A13
Enzyme 109 Synonyms
  1. CYPIIA13
Enzyme 109 Gene Name CYP2A13
Enzyme 109 Protein Sequence >Cytochrome P450 2A13 
MLASGLLLVTLLACLTVMVLMSVWRQRKSRGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSN
GERAKQLRRFSIATLRGFGVGKRGIEERIQEEAGFLIDALRGTHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKE
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFF
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQ
RFGDMLPMGLAHRVNKDTKFRDFFLPKGTEVFPMLGSVLRDPRFFSNPRDFNPQHFLDKK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Enzyme 109 Number of Residues 494
Enzyme 109 Molecular Weight 56687.1
Enzyme 109 Theoretical pI 9.78
Enzyme 109 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 109 General Function Involved in monooxygenase activity
Enzyme 109 Specific Function Exhibits a coumarin 7-hydroxylase activity. Active in the metabolic activation of hexamethylphosphoramide, N,N- dimethylaniline, 2'-methoxyacetophenone, N- nitrosomethylphenylamine, and the tobacco-specific carcinogen, 4- (methylnitrosamino)-1-(3-pyridyl)-1-butanone. Possesses phenacetin O-deethylation activity
Enzyme 109 Pathways
Enzyme 109 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 109 Pfam Domain Function
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • None
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein Not Available
Enzyme 109 UniProtKB/Swiss-Prot ID Q16696 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name CP2AD_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >1485 bp 
ATGCTGGCCTCAGGGCTGCTTCTGGTGACCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCAGTCTGGCGGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCATTG
CCCTTCATTGGAAACTACCTGCAGCTGAACACAGAGCAGATGTACAACTCCCTCATGAAG
ATCAGTGAGCGCTATGGCCCTGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGCGGACATGATGCCGTCAAGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAGGCCACCTTCGACTGGCTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCGGCGCTTCTCCATCGCCACCCTAAGGGGTTTTGGCGTG
GGCAAGCGCGGCATCGAGGAACGCATCCAGGAGGAGGCGGGCTTCCTCATCGACGCCCTC
CGGGGCACGCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGTTGCGCATGATGCTGGGAAGCTTCCAGTTCACGGCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGGAG
CTGCAAGGGCTGGAGGACTTCATCGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACGGGACTTCATCGACTCCTTTCTCATCCGCATGCAGGAGGAGGAGAAG
AACCCCAACACAGAGTTCTACTTGAAGAACCTGGTGATGACCACCCTGAACCTCTTCTTT
GCGGGCACTGAGACCGTGAGCACCACCCTGCGCTACGGTTTCCTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGGCCAAGATGCCCTACACAGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACATGCTCCCCATGGGTTTGGCCCACAGGGTCAACAAGGACACCAAGTTT
CGGGATTTCTTCCTCCCTAAGGGCACTGAAGTGTTCCCTATGCTGGGCTCCGTGCTGAGA
GACCCCAGGTTCTTCTCCAACCCCCGGGACTTCAATCCCCAGCACTTCCTGGATAAGAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGTACTGTTTT
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCATCATGCAGAACTTT
CGCTTCAAGTCCCCTCAGTCGCCTAAGGATATCGACGTGTCCCCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 109 GenBank Gene ID AF209774 Link Image
Enzyme 109 GeneCard ID CYP2A13 Link Image
Enzyme 109 GenAtlas ID CYP2A13 Link Image
Enzyme 109 HGNC ID HGNC:2608 Link Image
Enzyme 109 Chromosome Location 1
Enzyme 109 Locus 19q13.2
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References
  1. Fernandez-Salguero P, Hoffman SM, Cholerton S, Mohrenweiser H, Raunio H, Rautio A, Pelkonen O, Huang JD, Evans WE, Idle JR, et al.: A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. Am J Hum Genet. 1995 Sep;57(3):651-60. [PubMed Link Image]
  2. Su T, Bao Z, Zhang QY, Smith TJ, Hong JY, Ding X: Human cytochrome P450 CYP2A13: predominant expression in the respiratory tract and its high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. Cancer Res. 2000 Sep 15;60(18):5074-9. [PubMed Link Image]
  3. Cauffiez C, Lo-Guidice JM, Quaranta S, Allorge D, Chevalier D, Cenee S, Hamdan R, Lhermitte M, Lafitte JJ, Libersa C, Colombel JF, Stucker I, Broly F: Genetic polymorphism of the human cytochrome CYP2A13 in a French population: implication in lung cancer susceptibility. Biochem Biophys Res Commun. 2004 Apr 30;317(2):662-9. [PubMed Link Image]
  4. DeVore NM, Smith BD, Urban MJ, Scott EE: Key residues controlling phenacetin metabolism by human cytochrome P450 2A enzymes. Drug Metab Dispos. 2008 Dec;36(12):2582-90. Epub 2008 Sep 8. [PubMed Link Image]
  5. Sansen S, Hsu MH, Stout CD, Johnson EF: Structural insight into the altered substrate specificity of human cytochrome P450 2A6 mutants. Arch Biochem Biophys. 2007 Aug 15;464(2):197-206. Epub 2007 May 11. [PubMed Link Image]
  6. Smith BD, Sanders JL, Porubsky PR, Lushington GH, Stout CD, Scott EE: Structure of the human lung cytochrome P450 2A13. J Biol Chem. 2007 Jun 8;282(23):17306-13. Epub 2007 Apr 11. [PubMed Link Image]
  7. Zhang X, Su T, Zhang QY, Gu J, Caggana M, Li H, Ding X: Genetic polymorphisms of the human CYP2A13 gene: identification of single-nucleotide polymorphisms and functional characterization of an Arg257Cys variant. J Pharmacol Exp Ther. 2002 Aug;302(2):416-23. [PubMed Link Image]
  8. Fujieda M, Yamazaki H, Kiyotani K, Muroi A, Kunitoh H, Dosaka-Akita H, Sawamura Y, Kamataki T: Eighteen novel polymorphisms of the CYP2A13 gene in Japanese. Drug Metab Pharmacokinet. 2003;18(1):86-90. [PubMed Link Image]
  9. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 6853
Enzyme 110 Name Cytochrome P450 3A7
Enzyme 110 Synonyms
  1. CYPIIIA7
  2. Cytochrome P450-HFLA
Enzyme 110 Gene Name CYP3A7
Enzyme 110 Protein Sequence >Cytochrome P450 3A7 
MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTF
DMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISI
AEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYS
MDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITV
FPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSI
IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVV
NETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWREPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG
GLLLTEKPIVLKAESRDETVSGA
Enzyme 110 Number of Residues 503
Enzyme 110 Molecular Weight 57525.0
Enzyme 110 Theoretical pI 9.59
Enzyme 110 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 110 General Function Involved in monooxygenase activity
Enzyme 110 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 110 Pathways
Enzyme 110 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein 11177455 Link Image
Enzyme 110 UniProtKB/Swiss-Prot ID P24462 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name CP3A7_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence >1512 bp 
ATGGCTCTCATCCCAGACTTGGCCATGGAAACCTGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGAACCCATTCACATGGACTTTTTAAGAAGCTTGGAATTCCAGGG
CCCACACCTCTGCCTTTTTTGGGAAATATTTTGTCCTACCATAAGGGCTTTTGTATGTTT
GACATGGAATGTCATAAAAAGTATGGAAAAGTGTGGGGCTTTTATGATGGTCAACAGCCT
GTGCTGGCTATCACAGATCCTGACATGATCAAAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAACCGGAGGCCTTTTGGTCCAGTGGGATTTATGAAAAGTGCCATCTCTATA
GCTGAGGATGAAGAATGGAAGAGATTACGATCATTGCTGTCTCCAACCTTCACCAGTGGA
AAACTCAAGGAGATGGTCCCTATCATTGCCCAGTATGGAGATGTGTTGGTGAGAAATCTG
AGGCGGGAAGCAGAGACAGGCAAGCCTGTCACCTTGAAAGACGTCTTTGGGGCCTACAGC
ATGGATGTGATCACTAGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAAAACACCAAGAAGCTTTTAAGATTTGATTTTTTGGATCCATTCTTT
CTCTCAATAACAGTCTTTCCATTCCTCATCCCAATTCTTGAAGTATTAAATATCTGTGTG
TTTCCAAGAGAAGTTACAAATTTTTTAAGAAAATCTGTAAAAAGGATGAAAGAAAGTCGC
CTCGAAGATACACAAAAGCACCGAGTGGATTTCCTTCAGCTGATGATTGACTCTCAGAAT
TCAAAAGAAACTGAGTCCCACAAAGCTCTGTCCGATCTGGAGCTCGTGGCCCAATCAATT
ATCTTTATTTTTGCTGGCTATGAAACCACGAGCAGTGTTCTCTCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAAATTGATGCAGTTTTACCC
AATAAGGCACCACCCACCTATGATACTGTGCTACAGATGGAGTATCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAATTGCTATGAGACTTGAGAGGGTCTGCAAAAAAGAT
GTTGAGATCAATGGGATGTTCATTCCCAAAGGGGTGGTGGTGATGATTCCAAGCTATGCT
CTTCACCGTGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCCTCCCTGAAAGATTCAGC
AAGAAGAACAAGGACAACATAGATCCTTACATATACACACCCTTTGGAAGTGGACCCAGA
AACTGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTT
CAGAACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCCTGAAATTAAGCTTAGGA
GGACTTCTTCAACCAGAAAAACCCGTTGTTCTAAAGGTTGAGTCAAGGGATGGCACCGTA
AGTGGAGCCTGA
Enzyme 110 GenBank Gene ID AF280107 Link Image
Enzyme 110 GeneCard ID CYP3A7 Link Image
Enzyme 110 GenAtlas ID CYP3A7 Link Image
Enzyme 110 HGNC ID HGNC:2640 Link Image
Enzyme 110 Chromosome Location 7
Enzyme 110 Locus 7q21-q22.1
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References
  1. Komori M, Nishio K, Ohi H, Kitada M, Kamataki T: Molecular cloning and sequence analysis of cDNA containing the entire coding region for human fetal liver cytochrome P-450. J Biochem (Tokyo). 1989 Feb;105(2):161-3. [PubMed Link Image]
  2. Gellner K, Eiselt R, Hustert E, Arnold H, Koch I, Haberl M, Deglmann CJ, Burk O, Buntefuss D, Escher S, Bishop C, Koebe HG, Brinkmann U, Klenk HP, Kleine K, Meyer UA, Wojnowski L: Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics. 2001 Mar;11(2):111-21. [PubMed Link Image]
  3. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wrighton SA, Vandenbranden M: Isolation and characterization of human fetal liver cytochrome P450HLp2: a third member of the P450III gene family. Arch Biochem Biophys. 1989 Jan;268(1):144-51. [PubMed Link Image]
  6. Komori M, Nishio K, Fujitani T, Ohi H, Kitada M, Mima S, Itahashi K, Kamataki T: Isolation of a new human fetal liver cytochrome P450 cDNA clone: evidence for expression of a limited number of forms of cytochrome P450 in human fetal livers. Arch Biochem Biophys. 1989 Jul;272(1):219-25. [PubMed Link Image]
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 6854
Enzyme 111 Name Cytochrome P450 4B1
Enzyme 111 Synonyms
  1. CYPIVB1
  2. Cytochrome P450-HP
Enzyme 111 Gene Name CYP4B1
Enzyme 111 Protein Sequence >Cytochrome P450 4B1 
MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALE
IQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQ
WIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDI
FCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLT
PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKL
SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDL
GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWP
DPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP
SRLPIKMPQLVLRSKNGFHLHLKPLGPGSGK
Enzyme 111 Number of Residues 511
Enzyme 111 Molecular Weight 58990.6
Enzyme 111 Theoretical pI 8.39
Enzyme 111 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 111 General Function Involved in monooxygenase activity
Enzyme 111 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 111 Pathways
Enzyme 111 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 20067171 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID P13584 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name CP4B1_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >1536 bp 
ATGGTGCCCAGCTTCCTCTCCCTGAGCTTCTCCTCCTTGGGCCTGTGGGCTTCTGGGCTG
ATCTTGGTCTTAGGCTTTCTCAAGCTCATCCACCTGCTGCTGCGGAGGCAGACGTTGGCT
AAGGCTATGGACAAATTCCCAGGGCCTCCCACCCACTGGCTTTTTGGACATGCCCTCGAG
ATCCAGGAGACGGGGAGCCTGGACAAAGTGGTGTCCTGGGCCCACCAGTTCCCGTATGCC
CACCCACTCTGGTTCGGACAGTTCATTGGCTTCCTGAACATCTATGAGCCTGACTATGCC
AAAGCTGTGTACAGCCGTGGGGACCCTAAGGCCCCTGATGTGTATGACTTCTTCCTCCAG
TGGATTGGGAGAGGCCTGCTGGTTCTTGAGGGGCCCAAGTGGTTGCAGCACCGCAAGCTG
CTCACACCTGGCTTTCATTATGATGTGCTGAAGCCCTATGTGGCCGTGTTCACTGAGTCT
ACACGTATCATGCTGGACAAGTGGGAAGAGAAAGCTCGGGAGGGTAAGTCCTTTGACATC
TTCTGCGATGTGGGTCACATGGCGCTGAACACACTCATGAAGTGCACCTTTGGAAGAGGA
GACACCGGCCTGGGCCACAGGGACAGCAGCTACTACCTTGCAGTCAGCGATCTCACTCTG
TTGATGCAGCAGCGCCTTGTGTCCTTCCAGTACCATAATGACTTCATCTACTGGCTCACC
CCACATGGCCGCCGCTTCCTGCGGGCCTGCCAGGTGGCCCATGACCATACAGACCAGGTC
ATCAGGGAGCGGAAGGCAGCCCTGCAGGATGAGAAGGTGCGGAAGAAGATCCAGAACCGG
AGGCACCTGGACTTCCTGGACATTCTCCTGGGTGCCCGGGATGAAGATGACATCAAACTG
TCAGATGCAGACCTCCGGGCTGAAGTGGACACATTCATGTTTGAAGGCCATGACACCACC
ACCAGTGGTATCTCCTGGTTTCTCTACTGCATAGCCCTGTACCCTGAGCACCAGCATCGT
TGTAGAGAGGAGGTCCGCGAGATCCTAGGGGACCAGGACTTCTTCCAGTGGGATGATCTG
GGCAAAATGACTTATCTGACCATGTGCATCAAGGAGAGCTTCCGCCTCTACCCACCTGTG
CCCCAGGTGTACCGCCAGCTCAGCAAGCCTGTCACCTTTGTGGATGGCCGGTCTCTACCT
GCAGGAAGCCTGATCTCTATGCATATCTATGCCCTCCATAGGAACAGTGCTGTATGGCCC
GACCCTGAGGTCTTTGACTCTCTGCGCTTTTCCACTGAGAATGCATCCAAACGCCATCCC
TTTGCCTTTATGCCCTTCTCTGCTGGGCCCAGGAACTGCATTGGGCAGCAGTTTGCCATG
AGTGAGATGAAGGTGGTCACAGCCATGTGCTTGCTCCGCTTTGAGTTCTCTCTGGACCCC
TCACGGCTGCCCATCAAGATGCCCCAGCTTGTCCTGCGCTCCAAGAATGGCTTTCACCTC
CACCTGAAGCCACTGGGCCCTGGGTCTGGGAAGTAG
Enzyme 111 GenBank Gene ID AF491285 Link Image
Enzyme 111 GeneCard ID CYP4B1 Link Image
Enzyme 111 GenAtlas ID CYP4B1 Link Image
Enzyme 111 HGNC ID HGNC:2644 Link Image
Enzyme 111 Chromosome Location 1
Enzyme 111 Locus 1p34-p12
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References
  1. Nhamburo PT, Gonzalez FJ, McBride OW, Gelboin HV, Kimura S: Identification of a new P450 expressed in human lung: complete cDNA sequence, cDNA-directed expression, and chromosome mapping. Biochemistry. 1989 Oct 3;28(20):8060-6. [PubMed Link Image]
  2. Yokotani N, Sogawa K, Matsubara S, Gotoh O, Kusunose E, Kusunose M, Fujii-Kuriyama Y: cDNA cloning of cytochrome P-450 related to P-450p-2 from the cDNA library of human placenta. Gene structure and expression. Eur J Biochem. 1990 Jan 12;187(1):23-9. [PubMed Link Image]
  3. Lo-Guidice JM, Allorge D, Cauffiez C, Chevalier D, Lafitte JJ, Lhermitte M, Broly F: Genetic polymorphism of the human cytochrome P450 CYP4B1: evidence for a non-functional allelic variant. Pharmacogenetics. 2002 Jul;12(5):367-74. [PubMed Link Image]
  4. Carr BA, Ramakanth S, Dannan GA, Yost GS: Characterization of pulmonary CYP4B2, specific catalyst of methyl oxidation of 3-methylindole. Mol Pharmacol. 2003 May;63(5):1137-47. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 6855
Enzyme 112 Name Cytochrome P450 4Z1
Enzyme 112 Synonyms
  1. CYPIVZ1
Enzyme 112 Gene Name CYP4Z1
Enzyme 112 Protein Sequence >Cytochrome P450 4Z1 
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEF
YPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESW
VGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELF
QHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFS
SQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFS
EADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLS
QMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWED
PQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHS
RPPQPVRQVVLKSKNGIHVFAKKVC
Enzyme 112 Number of Residues 505
Enzyme 112 Molecular Weight 59085.4
Enzyme 112 Theoretical pI 9.63
Enzyme 112 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 112 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 112 Specific Function RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O
Enzyme 112 Pathways
Enzyme 112 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • 10-30
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein 158257782 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID Q86W10 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name CP4Z1_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >1518 bp 
ATGGAGCCCTCCTGGCTTCAGGAACTCATGGCTCACCCCTTCTTGCTGCTGATCCTCCTC
TGCATGTCTCTGCTGCTGTTTCAGGTAATCAGGTTGTACCAGAGGAGGAGATGGATGATC
AGAGCCCTGCACCTGTTTCCTGCACCCCCTGCCCACTGGTTCTATGGCCACAAGGAGTTT
TACCCAGTAAAGGAGTTTGAGGTGTATCATAAGCTGATGGAAAAATACCCATGTGCTGTT
CCCTTGTGGGTTGGACCCTTTACGATGTTCTTCAGTGTCCATGACCCAGACTATGCCAAG
ATTCTCCTGAAAAGACAAGATCCCAAAAGTGCTGTTAGCCACAAAATCCTTGAATCCTGG
GTTGGTCGAGGACTTGTGACCCTGGATGGTTCTAAATGGAAAAAGCACCGCCAGATTGTG
AAACCTGGCTTCAACATCAGCATTCTGAAAATATTCATCACCATGATGTCTGAGAGTGTT
CGGATGATGCTGAACAAATGGGAGGAACACATTGCCCAAAACTCACGTCTGGAGCTCTTT
CAACATGTCTCCCTGATGACCCTGGACAGCATCATGAAGTGTGCCTTCAGCCACCAGGGC
AGCATCCAGTTGGACAGTACCCTGGACTCATACCTGAAAGCAGTGTTCAACCTTAGCAAA
ATCTCCAACCAGCGCATGAACAATTTTCTACATCACAACGACCTGGTTTTCAAATTCAGC
TCTCAAGGCCAAATCTTTTCTAAATTTAACCAAGAACTTCATCAGTTCACAGAGAAAGTA
ATCCAGGACCGGAAGGAGTCTCTTAAGGATAAGCTAAAACAAGATACTACTCAGAAAAGG
CGCTGGGATTTTCTGGACATACTTTTGAGTGCCAAAAGCGAAAACACCAAAGATTTCTCT
GAAGCAGATCTCCAGGCTGAAGTGAAAACGTTCATGTTTGCAGGACATGACACCACATCC
AGTGCTATCTCCTGGATCCTTTACTGCTTGGCAAAGTACCCTGAGCATCAGCAGAGATGC
CGAGATGAAATCAGGGAACTCCTAGGGGATGGGTCTTCTATTACCTGGGAACACCTGAGC
CAGATGCCTTACACCACGATGTGCATCAAGGAATGCCTCCGCCTCTACGCACCGGTAGTA
AACATATCCCGGTTACTCGACAAACCCATTACTTTTCCAGATGGACGCTCCTTACCTGCA
GGAATAACTGTGTTTATCAATATTTGGGCTCTTCACCACAACCCCTATTTCTGGGAAGAC
CCTCAGGTCTTTAACCCCTTGAGATTCTCCAGGGAAAATTCTGAAAAAATACATCCCTAT
GCCTTCATACCATTCTCAGCTGGATTAAGGAACTGCATTGGGCAGCATTTTGCCATAATT
GAGTGTAAAGTGGCAGTGGCATTAACTCTGCTCCGCTTCAAGCTGGCTCCAGACCACTCA
AGGCCTCCCCAGCCTGTTCGTCAAGTTGTCCTCAAGTCCAAGAATGGAATCCATGTGTTT
GCAAAAAAAGTTTGCTAA
Enzyme 112 GenBank Gene ID AK292175 Link Image
Enzyme 112 GeneCard ID CYP4Z1 Link Image
Enzyme 112 GenAtlas ID Not Available
Enzyme 112 HGNC ID Not Available
Enzyme 112 Chromosome Location 1
Enzyme 112 Locus 1p33
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References
  1. Rieger MA, Ebner R, Bell DR, Kiessling A, Rohayem J, Schmitz M, Temme A, Rieber EP, Weigle B: Identification of a novel mammary-restricted cytochrome P450, CYP4Z1, with overexpression in breast carcinoma. Cancer Res. 2004 Apr 1;64(7):2357-64. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 6856
Enzyme 113 Name Cytochrome P450 1A2
Enzyme 113 Synonyms
  1. CYPIA2
  2. Cytochrome P(3)450
  3. Cytochrome P450 4
  4. Cytochrome P450-P3
Enzyme 113 Gene Name CYP1A2
Enzyme 113 Protein Sequence >Cytochrome P450 1A2 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Enzyme 113 Number of Residues 515
Enzyme 113 Molecular Weight 58293.8
Enzyme 113 Theoretical pI 9.43
Enzyme 113 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 113 General Function Involved in monooxygenase activity
Enzyme 113 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O- deethylation of phenacetin
Enzyme 113 Pathways
Enzyme 113 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 30339 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID P05177 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name CP1A2_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >1548 bp 
ATGGCATTGTCCCAGTCTGTTCCCTTCTCGGCCACAGAGCTTCTCCTGGCCTCTGCCATC
TTCTGCCTGGTATTCTGGGTGCTCAAGGGTTTGAGGCCTCGGGTCCCCAAAGGCCTGAAA
AGTCCACCAGAGCCATGGGGCTGGCCCTTGCTCGGGCATGTGCTGACCCTGGGGAAGAAC
CCGCACCTGGCACTGTCAAGGATGAGCCAGCGCTACGGGGACGTCCTGCAGATCCGCATT
GGCTCCACGCCCGTGCTGGTGCTGAGCCGCCTGGACACCATCCGGCAGGCCCTGGTGCGG
CAGGGCGACGATTTCAAGGGCCGGCCTGACCTCTACACCTCCACCCTCATCACTGATGGC
CAGAGCTTGACCTTCAGCACAGACTCTGGACCGGTGTGGGCTGCCCGCCGGCGCCTGGCC
CAGAATGCCCTCAACACCTTCTCCATCGCCTCTGACCCAGCTTCCTCATCCTCCTGCTAC
CTGGAGGAGCATGTGAGCAAGGAGGCTAAGGCCCTGATCAGCAGGTTGCAGGAGCTGATG
GCAGGGCCTGGGCACTTCGACCCTTACAATCAGGTGGTGGTGTCAGTGGCCAACGTCATT
GGTGCCATGTGCTTCGGACAGCACTTCCCTGAGAGTAGCGATGAGATGCTCAGCCTCGTG
AAGAACACTCATGAGTTCGTGGAGACTGCCTCCTCCGGGAACCCCCTGGACTTCTTCCCC
ATCCTTCGCTACCTGCCTAACCCTGCCCTGCAGAGGTTCAAGGCCTTCAACCAGAGGTTC
CTGTGGTTCCTGCAGAAAACAGTCCAGGAGCACTATCAGGACTTTGACAAGAACAGTGTC
CGGGACATCACGGGTGCCCTGTTCAAGCACAGCAAGAAGGGGCCTAGAGCCAGCGGCAAC
CTCATCCCACAGGAGAAGATTGTCAACCTTGTCAATGACATCTTTGGAGCAGGATTTGAC
ACAGTCACCACAGCCATCTCCTGGAGCCTCATGTACCTTGTGACCAAGCCTGAGATACAG
AGGAAGATCCAGAAGGAGCTGGACACTGTGATTGGCAGGGAGCGGCGGCCCCGGCTCTCT
GACAGACCCCAGCTGCCCTACTTGGAGGCCTTCATCCTGGAGACCTTCCGACACTCCTCC
TTCTTGCCCTTCACCATCCCCCACAGCACAACAAGGGACACAACGCTGAATGGCTTCTAC
ATCCCCAAGAAATGCTGTGTCTTCGTAAACCAGTGGCAGGTCAACCATGACCCAGAGCTG
TGGGAGGACCCCTCTGAGTTCCGGCCTGAGCGGTTCCTCACCGCCGATGGCACTGCCATT
AACAAGCCCTTGAGTGAGAAGATGATGCTGTTTGGCATGGGCAAGCGCCGGTGTATCGGG
GAAGTCCTGGCCAAGTGGGAGATCTTCCTCTTCCTGGCCATCCTGCTACAGCAACTGGAG
TTCAGCGTGCCGCCGGGCGTGAAAGTCGACCTGACCCCCATCTACGGGCTGACCATGAAG
CACGCCCGCTGTGAACATGTCCAGGCGCGGCGCTTCTCCATCAATTGA
Enzyme 113 GenBank Gene ID Z00036 Link Image
Enzyme 113 GeneCard ID CYP1A2 Link Image
Enzyme 113 GenAtlas ID CYP1A2 Link Image
Enzyme 113 HGNC ID HGNC:2596 Link Image
Enzyme 113 Chromosome Location 1
Enzyme 113 Locus 15q24.1
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References
  1. Jaiswal AK, Nebert DW, Gonzalez FJ: Human P3(450): cDNA and complete amino acid sequence. Nucleic Acids Res. 1986 Aug 26;14(16):6773-4. [PubMed Link Image]
  2. Quattrochi LC, Pendurthi UR, Okino ST, Potenza C, Tukey RH: Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6731-5. [PubMed Link Image]
  3. Ikeya K, Jaiswal AK, Owens RA, Jones JE, Nebert DW, Kimura S: Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. Mol Endocrinol. 1989 Sep;3(9):1399-408. [PubMed Link Image]
  4. Jaiswal AK, Nebert DW, McBride OW, Gonzalez FJ: Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15. J Exp Pathol. 1987 Winter;3(1):1-17. [PubMed Link Image]
  5. Corchero J, Pimprale S, Kimura S, Gonzalez FJ: Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation. Pharmacogenetics. 2001 Feb;11(1):1-6. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Wrighton SA, Campanile C, Thomas PE, Maines SL, Watkins PB, Parker G, Mendez-Picon G, Haniu M, Shively JE, Levin W, et al.: Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat. Mol Pharmacol. 1986 Apr;29(4):405-10. [PubMed Link Image]
  8. Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH: Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. DNA. 1985 Oct;4(5):395-400. [PubMed Link Image]
  9. Zhou H, Josephy PD, Kim D, Guengerich FP: Functional characterization of four allelic variants of human cytochrome P450 1A2. Arch Biochem Biophys. 2004 Feb 1;422(1):23-30. [PubMed Link Image]
  10. Sansen S, Yano JK, Reynald RL, Schoch GA, Griffin KJ, Stout CD, Johnson EF: Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J Biol Chem. 2007 May 11;282(19):14348-55. Epub 2007 Feb 20. [PubMed Link Image]
  11. Huang JD, Guo WC, Lai MD, Guo YL, Lambert GH: Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese. Drug Metab Dispos. 1999 Jan;27(1):98-101. [PubMed Link Image]
  12. Chevalier D, Cauffiez C, Allorge D, Lo-Guidice JM, Lhermitte M, Lafitte JJ, Broly F: Five novel natural allelic variants-951A>C, 1042G>A (D348N), 1156A>T (I386F), 1217G>A (C406Y) and 1291C>T (C431Y)-of the human CYP1A2 gene in a French Caucasian population. Hum Mutat. 2001 Apr;17(4):355-6. [PubMed Link Image]
  13. Murayama N, Soyama A, Saito Y, Nakajima Y, Komamura K, Ueno K, Kamakura S, Kitakaze M, Kimura H, Goto Y, Saitoh O, Katoh M, Ohnuma T, Kawai M, Sugai K, Ohtsuki T, Suzuki C, Minami N, Ozawa S, Sawada J: Six novel nonsynonymous CYP1A2 gene polymorphisms: catalytic activities of the naturally occurring variant enzymes. J Pharmacol Exp Ther. 2004 Jan;308(1):300-6. Epub 2003 Oct 16. [PubMed Link Image]
  14. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  15. Soyama A, Saito Y, Hanioka N, Maekawa K, Komamura K, Kamakura S, Kitakaze M, Tomoike H, Ueno K, Goto Y, Kimura H, Katoh M, Sugai K, Saitoh O, Kawai M, Ohnuma T, Ohtsuki T, Suzuki C, Minami N, Kamatani N, Ozawa S, Sawada J: Single nucleotide polymorphisms and haplotypes of CYP1A2 in a Japanese population. Drug Metab Pharmacokinet. 2005 Feb;20(1):24-33. [PubMed Link Image]
  16. Jiang Z, Dalton TP, Jin L, Wang B, Tsuneoka Y, Shertzer HG, Deka R, Nebert DW: Toward the evaluation of function in genetic variability: characterizing human SNP frequencies and establishing BAC-transgenic mice carrying the human CYP1A1_CYP1A2 locus. Hum Mutat. 2005 Feb;25(2):196-206. [PubMed Link Image]
  17. Cornelis MC, El-Sohemy A, Kabagambe EK, Campos H: Coffee, CYP1A2 genotype, and risk of myocardial infarction. JAMA. 2006 Mar 8;295(10):1135-41. [PubMed Link Image]
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 6857
Enzyme 114 Name Cytochrome P450 19A1
Enzyme 114 Synonyms
  1. Aromatase
  2. CYPXIX
  3. Cytochrome P-450AROM
  4. Estrogen synthase
Enzyme 114 Gene Name CYP19A1
Enzyme 114 Protein Sequence >Cytochrome P450 19A1 
MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLI
SHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKL
GLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTN
ESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWL
YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCI
LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFI
YESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAK
NVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLH
PDETKNMLEMIFTPRNSDRCLEH
Enzyme 114 Number of Residues 503
Enzyme 114 Molecular Weight 57882.5
Enzyme 114 Theoretical pI 7.56
Enzyme 114 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 114 General Function Involved in monooxygenase activity
Enzyme 114 Specific Function Catalyzes the formation of aromatic C18 estrogens from C19 androgens
Enzyme 114 Pathways
Enzyme 114 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein 61354153 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID P11511 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name CP19A_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >1512 bp 
ATGGTTTTGGAAATGCTGAACCCGATACATTATAACATCACCAGCATCGTGCCTGAAGCC
ATGCCTGCTGCCACCATGCCAGTCCTGCTCCTCACTGGCCTTTTTCTCTTGGTGTGGAAT
TATGAGGGCACATCCTCAATACCAGGTCCTGGCTACTGCATGGGAATTGGACCCCTCATC
TCCCACGGCAGATTCCTGTGGATGGGGATCGGCAGTGCCTGCAACTACTACAACCGGGTA
TATGGAGAATTCATGCGAGTCTGGATCTCTGGAGAGGAAACACTCATTATCAGCAAGTCC
TCAAGTATGTTCCACATAATGAAGCACAATCATTACAGCTCTCGATTCGGCAGCAAACTT
GGGCTGCAGTGCATCGGTATGCATGAGAAAGGCATCATATTTAACAACAATCCAGAGCTC
TGGAAAACAACTCGACCCTTCTTTATGAAAGCTCTGTCAGGCCCCGGCCTTGTTCGTATG
GTCACAGTCTGTGCTGAATCCCTCAAAACACATCTGGACAGGTTGGAGGAGGTGACCAAT
GAATCGGGCTATGTGGACGTGTTGACCCTTCTGCGTCGTGTCATGCTGGACACCTCTAAC
ACGCTCTTCTTGAGGATCCCTTTGGACGAAAGTGCTATCGTGGTTAAAATCCAAGGTTAT
TTTGATGCATGGCAAGCTCTCCTCATCAAACCAGACATCTTCTTTAAGATTTCTTGGCTA
TACAAAAAGTATGAGAAGTCTGTCAAGGATTTGAAAGATGCCATAGAAGTTCTGATAGCA
GAAAAAAGACGCAGGATTTCCACAGAAGAGAAACTGGAAGAATGTATGGACTTTGCCACT
GAGTTGATTTTAGCAGAGAAACGTGGTGACCTGACAAGAGAGAATGTGAACCAGTGCATA
TTGGAAATGCTGATCGCAGCTCCTGACACCATGTCTGTCTCTTTGTTCTTCATGCTATTT
CTCATTGCAAAGCACCCTAATGTTGAAGAGGCAATAATAAAGGAAATCCAGACTGTTATT
GGTGAGAGAGACATAAAGATTGATGATATACAAAAATTAAAAGTGATGGAAAACTTCATT
TATGAGAGCATGCGGTACCAGCCTGTCGTGGACTTGGTCATGCGCAAAGCCTTAGAAGAT
GATGTAATCGATGGCTACCCAGTGAAAAAGGGGACAAACATTATCCTGAATATTGGAAGG
ATGCACAGACTCGAGTTTTTCCCCAAACCCAATGAATTTACTCTTGAAAATTTTGCAAAG
AATGTTCCTTATAGGTACTTTCAGCCATTTGGCTTTGGGCCCCGTGGCTGTGCAGGAAAG
TACATCGCCATGGTGATGATGAAAGCCATCCTCGTTACACTTCTGAGACGATTCCACGTG
AAGACATTGCAAGGACAGTGTGTTGAGAGCATACAGAAGATACACGACTTGTCCTTGCAC
CCAGATGAGACTAAAAACATGCTGGAAATGATCTTTACCCCAAGAAACTCAGACAGGTGT
CTGGAACACTAG
Enzyme 114 GenBank Gene ID AY957953 Link Image
Enzyme 114 GeneCard ID CYP19A1 Link Image
Enzyme 114 GenAtlas ID CYP19A1 Link Image
Enzyme 114 HGNC ID HGNC:2594 Link Image
Enzyme 114 Chromosome Location 1
Enzyme 114 Locus 15q21.1
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References
  1. Harada N: Cloning of a complete cDNA encoding human aromatase: immunochemical identification and sequence analysis. Biochem Biophys Res Commun. 1988 Oct 31;156(2):725-32. [PubMed Link Image]
  2. Chen SA, Besman MJ, Sparkes RS, Zollman S, Klisak I, Mohandas T, Hall PF, Shively JE: Human aromatase: cDNA cloning, Southern blot analysis, and assignment of the gene to chromosome 15. DNA. 1988 Jan-Feb;7(1):27-38. [PubMed Link Image]
  3. Corbin CJ, Graham-Lorence S, McPhaul M, Mason JI, Mendelson CR, Simpson ER: Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8948-52. [PubMed Link Image]
  4. Toda K, Terashima M, Mitsuuchi Y, Yamasaki Y, Yokoyama Y, Nojima S, Ushiro H, Maeda T, Yamamoto Y, Sagara Y, et al.: Alternative usage of different poly(A) addition signals for two major species of mRNA encoding human aromatase P-450. FEBS Lett. 1989 Apr 24;247(2):371-6. [PubMed Link Image]
  5. Means GD, Mahendroo MS, Corbin CJ, Mathis JM, Powell FE, Mendelson CR, Simpson ER: Structural analysis of the gene encoding human aromatase cytochrome P-450, the enzyme responsible for estrogen biosynthesis. J Biol Chem. 1989 Nov 15;264(32):19385-91. [PubMed Link Image]
  6. Pompon D, Liu RY, Besman MJ, Wang PL, Shively JE, Chen S: Expression of human placental aromatase in Saccharomyces cerevisiae. Mol Endocrinol. 1989 Sep;3(9):1477-87. [PubMed Link Image]
  7. Harada N, Ogawa H, Shozu M, Yamada K, Suhara K, Nishida E, Takagi Y: Biochemical and molecular genetic analyses on placental aromatase (P-450AROM) deficiency. J Biol Chem. 1992 Mar 5;267(7):4781-5. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Evans CT, Ledesma DB, Schulz TZ, Simpson ER, Mendelson CR: Isolation and characterization of a complementary DNA specific for human aromatase-system cytochrome P-450 mRNA. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6387-91. [PubMed Link Image]
  10. Simpson ER, Evans CT, Corbin CJ, Powell FE, Ledesma DB, Mendelson CR: Sequencing of cDNA inserts encoding aromatase cytochrome P-450 (P-450AROM). Mol Cell Endocrinol. 1987 Aug;52(3):267-72. [PubMed Link Image]
  11. Mahendroo MS, Means GD, Mendelson CR, Simpson ER: Tissue-specific expression of human P-450AROM. The promoter responsible for expression in adipose tissue is different from that utilized in placenta. J Biol Chem. 1991 Jun 15;266(17):11276-81. [PubMed Link Image]
  12. Mahendroo MS, Mendelson CR, Simpson ER: Tissue-specific and hormonally controlled alternative promoters regulate aromatase cytochrome P450 gene expression in human adipose tissue. J Biol Chem. 1993 Sep 15;268(26):19463-70. [PubMed Link Image]
  13. Chen S, Shively JE, Nakajin S, Shinoda M, Hall PF: Amino terminal sequence analysis of human placenta aromatase. Biochem Biophys Res Commun. 1986 Mar 28;135(3):713-9. [PubMed Link Image]
  14. Honda S, Harada N, Takagi Y: Novel exon 1 of the aromatase gene specific for aromatase transcripts in human brain. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1153-60. [PubMed Link Image]
  15. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  16. Ghosh D, Griswold J, Erman M, Pangborn W: Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature. 2009 Jan 8;457(7226):219-23. [PubMed Link Image]
  17. Ito Y, Fisher CR, Conte FA, Grumbach MM, Simpson ER: Molecular basis of aromatase deficiency in an adult female with sexual infantilism and polycystic ovaries. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11673-7. [PubMed Link Image]
  18. Morishima A, Grumbach MM, Simpson ER, Fisher C, Qin K: Aromatase deficiency in male and female siblings caused by a novel mutation and the physiological role of estrogens. J Clin Endocrinol Metab. 1995 Dec;80(12):3689-98. [PubMed Link Image]
  19. Carani C, Qin K, Simoni M, Faustini-Fustini M, Serpente S, Boyd J, Korach KS, Simpson ER: Effect of testosterone and estradiol in a man with aromatase deficiency. N Engl J Med. 1997 Jul 10;337(2):91-5. [PubMed Link Image]
  20. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed Link Image]
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 6858
Enzyme 115 Name Cytochrome P450 2C8
Enzyme 115 Synonyms
  1. CYPIIC8
  2. Cytochrome P450 IIC2
  3. Cytochrome P450 MP-12
  4. Cytochrome P450 MP-20
  5. Cytochrome P450 form 1
  6. S-mephenytoin 4-hydroxylase
Enzyme 115 Gene Name CYP2C8
Enzyme 115 Protein Sequence >Cytochrome P450 2C8 
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
Enzyme 115 Number of Residues 490
Enzyme 115 Molecular Weight 55824.3
Enzyme 115 Theoretical pI 8.62
Enzyme 115 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 115 General Function Involved in monooxygenase activity
Enzyme 115 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti- cancer drug paclitaxel (taxol)
Enzyme 115 Pathways
Enzyme 115 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • None
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 158258943 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID P10632 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name CP2C8_HUMAN Link Image
Enzyme 115 PDB ID 1PQ2 Link Image
Enzyme 115 PDB File Show
Enzyme 115 3D Structure
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >1473 bp 
ATGGAACCTTTTGTGGTCCTGGTGCTGTGTCTCTCTTTTATGCTTCTCTTTTCACTCTGG
AGACAGAGCTGTAGGAGAAGGAAGCTCCCTCCTGGCCCCACTCCTCTTCCTATTATTGGA
AATATGCTACAGATAGATGTTAAGGACATCTGCAAATCTTTCACCAATTTCTCAAAAGTC
TATGGTCCTGTGTTCACCGTGTATTTTGGCATGAATCCCATAGTGGTGTTTCATGGATAT
GAGGCAGTGAAGGAAGCCCTGATTGATAATGGAGAGGAGTTTTCTGGAAGAGGCAATTCC
CCAATATCTCAAAGAATTACTAAAGGACTTGGAATCATTTCCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCACAACCTTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCTCACTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
GTTGTTTTCCAGAAACGATTTGATTATAAAGATCAGAATTTTCTCACCCTGATGAAAAGA
TTCAATGAAAACTTCAGGATTCTGAACTCCCCATGGATCCAGGTCTGCAATAATTTCCCT
CTACTCATTGATTGTTTCCCAGGAACTCACAACAAAGTGCTTAAAAATGTTGCTCTTACA
CGAAGTTACATTAGGGAGAAAGTAAAAGAACACCAAGCATCACTGGATGTTAACAATCCT
CGGGACTTTATCGATTGCTTCCTGATCAAAATGGAGCAGGAAAAGGACAACCAAAAGTCA
GAATTCAATATTGAAAACTTGGTTGGCACTGTAGCTGATCTATTTGTTGCTGGAACAGAG
ACAACAAGCACCACTCTGAGATATGGACTCCTGCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGATCATGTAATTGGCAGACACAGGAGCCCCTGCATGCAG
GATAGGAGCCACATGCCTTACACTGATGCTGTAGTGCACGAGATCCAGAGATACAGTGAC
CTTGTCCCCACCGGTGTGCCCCATGCAGTGACCACTGATACTAAGTTCAGAAACTACCTC
ATCCCCAAGGGCACAGCCATAATGGCATTACTGACTTCCGTGCTACATGATGACAAAGAA
TTTCCTAATCCAAATATCTTTGACCCTGGCCACTTTCTAGATAAGAATGGCAACTTTAAG
AAAAGTGACTACTTCATGCCTTTCTCAGCAGGAAAACGAATTTGTGCAGGAGAAGGACTT
GCCCGCATGGAGCTATTTTTATTTCTAACCACAATTTTACAGAACTTTAACCTGAAATCT
GTTGATGATTTAAAGAACCTCAATACTACTGCAGTTACCAAAGGGATTGTTTCTCTGCCA
CCCTCATACCAGATCTGCTTCATCCCTGTCTGA
Enzyme 115 GenBank Gene ID AK292753 Link Image
Enzyme 115 GeneCard ID CYP2C8 Link Image
Enzyme 115 GenAtlas ID CYP2C8 Link Image
Enzyme 115 HGNC ID HGNC:2622 Link Image
Enzyme 115 Chromosome Location 1
Enzyme 115 Locus 10q23.33
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References
  1. Okino ST, Quattrochi LC, Pendurthi UR, McBride OW, Tukey RH: Characterization of multiple human cytochrome P-450 1 cDNAs. The chromosomal localization of the gene and evidence for alternate RNA splicing. J Biol Chem. 1987 Nov 25;262(33):16072-9. [PubMed Link Image]
  2. Kimura S, Pastewka J, Gelboin HV, Gonzalez FJ: cDNA and amino acid sequences of two members of the human P450IIC gene subfamily. Nucleic Acids Res. 1987 Dec 10;15(23):10053-4. [PubMed Link Image]
  3. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ged C, Beaune P: Isolation of the human cytochrome P-450 IIC8 gene: multiple glucocorticoid responsive elements in the 5' region. Biochim Biophys Acta. 1991 Mar 26;1088(3):433-5. [PubMed Link Image]
  8. Zeldin DC, DuBois RN, Falck JR, Capdevila JH: Molecular cloning, expression and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform. Arch Biochem Biophys. 1995 Sep 10;322(1):76-86. [PubMed Link Image]
  9. Ged C, Umbenhauer DR, Bellew TM, Bork RW, Srivastava PK, Shinriki N, Lloyd RS, Guengerich FP: Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase. Biochemistry. 1988 Sep 6;27(18):6929-40. [PubMed Link Image]
  10. Shephard EA, Phillips IR, Santisteban I, Palmer CN, Povey S: Cloning, expression and chromosomal localization of a member of the human cytochrome P450IIC gene sub-family. Ann Hum Genet. 1989 Jan;53(Pt 1):23-31. [PubMed Link Image]
  11. Kolyada AY: Sequence of a human liver cytochrome P-450 cDNA clone. Nucleic Acids Res. 1990 Sep 25;18(18):5550. [PubMed Link Image]
  12. Schoch GA, Yano JK, Wester MR, Griffin KJ, Stout CD, Johnson EF: Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site. J Biol Chem. 2004 Mar 5;279(10):9497-503. Epub 2003 Dec 15. [PubMed Link Image]
  13. Dai D, Zeldin DC, Blaisdell JA, Chanas B, Coulter SJ, Ghanayem BI, Goldstein JA: Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug paclitaxel and arachidonic acid. Pharmacogenetics. 2001 Oct;11(7):597-607. [PubMed Link Image]
  14. Bahadur N, Leathart JB, Mutch E, Steimel-Crespi D, Dunn SA, Gilissen R, Houdt JV, Hendrickx J, Mannens G, Bohets H, Williams FM, Armstrong M, Crespi CL, Daly AK: CYP2C8 polymorphisms in Caucasians and their relationship with paclitaxel 6alpha-hydroxylase activity in human liver microsomes. Biochem Pharmacol. 2002 Dec 1;64(11):1579-89. [PubMed Link Image]
  15. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 6859
Enzyme 116 Name Cytochrome P450 2S1
Enzyme 116 Synonyms
  1. CYPIIS1
Enzyme 116 Gene Name CYP2S1
Enzyme 116 Protein Sequence >Cytochrome P450 2S1 
MEATGTWALLLALALLLLLTLALSGTRARGHLPPGPTPLPLLGNLLQLRPGALYSGLMRL
SKKYGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN
GERWRQLRKFTMLALRDLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSN
VVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHH
VSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLL
FAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEA
QRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDA
DGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSG
LFNIPPAFQLQVRPTDLHSTTQTR
Enzyme 116 Number of Residues 504
Enzyme 116 Molecular Weight 55816.2
Enzyme 116 Theoretical pI 8.84
Enzyme 116 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 116 General Function Involved in monooxygenase activity
Enzyme 116 Specific Function Has a potential importance for extrahepatic xenobiotic metabolism
Enzyme 116 Pathways
Enzyme 116 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 13161184 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q96SQ9 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name CP2S1_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >1515 bp 
ATGGAGGCGACCGGCACCTGGGCGCTGCTGCTGGCGCTGGCGCTGCTCCTGCTGCTGACG
CTGGCGCTGTCCGGGACCAGGGCCCGAGGCCACCTGCCCCCCGGGCCCACGCCGCTACCA
CTGCTGGGAAACCTCCTGCAGCTACGGCCCGGGGCGCTGTATTCAGGGCTCATGCGGCTG
AGTAAGAAGTACGGACCGGTGTTCACCATCTACCTGGGACCCTGGCGGCCTGTGGTGGTC
CTGGTTGGGCAGGAGGCTGTGCGGGAGGCCCTGGGAGGTCAGGCTGAGGAGTTCAGCGGC
CGGGGAACCGTAGCGATGCTGGAAGGGACTTTTGATGGCCATGGGGTTTTCTTCTCCAAC
GGGGAGCGGTGGAGGCAGCTGAGGAAGTTTACCATGCTTGCTCTGCGGGACCTGGGCATG
GGGAAGCGAGAAGGCGAGGAGCTGATCCAGGCGGAGGCCCGGTGTCTGGTGGAGACATTC
CAGGGGACAGAAGGACGCCCATTCGATCCCTCCCTGCTGCTGGCCCAGGCCACCTCCAAC
GTAGTCTGCTCCCTCCTCTTTGGCCTCCGCTTCTCCTATGAGGATAAGGAGTTCCAGGCC
GTGGTCCGGGCAGCTGGTGGTACCCTGCTGGGAGTCAGCTCCCAGGGGGGTCAGACCTAC
GAGATGTTCTCCTGGTTCCTGCGGCCCCTGCCAGGCCCCCACAAGCAGCTCCTCCACCAC
GTCAGCACCTTGGCTGCCTTCACAGTCCGGCAGGTGCAGCAGCACCAGGGGAACCTGGAT
GCTTCGGGCCCCGCACGTGACCTTGTCGATGCCTTCCTGCTGAAGATGGCACAGGAGGAA
CAAAACCCAGGCACAGAATTCACCAACAAGAACATGCTGATGACAGTCATTTATTTGCTG
TTTGCTGGGACGATGACGGTCAGCACCACGGTCGGCTATACCCTCCTGCTCCTGATGAAA
TACCCTCATGTCCAAAAGTGGGTACGTGAGGAGCTGAATCGGGAGCTGGGGGCTGGCCAG
GCACCAAGCCTAGGGGACCGTACCCGCCTCCCTTACACCGACGCGGTTCTGCATGAGGCG
CAGCGGCTGCTGGCGCTGGTGCCCATGGGAATACCCCGCACCCTCATGCGGACCACCCGC
TTCCGAGGGTACACCCTGCCCCAGGGCACGGAGGTCTTCCCCCTCCTTGGCTCCATCCTG
CATGACCCCAACATCTTCAAGCACCCAGAAGAGTTCAACCCAGACCGTTTCCTGGATGCA
GATGGACGGTTCAGGAAGCATGAGGCGTTCCTGCCCTTCTCCTTAGGGAAGCGTGTCTGC
CTTGGAGAGGGCCTGGCAAAAGCGGAGCTCTTCCTCTTCTTCACCACCATCCTACAAGCC
TTCTCCCTGGAGAGCCCGTGCCCGCCGGACACCCTGAGCCTCAAGCCCACCGTCAGTGGC
CTTTTCAACATTCCCCCAGCCTTCCAGCTGCAAGTCCGTCCCACTGACCTTCACTCCACC
ACGCAGACCAGATGA
Enzyme 116 GenBank Gene ID AF335278 Link Image
Enzyme 116 GeneCard ID CYP2S1 Link Image
Enzyme 116 GenAtlas ID CYP2S1 Link Image
Enzyme 116 HGNC ID HGNC:15654 Link Image
Enzyme 116 Chromosome Location 1
Enzyme 116 Locus 19q13.1
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References
  1. Rylander T, Neve EP, Ingelman-Sundberg M, Oscarson M: Identification and tissue distribution of the novel human cytochrome P450 2S1 (CYP2S1). Biochem Biophys Res Commun. 2001 Feb 23;281(2):529-35. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 6861
Enzyme 117 Name Cytochrome P450 2J2
Enzyme 117 Synonyms
  1. Arachidonic acid epoxygenase
  2. CYPIIJ2
Enzyme 117 Gene Name CYP2J2
Enzyme 117 Protein Sequence >Cytochrome P450 2J2 
MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVD
FEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHI
FKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDP
HFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFL
PGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEEN
LICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMP
YTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDT
FNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLS
LKFRMGITISPVSHRLCAVPQV
Enzyme 117 Number of Residues 502
Enzyme 117 Molecular Weight 57610.2
Enzyme 117 Theoretical pI 8.87
Enzyme 117 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 117 General Function Involved in monooxygenase activity
Enzyme 117 Specific Function This enzyme metabolizes arachidonic acid predominantly via a NADPH-dependent olefin epoxidation to all four regioisomeric cis-epoxyeicosatrienoic acids. One of the predominant enzymes responsible for the epoxidation of endogenous cardiac arachidonic acid pools
Enzyme 117 Pathways
Enzyme 117 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein Not Available
Enzyme 117 UniProtKB/Swiss-Prot ID P51589 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name CP2J2_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >1509 bp 
ATGCTCGCGGCGATGGGCTCTCTGGCGGCTGCCCTCTGGGCAGTGGTCCATCCTCGGACT
CTCCTACTGGGCACTGTCGCCTTTCTGCTCGCTGCTGACTTTCTCAAAAGACGGCGCCCA
AAGAACTACCCGCCGGGGCCCTGGCGCCTGCCCTTCCTTGGCAACTTCTTCCTTGTGGAC
TTCGAGCAGTCGCACCTGGAGGTTCAGCTGTTTGTGAAGAAATATGGGAACCTTTTTAGC
TTGGAGCTTGGTGACATATCTGCAGTTCTTATTACTGGCTTGCCCTTAATCAAAGAAGCC
CTTATCCACATGGACCAAAACTTTGGGAACCGCCCCGTGACCCCTATGCGAGAACATATC
TTTAAGAAAAATGGATTGATTATGTCAAGTGGCCAGGCATGGAAGGAGCAAAGAAGGTTC
ACTCTGACAGCACTAAGGAACTTTGGTTTAGGAAAGAAGAGCTTAGAGGAACGCATTCAG
GAGGAGGCCCAACACCTCACTGAAGCAATAAAAGAGGAGAACGGACAGCCTTTTGACCCT
CATTTCAAGATCAACAATGCAGTTTCCAATATCATTTGCTCCATCACCTTCGGAGAACGC
TTTGAGTACCAGGATAGTTGGTTTCAGCAGCTGCTGAAGTTACTAGATGAAGTCACATAC
TTGGAGGCTTCAAAGACATGCCAGCTCTACAATGTCTTTCCATGGATAATGAAATTCCTG
CCTGGACCCCACCAAACTCTCTTCAGCAACTGGAAAAAACTGAAATTGTTTGTTTCTCAT
ATGATTGACAAACACAGAAAGGATTGGAATCCTGCAGAAACAAGAGACTTTATTGATGCT
TACCTTAAAGAAATGTCAAAGCACACAGGCAATCCTACTTCAAGTTTCCATGAAGAAAAC
CTCATCTGCAGCACCCTGGACCTCTTCTTTGCCGGAACCGAGACAACTTCCACAACTCTG
CGATGGGCTCTGCTTTATATGGCCCTCTACCCAGAAATCCAAGAAAAAGTACAAGCTGAG
ATTGACAGAGTGATTGGCCAGGGGCAGCAGCCGAGCACAGCCGCCCGGGAGTCCATGCCC
TACACCAATGCTGTCATCCATGAGGTGCAGAGAATGGGCAACATCATCCCCCTGAACGTT
CCCAGGGAAGTGACAGTTGATACCACTTTGGCTGGGTACCACCTGCCCAAGGGTACCATG
ATCCTGACCAATTTGACGGCGCTGCACAGGGACCCCACAGAGTGGGCCACCCCTGACACA
TTCAATCCGGACCATTTTCTGGAGAATGGACAGTTTAAGAAAAGGGAAGCCTTTATGCCT
TTCTCAATAGGAAAGCGGGCATGCCTCGGAGAACAGTTGGCCAGGACTGAGCTGTTTATT
TTCTTCACTTCCCTTATGCAAAAATTTACCTTCAGGCCCCCAAACAATGAGAAGCTGAGC
CTGAAGTTTAGAATGGGTATCACCATTTCCCCAGTCAGTCACCGCCTCTGCGCTGTTCCT
CAGGTGTAA
Enzyme 117 GenBank Gene ID U37143 Link Image
Enzyme 117 GeneCard ID CYP2J2 Link Image
Enzyme 117 GenAtlas ID CYP2J2 Link Image
Enzyme 117 HGNC ID HGNC:2634 Link Image
Enzyme 117 Chromosome Location 1
Enzyme 117 Locus 1p31.3-p31.2
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Wu S, Moomaw CR, Tomer KB, Falck JR, Zeldin DC: Molecular cloning and expression of CYP2J2, a human cytochrome P450 arachidonic acid epoxygenase highly expressed in heart. J Biol Chem. 1996 Feb 16;271(7):3460-8. [PubMed Link Image]
  2. King LM, Ma J, Srettabunjong S, Graves J, Bradbury JA, Li L, Spiecker M, Liao JK, Mohrenweiser H, Zeldin DC: Cloning of CYP2J2 gene and identification of functional polymorphisms. Mol Pharmacol. 2002 Apr;61(4):840-52. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 6862
Enzyme 118 Name Cytochrome P450 2A7
Enzyme 118 Synonyms
  1. CYPIIA7
  2. Cytochrome P450 IIA4
Enzyme 118 Gene Name CYP2A7
Enzyme 118 Protein Sequence >Cytochrome P450 2A7 
MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMK
FSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSN
GERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSTHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKL
LQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFI
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVVF
ATIPRNYTMSFLPR
Enzyme 118 Number of Residues 494
Enzyme 118 Molecular Weight 56424.7
Enzyme 118 Theoretical pI 7.96
Enzyme 118 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 118 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 118 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 118 Pathways
Enzyme 118 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 15147330 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID P20853 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name CP2A7_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >1485 bp 
ATGCTGGCCTCAGGGCTGCTTCTGGTGGCCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCTGTCTGGCAGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCACTG
CCCTTCATTGGAAACTACCTCCAGCTGAACACAGAGCACATATGTGACTCCATCATGAAG
TTCAGTGAGTGCTATGGCCCCGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGTGGACATGATGCCGTCAGGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAAGCCACCTTCGACTGGGTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCTGCGCTTTGCCATCGCCACCCTGAGGGACTTCGGGGTG
GGCAAGCGAGGCATCGAGGAGCGCATCCAGGAGGAGTCGGGCTTCCTCATCGAGGCCATC
CGGAGCACGCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGCTGAGCATGATGCTAGGAATCTTCCAGTTCACGTCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGTTG
CTGCAAGGGCTGGAGGACTTCATAGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACAGGACTTCATCGACTCCTTTCTCATCCACATGCAGGAGGAGGAGAAG
AACCCCAACACGGAGTTCTACTTGAAGAACCTGATGATGAGCACGTTGAACCTCTTCATT
GCAGGCACCGAGACGGTCAGCACCACCCTGCGCTATGGCTTCTTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGACCAAGATGCCCTACATGGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACGTGATCCCCATGAGTTTGGCCCGCAGGGTTAAAAAGGACACCAAGTTT
CGGGATTTTTTCCTCCCTAAGGGCACCGAAGTGTTCCCTATGCTGGGCTCCGTGCTGAGA
GACCCCAGCTTCTTCTCCAACCCTCAGGACTTCAATCCCCAGCATTTCCTGGATGACAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGAACTGTTTC
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCGTCATGCAGAACTTC
CGCCTCAAGTCCTCCCAGTCACCTAAGGACATTGACGTGTCCCCCAAACACGTGGTCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 118 GenBank Gene ID NM_000764.2 Link Image
Enzyme 118 GeneCard ID CYP2A7 Link Image
Enzyme 118 GenAtlas ID Not Available
Enzyme 118 HGNC ID Not Available
Enzyme 118 Chromosome Location 1
Enzyme 118 Locus 19q13.2
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 General References
  1. Yamano S, Tatsuno J, Gonzalez FJ: The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. Biochemistry. 1990 Feb 6;29(5):1322-9. [PubMed Link Image]
  2. Fernandez-Salguero P, Hoffman SM, Cholerton S, Mohrenweiser H, Raunio H, Rautio A, Pelkonen O, Huang JD, Evans WE, Idle JR, et al.: A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. Am J Hum Genet. 1995 Sep;57(3):651-60. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 6863
Enzyme 119 Name Cytochrome P450 2A6
Enzyme 119 Synonyms
  1. CYPIIA6
  2. Coumarin 7-hydroxylase
  3. Cytochrome P450 IIA3
  4. Cytochrome P450(I)
Enzyme 119 Gene Name CYP2A6
Enzyme 119 Protein Sequence >Cytochrome P450 2A6 
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN
GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSN
VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI
GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLNEK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Enzyme 119 Number of Residues 494
Enzyme 119 Molecular Weight 56501.0
Enzyme 119 Theoretical pI 9.72
Enzyme 119 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 119 General Function Involved in monooxygenase activity
Enzyme 119 Specific Function Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Possesses low phenacetin O-deethylation activity
Enzyme 119 Pathways
Enzyme 119 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein 189339233 Link Image
Enzyme 119 UniProtKB/Swiss-Prot ID P11509 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name CP2A6_HUMAN Link Image
Enzyme 119 PDB ID Not Available
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence >1485 bp 
ATGCTGGCCTCAGGGATGCTTCTGGTGGCCTTGCTGGTCTGCCTGACTGTAATGGTCTTG
ATGTCTGTTTGGCAGCAGAGGAAGAGCAAGGGGAAGCTGCCTCCGGGACCCACCCCATTG
CCCTTCATTGGAAACTACCTGCAGCTGAACACAGAGCAGATGTACAACTCCCTCATGAAG
ATCAGTGAGCGCTATGGCCCCGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGTGGACATGATGCCGTCAGGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAAGCCACCTTCGACTGGGTCTTCAAAGGCTATGGCGTGGTATTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCGGCGCTTCTCCATCGCCACCCTGCGGGACTTCGGGGTG
GGCAAGCGAGGCATCGAGGAGCGCATCCAGGAGGAGGCGGGCTTCCTCATCGACGCCCTC
CGGGGCACTGGCGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATAAGGACAAAGAGTTCCTGTCA
CTGTTGCGCATGATGCTAGGAATCTTCCAGTTCACGTCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTCAGTTG
CTGCAAGGGCTGGAGGACTTCATAGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACGGGACTTCATTGACTCCTTTCTCATCCGCATGCAGGAGGAGGAGAAG
AACCCCAACACGGAGTTCTACTTGAAAAACCTGGTGATGACCACGTTGAACCTCTTCATT
GGGGGCACCGAGACCGTCAGCACCACCCTGCGCTATGGCTTCTTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGGCCAAGATGCCCTACATGGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACGTGATCCCCATGAGTTTGGCCCGCAGAGTCAAAAAGGACACCAAGTTT
CGGGATTTCTTCCTCCCTAAGGGCACCGAAGTGTACCCTATGCTGGGCTCTGTGCTGAGA
GACCCCAGTTTCTTCTCCAACCCCCAGGACTTCAATCCCCAGCACTTCCTGAATGAGAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGAACTGTTTC
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCGTCATGCAGAACTTC
CGCCTCAAGTCCTCCCAGTCACCTAAGGACATTGACGTGTCCCCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 119 GenBank Gene ID NM_000762.5 Link Image
Enzyme 119 GeneCard ID CYP2A6 Link Image
Enzyme 119 GenAtlas ID CYP2A6 Link Image
Enzyme 119 HGNC ID HGNC:2610 Link Image
Enzyme 119 Chromosome Location 1
Enzyme 119 Locus 19q13.2
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References
  1. Miles JS, Bickmore W, Brook JD, McLaren AW, Meehan R, Wolf CR: Close linkage of the human cytochrome P450IIA and P450IIB gene subfamilies: implications for the assignment of substrate specificity. Nucleic Acids Res. 1989 Apr 25;17(8):2907-17. [PubMed Link Image]
  2. Yamano S, Nagata K, Yamazoe Y, Kato R, Gelboin HV, Gonzalez FJ: cDNA and deduced amino acid sequences of human P450 IIA3 (CYP2A3). Nucleic Acids Res. 1989 Jun 26;17(12):4888. [PubMed Link Image]
  3. Yamano S, Tatsuno J, Gonzalez FJ: The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. Biochemistry. 1990 Feb 6;29(5):1322-9. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Maurice M, Emiliani S, Dalet-Beluche I, Derancourt J, Lange R: Isolation and characterization of a cytochrome P450 of the IIA subfamily from human liver microsomes. Eur J Biochem. 1991 Sep 1;200(2):511-7. [PubMed Link Image]
  8. Yun CH, Shimada T, Guengerich FP: Purification and characterization of human liver microsomal cytochrome P-450 2A6. Mol Pharmacol. 1991 Nov;40(5):679-85. [PubMed Link Image]
  9. Kitagawa K, Kunugita N, Kitagawa M, Kawamoto T: CYP2A6*6, a novel polymorphism in cytochrome p450 2A6, has a single amino acid substitution (R128Q) that inactivates enzymatic activity. J Biol Chem. 2001 May 25;276(21):17830-5. Epub 2001 Feb 16. [PubMed Link Image]
  10. Phillips IR, Shephard EA, Ashworth A, Rabin BR: Isolation and sequence of a human cytochrome P-450 cDNA clone. Proc Natl Acad Sci U S A. 1985 Feb;82(4):983-7. [PubMed Link Image]
  11. Yano JK, Hsu MH, Griffin KJ, Stout CD, Johnson EF: Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. Nat Struct Mol Biol. 2005 Sep;12(9):822-3. Epub 2005 Aug 7. [PubMed Link Image]
  12. Yano JK, Denton TT, Cerny MA, Zhang X, Johnson EF, Cashman JR: Synthetic inhibitors of cytochrome P-450 2A6: inhibitory activity, difference spectra, mechanism of inhibition, and protein cocrystallization. J Med Chem. 2006 Nov 30;49(24):6987-7001. [PubMed Link Image]
  13. DeVore NM, Smith BD, Urban MJ, Scott EE: Key residues controlling phenacetin metabolism by human cytochrome P450 2A enzymes. Drug Metab Dispos. 2008 Dec;36(12):2582-90. Epub 2008 Sep 8. [PubMed Link Image]
  14. Hadidi H, Zahlsen K, Idle JR, Cholerton S: A single amino acid substitution (Leu160His) in cytochrome P450 CYP2A6 causes switching from 7-hydroxylation to 3-hydroxylation of coumarin. Food Chem Toxicol. 1997 Sep;35(9):903-7. [PubMed Link Image]
  15. Oscarson M, McLellan RA, Gullsten H, Agundez JA, Benitez J, Rautio A, Raunio H, Pelkonen O, Ingelman-Sundberg M: Identification and characterisation of novel polymorphisms in the CYP2A locus: implications for nicotine metabolism. FEBS Lett. 1999 Oct 29;460(2):321-7. [PubMed Link Image]
  16. Ariyoshi N, Sawamura Y, Kamataki T: A novel single nucleotide polymorphism altering stability and activity of CYP2a6. Biochem Biophys Res Commun. 2001 Mar 2;281(3):810-4. [PubMed Link Image]
  17. Kiyotani K, Fujieda M, Yamazaki H, Shimada T, Guengerich FP, Parkinson A, Nakagawa K, Ishizaki T, Kamataki T: Twenty one novel single nucleotide polymorphisms (SNPs) of the CYP2A6 gene in Japanese and Caucasians. Drug Metab Pharmacokinet. 2002;17(5):482-7. [PubMed Link Image]
  18. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
  19. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  20. Mwenifumbo JC, Al Koudsi N, Ho MK, Zhou Q, Hoffmann EB, Sellers EM, Tyndale RF: Novel and established CYP2A6 alleles impair in vivo nicotine metabolism in a population of Black African descent. Hum Mutat. 2008 May;29(5):679-88. [PubMed Link Image]
  21. Ho MK, Mwenifumbo JC, Zhao B, Gillam EM, Tyndale RF: A novel CYP2A6 allele, CYP2A6*23, impairs enzyme function in vitro and in vivo and decreases smoking in a population of Black-African descent. Pharmacogenet Genomics. 2008 Jan;18(1):67-75. [PubMed Link Image]
Enzyme 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 6937
Enzyme 120 Name Neutrophil cytosol factor 2
Enzyme 120 Synonyms
  1. NCF-2
  2. 67 kDa neutrophil oxidase factor
  3. NADPH oxidase activator 2
  4. Neutrophil NADPH oxidase factor 2
  5. p67-phox
Enzyme 120 Gene Name NCF2
Enzyme 120 Protein Sequence >Neutrophil cytosol factor 2 
MSLVEAISLWNEGVLAADKKDWKGALDAFSAVQDPHSRICFNIGCMYTILKNMTEAEKAF
TRSINRDKHLAVAYFQRGMLYYQTEKYDLAIKDLKEALIQLRGNQLIDYKILGLQFKLFA
CEVLYNIAFMYAKKEEWKKAEEQLALATSMKSEPRHSKIDKAMECVWKQKLYEPVVIPVG
KLFRPNERQVAQLAKKDYLGKATVVASVVDQDSFSGFAPLQPQAAEPPPRPKTPEIFRAL
EGEAHRVLFGFVPETKEELQVMPGNIVFVLKKGNDNWATVMFNGQKGLVPCNYLEPVELR
IHPQQQPQEESSPQSDIPAPPSSKAPGRPQLSPGQKQKEEPKEVKLSVPMPYTLKVHYKY
TVVMKTQPGLPYSQVRDMVSKKLELRLEHTKLSYRPRDSNELVPLSEDSMKDAWGQVKNY
CLTLWCENTVGDQGFPDEPKESEKADANNQTTEPQLKKGSQVEALFSYEATQPEDLEFQE
GDIILVLSKVNEEWLEGECKGKVGIFPKVFVEDCATTDLESTRREV
Enzyme 120 Number of Residues 526
Enzyme 120 Molecular Weight 59761.1
Enzyme 120 Theoretical pI 6.02
Enzyme 120 GO Classification
Function
  • binding
Process
—
Component
—
Enzyme 120 General Function Involved in electron carrier activity
Enzyme 120 Specific Function NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production)
Enzyme 120 Pathways Not Available
Enzyme 120 Reactions Not Available
Enzyme 120 Pfam Domain Function
Enzyme 120 Signals
  • None
Enzyme 120 Transmembrane Regions
  • None
Enzyme 120 Essentiality Not Available
Enzyme 120 GenBank ID Protein 22023953 Link Image
Enzyme 120 UniProtKB/Swiss-Prot ID P19878 Link Image
Enzyme 120 UniProtKB/Swiss-Prot Entry Name NCF2_HUMAN Link Image
Enzyme 120 PDB ID 1HH8 Link Image
Enzyme 120 PDB File Show
Enzyme 120 3D Structure
Enzyme 120 Cellular Location Not Available
Enzyme 120 Gene Sequence >1581 bp 
ATGTCCCTGGTGGAGGCCATCAGCCTCTGGAATGAAGGGGTGCTGGCAGCGGACAAGAAG
GACTGGAAGGGAGCCCTGGATGCCTTCAGTGCCGTCCAGGACCCCCACTCCCGGATTTGC
TTCAACATTGGCTGCATGTACACTATCCTGAAGAACATGACTGAAGCAGAGAAGGCCTTT
ACCAGAAGCATTAACCGAGACAAGCACTTGGCAGTGGCTTACTTCCAACGAGGGATGCTC
TACTACCAGACAGAGAAATATGATTTGGCTATCAAAGACCTTAAAGAAGCCTTGATTCAG
CTTCGAGGGAACCAGCTGATAGACTATAAGATCCTGGGGCTCCAGTTCAAGCTGTTTGCC
TGTGAGGTGTTATATAACATTGCTTTCATGTATGCCAAGAAGGAGGAATGGAAAAAAGCT
GAAGAACAGTTAGCATTGGCCACGAGCATGAAGTCTGAGCCCAGACATTCCAAAATCGAC
AAGGCGATGGAGTGTGTCTGGAAGCAGAAGCTATATGAGCCAGTGGTGATCCCTGTGGGC
AGGCTGTTTCGACCAAATGAGAGACAAGTGGCTCAGCTGGCCAAGAAGGATTACCTAGGC
AAGGCGACGGTCGTGGCATCTGTGGTGGATCAAGACAGTTTCTCTGGGTTTGCCCCTCTG
CAACCACAGGCAGCTGAGCCTCCACCCAGACCGAAAACCCCAGAGATCTTCAGGGCTCTG
GAAGGGGAGGCTCACCGTGTGCTATTTGGGTTTGTGCCTGAGACAAAAGAAGAGCTCCAG
GTCATGCCAGGGAACATTGTCTTTGTCTTGAAGAAGGGCAATGATAACTGGGCCACGGTC
ATGTTCAACGGGCAGAAGGGGCTTGTTCCCTGCAACTACCTTGAACCAGTTGAGCTGCGG
ATCCACCCTCAGCAGCAGCCCCAGGAGGAAAGCTCTCCGCAGTCCGACATCCCAGCTCCT
CCTAGTTCCAAAGCCCCTGGAAGACCCCAGCTGTCACCAGGCCAGAAACAAAAAGAAGAG
CCTAAGGAAGTGAAGCTCAGTGTTCCCATGCCCTACACACTCAAGGTGCACTACAAGTAC
ACGGTAGTCATGAAGACTCAGCCCGGGCTCCCCTACAGCCAGGTCCGGGACATGGTGTCT
AAGAAACTGGAGCTCCGGCTGGAACACACTAAGCTGAGCTATCGGCCTCGGGACAGCAAT
GAGCTGGTGCCCCTTTCAGAAGACAGCATGAAGGATGCCTGGGGCCAGGTGAAAAACTAC
TGCCTGACTCTGTGGTGTGAGAACACAGTGGGTGACCAAGGCTTTCCAGATGAACCCAAG
GAAAGTGAAAAAGCTGATGCTAATAACCAGACAACAGAACCTCAGCTTAAGAAAGGCAGC
CAAGTGGAGGCACTCTTCAGTTATGAGGCTACCCAACCAGAGGACCTGGAGTTTCAGGAA
GGGGATATAATCCTGGTGTTATCAAAGGTGAATGAAGAATGGCTGGAAGGGGAGTGCAAA
GGGAAGGTGGGCATTTTCCCCAAAGTTTTTGTTGAAGACTGCGCAACTACAGATTTGGAA
AGCACTCGGAGAGAAGTCTAG
Enzyme 120 GenBank Gene ID AF527950 Link Image
Enzyme 120 GeneCard ID NCF2 Link Image
Enzyme 120 GenAtlas ID Not Available
Enzyme 120 HGNC ID Not Available
Enzyme 120 Chromosome Location 1
Enzyme 120 Locus 1q25
Enzyme 120 SNPs SNPJam Report Link Image
Enzyme 120 General References
  1. Leto TL, Lomax KJ, Volpp BD, Nunoi H, Sechler JM, Nauseef WM, Clark RA, Gallin JI, Malech HL: Cloning of a 67-kD neutrophil oxidase factor with similarity to a noncatalytic region of p60c-src. Science. 1990 May 11;248(4956):727-30. [PubMed Link Image]
  2. Kenney RT, Malech HL, Epstein ND, Roberts RL, Leto TL: Characterization of the p67phox gene: genomic organization and restriction fragment length polymorphism analysis for prenatal diagnosis in chronic granulomatous disease. Blood. 1993 Dec 15;82(12):3739-44. [PubMed Link Image]
  3. Yoshida L, Nishida S, Shimoyama T, Kawahara T, Rokutan K, Tsunawaki S: Expression of a p67(phox) homolog in Caco-2 cells giving O(2)(-)-reconstituting ability to cytochrome b(558) together with recombinant p47(phox). Biochem Biophys Res Commun. 2002 Sep 6;296(5):1322-8. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. McAdara Berkowitz JK, Catz SD, Johnson JL, Ruedi JM, Thon V, Babior BM: JFC1, a novel tandem C2 domain-containing protein associated with the leukocyte NADPH oxidase. J Biol Chem. 2001 Jun 1;276(22):18855-62. Epub 2001 Mar 13. [PubMed Link Image]
  8. Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H: Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003 Jul 4;278(27):25234-46. Epub 2003 Apr 25. [PubMed Link Image]
  9. Lapouge K, Smith SJ, Walker PA, Gamblin SJ, Smerdon SJ, Rittinger K: Structure of the TPR domain of p67phox in complex with Rac.GTP. Mol Cell. 2000 Oct;6(4):899-907. [PubMed Link Image]
  10. de Boer M, Hilarius-Stokman PM, Hossle JP, Verhoeven AJ, Graf N, Kenney RT, Seger R, Roos D: Autosomal recessive chronic granulomatous disease with absence of the 67-kD cytosolic NADPH oxidase component: identification of mutation and detection of carriers. Blood. 1994 Jan 15;83(2):531-6. [PubMed Link Image]
  11. Bonizzato A, Russo MP, Donini M, Dusi S: Identification of a double mutation (D160V-K161E) in the p67phox gene of a chronic granulomatous disease patient. Biochem Biophys Res Commun. 1997 Feb 24;231(3):861-3. [PubMed Link Image]
  12. Patino PJ, Rae J, Noack D, Erickson R, Ding J, de Olarte DG, Curnutte JT: Molecular characterization of autosomal recessive chronic granulomatous disease caused by a defect of the nicotinamide adenine dinucleotide phosphate (reduced form) oxidase component p67-phox. Blood. 1999 Oct 1;94(7):2505-14. [PubMed Link Image]
  13. Noack D, Rae J, Cross AR, Munoz J, Salmen S, Mendoza JA, Rossi N, Curnutte JT, Heyworth PG: Autosomal recessive chronic granulomatous disease caused by novel mutations in NCF-2, the gene encoding the p67-phox component of phagocyte NADPH oxidase. Hum Genet. 1999 Nov;105(5):460-7. [PubMed Link Image]
Enzyme 120 Metabolite References Not Available
Enzyme 121 [top]
Enzyme 121 ID 6938
Enzyme 121 Name Neutrophil cytosol factor 4
Enzyme 121 Synonyms
  1. NCF-4
  2. Neutrophil NADPH oxidase factor 4
  3. SH3 and PX domain-containing protein 4
  4. p40-phox
  5. p40phox
Enzyme 121 Gene Name NCF4
Enzyme 121 Protein Sequence >Neutrophil cytosol factor 4 
MAVAQQLRAESDFEQLPDDVAISANIADIEEKRGFTSHFVFVIEVKTKGGSKYLIYRRYR
QFHALQSKLEERFGPDSKSSALACTLPTLPAKVYVGVKQEIAEMRIPALNAYMKSLLSLP
VWVLMDEDVRIFFYQSPYDSEQVPQALRRLRPRTRKVKSVSPQGNSVDRMAAPRAEALFD
FTGNSKLELNFKAGDVIFLLSRINKDWLEGTVRGATGIFPLSFVKILKDFPEEDDPTNWL
RCYYYEDTISTIKDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLVRLLSD
EDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVYNTMP
Enzyme 121 Number of Residues 339
Enzyme 121 Molecular Weight 39031.3
Enzyme 121 Theoretical pI 6.81
Enzyme 121 GO Classification
Function
  • binding
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
Component
—
Enzyme 121 General Function Involved in protein binding
Enzyme 121 Specific Function Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex
Enzyme 121 Pathways Not Available
Enzyme 121 Reactions Not Available
Enzyme 121 Pfam Domain Function
Enzyme 121 Signals
  • None
Enzyme 121 Transmembrane Regions
  • None
Enzyme 121 Essentiality Not Available
Enzyme 121 GenBank ID Protein 47519798 Link Image
Enzyme 121 UniProtKB/Swiss-Prot ID Q15080 Link Image
Enzyme 121 UniProtKB/Swiss-Prot Entry Name NCF4_HUMAN Link Image
Enzyme 121 PDB ID 1H6H Link Image
Enzyme 121 PDB File Show
Enzyme 121 3D Structure
Enzyme 121 Cellular Location Not Available
Enzyme 121 Gene Sequence >1020 bp 
ATGGCTGTGGCCCAGCAGCTGCGGGCCGAGAGTGACTTTGAACAGCTTCCGGATGATGTT
GCCATCTCGGCCAACATTGCTGACATCGAGGAGAAGAGAGGCTTCACCAGCCACTTTGTT
TTCGTCATCGAGGTGAAGACAAAAGGAGGATCCAAGTACCTCATCTACCGCCGCTACCGC
CAGTTCCATGCTTTGCAGAGCAAGCTGGAGGAGCGCTTCGGGCCAGACAGCAAGAGCAGT
GCCCTGGCCTGTACCCTGCCCACACTCCCAGCCAAAGTCTACGTGGGTGTGAAACAGGAG
ATCGCCGAGATGCGGATACCTGCCCTCAACGCCTACATGAAGAGCCTGCTCAGCCTGCCG
GTCTGGGTGCTGATGGATGAGGACGTCCGGATCTTCTTTTACCAGTCGCCCTATGACTCA
GAGCAGGTGCCCCAGGCACTCCGCCGGCTCCGCCCGCGCACCCGGAAAGTCAAGAGCGTG
TCCCCACAGGGCAACAGCGTTGACCGCATGGCAGCTCCGAGAGCAGAGGCTCTATTTGAC
TTCACTGGAAACAGCAAACTGGAGCTGAATTTCAAAGCTGGAGATGTGATCTTCCTCCTC
AGTCGGATCAACAAAGACTGGCTGGAGGGCACTGTCCGGGGAGCCACGGGCATCTTCCCT
CTCTCCTTCGTGAAGATCCTCAAAGACTTCCCTGAGGAGGACGACCCCACCAACTGGCTG
CGTTGCTACTACTACGAAGACACCATCAGCACCATCAAGGACATCGCGGTGGAGGAAGAT
CTCAGCAGCACTCCCCTATTGAAAGACCTGCTGGAGCTCACAAGGCGGGAGTTCCAGAGA
GAGGACATAGCTCTGAATTACCGGGACGCTGAGGGGGATCTGGTTCGGCTGCTGTCGGAT
GAGGACGTAGCGCTCATGGTGCGGCAGGCTCGTGGCCTCCCCTCCCAGAAGCGCCTCTTC
CCCTGGAAGCTGCACATCACGCAGAAGGACAACTACAGGGTCTACAACACGATGCCATGA
Enzyme 121 GenBank Gene ID NM_000631.4 Link Image
Enzyme 121 GeneCard ID NCF4 Link Image
Enzyme 121 GenAtlas ID NCF4 Link Image
Enzyme 121 HGNC ID HGNC:7662 Link Image
Enzyme 121 Chromosome Location 2
Enzyme 121 Locus 22q13.1
Enzyme 121 SNPs SNPJam Report Link Image
Enzyme 121 General References
  1. Wientjes FB, Hsuan JJ, Totty NF, Segal AW: p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem J. 1993 Dec 15;296 ( Pt 3):557-61. [PubMed Link Image]
  2. Zhan S, Vazquez N, Zhan S, Wientjes FB, Budarf ML, Schrock E, Ried T, Green ED, Chanock SJ: Genomic structure, chromosomal localization, start of transcription, and tissue expression of the human p40-phox, a new component of the nicotinamide adenine dinucleotide phosphate-oxidase complex. Blood. 1996 Oct 1;88(7):2714-21. [PubMed Link Image]
  3. Hasebe T, Someya A, Nagaoka I: Identification of a splice variant mRNA of p40phox, an NADPH oxidase component of phagocytes. FEBS Lett. 1999 Jul 23;455(3):257-61. [PubMed Link Image]
  4. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  5. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bouin AP, Grandvaux N, Vignais PV, Fuchs A: p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase. Implication of a protein kinase c-type kinase in the phosphorylation process. J Biol Chem. 1998 Nov 13;273(46):30097-103. [PubMed Link Image]
  8. Bravo J, Karathanassis D, Pacold CM, Pacold ME, Ellson CD, Anderson KE, Butler PJ, Lavenir I, Perisic O, Hawkins PT, Stephens L, Williams RL: The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol Cell. 2001 Oct;8(4):829-39. [PubMed Link Image]
  9. Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL: PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mol Cell. 2003 Jul;12(1):39-50. [PubMed Link Image]
  10. Massenet C, Chenavas S, Cohen-Addad C, Dagher MC, Brandolin G, Pebay-Peyroula E, Fieschi F: Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains. J Biol Chem. 2005 Apr 8;280(14):13752-61. Epub 2005 Jan 18. [PubMed Link Image]
Enzyme 121 Metabolite References Not Available
Enzyme 122 [top]
Enzyme 122 ID 6952
Enzyme 122 Name 25-hydroxycholesterol 7-alpha-hydroxylase
Enzyme 122 Synonyms
  1. Oxysterol 7-alpha-hydroxylase
  2. Cytochrome P450 7B1
Enzyme 122 Gene Name CYP7B1
Enzyme 122 Protein Sequence >25-hydroxycholesterol 7-alpha-hydroxylase 
MAGEVSAATGRFSLERLGLPGLALAAALLLLALCLLVRRTRRPGEPPLIKGWLPYLGVVL
NLRKDPLRFMKTLQKQHGDTFTVLLGGKYITFILDPFQYQLVIKNHKQLSFRVFSNKLLE
KAFSISQLQKNHDMNDELHLCYQFLQGKSLDILLESMMQNLKQVFEPQLLKTTSWDTAEL
YPFCSSIIFEITFTTIYGKVIVCDNNKFISELRDDFLKFDDKFAYLVSNIPIELLGNVKS
IREKIIKCFSSEKLAKMQGWSEVFQSRQDVLEKYYVHEDLEIGAHHLGFLWASVANTIPT
MFWAMYYLLRHPEAMAAVRDEIDRLLQSTGQKKGSGFPIHLTREQLDSLICLESSIFEAL
RLSSYSTTIRFVEEDLTLSSETGDYCVRKGDLVAIFPPVLHGDPEIFEAPEEFRYDRFIE
DGKKKTTFFKRGKKLKCYLMPFGTGTSKCPGRFFALMEIKQLLVILLTYFDLEIIDDKPI
GLNYSRLLFGIQYPDSDVLFRYKVKS
Enzyme 122 Number of Residues 506
Enzyme 122 Molecular Weight 58255.3
Enzyme 122 Theoretical pI 8.13
Enzyme 122 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
—
Component
—
Enzyme 122 General Function Involved in monooxygenase activity
Enzyme 122 Specific Function Cholest-5-ene-3-beta,25-diol + NADPH + O(2) = cholest-5-ene-3-beta,7-alpha,25-triol + NADP(+) + H(2)O
Enzyme 122 Pathways Not Available
Enzyme 122 Reactions
  • (1) cholest-5-ene-3beta,25-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,25-triol + NADP+ + H2O [RN:R07209]
  • (2) cholest-5-ene-3beta,27-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,27-triol + NADP+ + H2O [RN:R07372]
Enzyme 122 Pfam Domain Function
Enzyme 122 Signals
  • None
Enzyme 122 Transmembrane Regions
  • None
Enzyme 122 Essentiality Not Available
Enzyme 122 GenBank ID Protein 3702794 Link Image
Enzyme 122 UniProtKB/Swiss-Prot ID O75881 Link Image
Enzyme 122 UniProtKB/Swiss-Prot Entry Name CP7B1_HUMAN Link Image
Enzyme 122 PDB ID Not Available
Enzyme 122 Cellular Location Not Available
Enzyme 122 Gene Sequence >1521 bp 
ATGGCAGGAGAAGTGTCCGCGGCCACGGGCCGCTTTTCGCTGGAGCGGTTGGGCCTCCCG
GGCCTGGCCCTCGCCGCGGCCCTGCTGCTCCTGGCCCTCTGCTTGCTTGTCCGGCGCACC
AGGAGACCCGGTGAGCCTCCATTGATAAAAGGTTGGCTTCCTTATCTTGGAGTGGTCCTG
AACTTACGAAAAGACCCCTTAAGGTTCATGAAAACACTTCAAAAGCAACATGGTGACACT
TTCACAGTTCTTCTTGGTGGAAAGTACATAACATTTATCCTGGACCCCTTCCAGTACCAG
CTAGTGATAAAAAATCATAAACAATTAAGCTTTCGAGTATTTTCTAATAAATTATTAGAG
AAAGCATTTAGCATCAGTCAGTTGCAAAAAAATCATGACATGAATGATGAGCTTCACCTC
TGCTATCAATTTTTGCAAGGCAAATCTTTGGACATACTCTTGGAAAGCATGATGCAGAAT
CTAAAACAAGTTTTTGAACCCCAGCTGTTAAAAACCACAAGTTGGGACACGGCAGAACTG
TATCCATTCTGCAGCTCAATAATATTTGAGATCACATTTACAACTATATATGGAAAAGTT
ATTGTTTGTGACAACAACAAATTTATTAGTGAGCTAAGAGATGATTTTTTAAAATTTGAT
GACAAGTTTGCATATTTAGTATCCAACATACCCATTGAGCTTCTAGGAAATGTCAAGTCT
ATTAGAGAGAAAATTATAAAATGCTTCTCATCAGAAAAGTTAGCCAAGATGCAAGGATGG
TCAGAAGTTTTTCAAAGCAGGCAAGATGTCCTGGAGAAATATTATGTGCACGAGGACCTT
GAAATAGGAGCACATCATTTAGGCTTTCTCTGGGCCTCTGTGGCAAACACTATTCCAACT
ATGTTCTGGGCAATGTATTATCTTCTGCGGCACCCAGAAGCTATGGCAGCAGTGCGTGAC
GAAATTGACCATTTGCTGCAGTCAACAGGTCAAAAGAAAGGGTCTGGATTTCCCATCCAC
CTCACCAGAGAACAATTGGACAGCCTAATCTGCCTAGAAAGCAGCATTTTTGAAGCTTTA
CGACTGTCCTCATATTCAACCACCATTCGTTTTGTTGAGGAGGATTTGACTCTCAGTTCA
GAGACCGGGGACTACTGTGTGCGAAAGGGAGACTTGGTAGCCATCTTTCCTCCAGTCCTA
CATGGTGACCCTGAAATCTTTGAAGCTCCAGAGGAGTTTAGATATGATCGTTTTATAGAA
GATGGTAAGAAGAAAACCACCTTTTTCAAAAGAGGGAAAAAGCTGAAGTGTTACCTAATG
CCGTTTGGAACTGGAACCAGCAAATGTCCAGGCCGATTTTTTGCACTTATGGAAATAAAA
CAATTGTTGGTTATACTTTTAACTTATTTTGATTTAGAAATAATTGATGATAAGCCCATA
GGACTAAACTACAGCCGCTTGTTGTTTGGTATTCAGTATCCAGATTCTGATGTTTTATTT
AGATACAAAGTGAAATCTTAG
Enzyme 122 GenBank Gene ID AF029403 Link Image
Enzyme 122 GeneCard ID CYP7B1 Link Image
Enzyme 122 GenAtlas ID CYP7B1 Link Image
Enzyme 122 HGNC ID HGNC:2652 Link Image
Enzyme 122 Chromosome Location 8
Enzyme 122 Locus 8q21.3
Enzyme 122 SNPs SNPJam Report Link Image
Enzyme 122 General References
  1. Setchell KD, Schwarz M, O'Connell NC, Lund EG, Davis DL, Lathe R, Thompson HR, Weslie Tyson R, Sokol RJ, Russell DW: Identification of a new inborn error in bile acid synthesis: mutation of the oxysterol 7alpha-hydroxylase gene causes severe neonatal liver disease. J Clin Invest. 1998 Nov 1;102(9):1690-703. [PubMed Link Image]
  2. Wu Z, Martin KO, Javitt NB, Chiang JY: Structure and functions of human oxysterol 7alpha-hydroxylase cDNAs and gene CYP7B1. J Lipid Res. 1999 Dec;40(12):2195-203. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Tsaousidou MK, Ouahchi K, Warner TT, Yang Y, Simpson MA, Laing NG, Wilkinson PA, Madrid RE, Patel H, Hentati F, Patton MA, Hentati A, Lamont PJ, Siddique T, Crosby AH: Sequence alterations within CYP7B1 implicate defective cholesterol homeostasis in motor-neuron degeneration. Am J Hum Genet. 2008 Feb;82(2):510-5. Epub 2008 Jan 18. [PubMed Link Image]
Enzyme 122 Metabolite References Not Available
Enzyme 123 [top]
Enzyme 123 ID 7026
Enzyme 123 Name NAD(P)H dehydrogenase [quinone] 1
Enzyme 123 Synonyms
  1. Azoreductase
  2. DT-diaphorase
  3. DTD
  4. Menadione reductase
  5. NAD(P)H:quinone oxidoreductase 1
  6. Phylloquinone reductase
  7. Quinone reductase 1
  8. QR1
Enzyme 123 Gene Name NQO1
Enzyme 123 Protein Sequence >NAD(P)H dehydrogenase [quinone] 1 
MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKL
KDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERV
FIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFC
GFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMK
KEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK
Enzyme 123 Number of Residues 274
Enzyme 123 Molecular Weight 30867.4
Enzyme 123 Theoretical pI 9.34
Enzyme 123 GO Classification
Function
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • electron carrier activity
  • oxidoreductase activity
Process
—
Component
—
Enzyme 123 General Function Involved in electron carrier activity
Enzyme 123 Specific Function The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis
Enzyme 123 Pathways Not Available
Enzyme 123 Reactions
  • NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone [RN:R07358 R07359]
Enzyme 123 Pfam Domain Function
Enzyme 123 Signals
  • None
Enzyme 123 Transmembrane Regions
  • None
Enzyme 123 Essentiality Not Available
Enzyme 123 GenBank ID Protein Not Available
Enzyme 123 UniProtKB/Swiss-Prot ID P15559 Link Image
Enzyme 123 UniProtKB/Swiss-Prot Entry Name NQO1_HUMAN Link Image
Enzyme 123 PDB ID 1KBQ Link Image
Enzyme 123 PDB File Show
Enzyme 123 3D Structure
Enzyme 123 Cellular Location Not Available
Enzyme 123 Gene Sequence >825 bp 
ATGGTCGGCAGAAGAGCACTGATCGTACTGGCTCACTCAGAGAGGACCTCCTTCAACTAT
GCCATGAAGGAGGCTGCTGCAGCGGCTTTGAAGAAGAAAGGATGGGAGGTGGTGGAGTCG
GACCTCTATGCCATGAACTTCAATCCCATCATTTCCAGAAAGGACATCACAGGTAAACTG
AAGGACCCTGCGAACTTTCAGTATCCTGCCGAGTCTGTTCTGGCTTATAAAGAAGGCCAT
CTGAGCCCAGATATTGTGGCTGAACAAAAGAAGCTGGAAGCCGCAGACCTTGTGATATTC
CAGTTCCCCCTGCAGTGGTTTGGAGTCCCTGCCATTCTGAAAGGCTGGTTTGAGCGAGTG
TTCATAGGAGAGTTTGCTTACACTTACGCTGCCATGTATGACAAAGGACCCTTCCGGAGT
AAGAAGGCAGTGCTTTCCATCACCACTGGTGGCAGTGGCTCCATGTACTCTCTGCAAGGG
ATCCACGGGGACATGAATGTCATTCTCTGGCCAATTCAGAGTGGCATTCTGCATTTCTGT
GGCTTCCAAGTCTTAGAACCTCAACTGACATATAGCATTGGGCACACTCCAGCAGACGCC
CGAATTCAAATCCTGGAAGGATGGAAGAAACGCCTGGAGAATATTTGGGATGAGACACCA
CTGTATTTTGCTCCAAGCAGCCTCTTTGACCTAAACTTCCAGGCAGGATTCTTAATGAAA
AAAGAGGTACAGGATGAGGAGAAAAACAAGAAATTTGGCCTTTCTGTGGGCCATCACTTG
GGCAAGTCCATCCCAACTGACAACCAGATCAAAGCTAGAAAATGA
Enzyme 123 GenBank Gene ID J03934 Link Image
Enzyme 123 GeneCard ID NQO1 Link Image
Enzyme 123 GenAtlas ID NQO1 Link Image
Enzyme 123 HGNC ID HGNC:2874 Link Image
Enzyme 123 Chromosome Location 1
Enzyme 123 Locus 16q22.1
Enzyme 123 SNPs SNPJam Report Link Image
Enzyme 123 General References
  1. Jaiswal AK, McBride OW, Adesnik M, Nebert DW: Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16. J Biol Chem. 1988 Sep 25;263(27):13572-8. [PubMed Link Image]
  2. Jaiswal AK: Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin. Biochemistry. 1991 Nov 5;30(44):10647-53. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Skelly JV, Sanderson MR, Suter DA, Baumann U, Read MA, Gregory DS, Bennett M, Hobbs SM, Neidle S: Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954). J Med Chem. 1999 Oct 21;42(21):4325-30. [PubMed Link Image]
  7. Faig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D, Amzel LM: Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3177-82. [PubMed Link Image]
  8. Winski SL, Faig M, Bianchet MA, Siegel D, Swann E, Fung K, Duncan MW, Moody CJ, Amzel LM, Ross D: Characterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass spectrometric approaches. Biochemistry. 2001 Dec 18;40(50):15135-42. [PubMed Link Image]
  9. Faig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM: Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones. Structure. 2001 Aug;9(8):659-67. [PubMed Link Image]
  10. Asher G, Dym O, Tsvetkov P, Adler J, Shaul Y: The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry. 2006 May 23;45(20):6372-8. [PubMed Link Image]
  11. Traver RD, Horikoshi T, Danenberg KD, Stadlbauer TH, Danenberg PV, Ross D, Gibson NW: NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity. Cancer Res. 1992 Feb 15;52(4):797-802. [PubMed Link Image]
  12. Kristiansen OP, Larsen ZM, Johannesen J, Nerup J, Mandrup-Poulsen T, Pociot F: No linkage of P187S polymorphism in NAD(P)H: quinone oxidoreductase (NQO1/DIA4) and type 1 diabetes in the Danish population. DIEGG and DSGD. Danish IDDM Epidemiology and Genetics Group and The Danish Study Group of Diabetes in Childhood. Hum Mutat. 1999;14(1):67-70. [PubMed Link Image]
Enzyme 123 Metabolite References Not Available
Enzyme 124 [top]
Enzyme 124 ID 7029
Enzyme 124 Name Glutaredoxin-1
Enzyme 124 Synonyms
  1. Thioltransferase-1
  2. TTase-1
Enzyme 124 Gene Name GLRX
Enzyme 124 Protein Sequence >Glutaredoxin-1 
MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDY
LQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ
Enzyme 124 Number of Residues 106
Enzyme 124 Molecular Weight 11775.7
Enzyme 124 Theoretical pI 8.21
Enzyme 124 GO Classification
Function
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron carrier activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • protein disulfide oxidoreductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
Component
—
Enzyme 124 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 124 Specific Function Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins
Enzyme 124 Pathways Not Available
Enzyme 124 Reactions Not Available
Enzyme 124 Pfam Domain Function
Enzyme 124 Signals
  • None
Enzyme 124 Transmembrane Regions
  • None
Enzyme 124 Essentiality Not Available
Enzyme 124 GenBank ID Protein 3603310 Link Image
Enzyme 124 UniProtKB/Swiss-Prot ID P35754 Link Image
Enzyme 124 UniProtKB/Swiss-Prot Entry Name GLRX1_HUMAN Link Image
Enzyme 124 PDB ID 1JHB Link Image
Enzyme 124 PDB File Show
Enzyme 124 3D Structure
Enzyme 124 Cellular Location Not Available
Enzyme 124 Gene Sequence >321 bp 
ATGGCTCAAGAGTTTGTGAACTGCAAAATCCAGCCTGGGAAGGTGGTTGTGTTCATCAAG
CCCACCTGCCCGTACTGCAGGAGGGCCCAAGAGATCCTCAGTCAATTGCCCATCAAACAA
GGGCTTCTGGAATTTGTCGATATCACAGCCACCAACCACACTAACGAGATTCAAGATTAT
TTGCAACAGCTCACGGGAGCAAGAACGGTGCCTCGAGTCTTTATTGGTAAAGATTGTATA
GGCGGATGCAGTGATCTAGTCTCTTTGCAACAGAGTGGGGAACTGCTGACGCGGCTAAAG
CAGATTGGAGCTCTGCAGTAA
Enzyme 124 GenBank Gene ID AF069668 Link Image
Enzyme 124 GeneCard ID GLRX Link Image
Enzyme 124 GenAtlas ID Not Available
Enzyme 124 HGNC ID Not Available
Enzyme 124 Chromosome Location 5
Enzyme 124 Locus 5q14
Enzyme 124 SNPs SNPJam Report Link Image
Enzyme 124 General References
  1. Fernando MR, Sumimoto H, Nanri H, Kawabata S, Iwanaga S, Minakami S, Fukumaki Y, Takeshige K: Cloning and sequencing of the cDNA encoding human glutaredoxin. Biochim Biophys Acta. 1994 Jun 21;1218(2):229-31. [PubMed Link Image]
  2. Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A: Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. Eur J Biochem. 1995 Jan 15;227(1-2):27-34. [PubMed Link Image]
  3. Park JB, Levine M: Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin. Biochem J. 1996 May 1;315 ( Pt 3):931-8. [PubMed Link Image]
  4. Park JB, Levine M: The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis. Gene. 1997 Sep 15;197(1-2):189-93. [PubMed Link Image]
  5. Qiao F, Xing K, Liu A, Ehlers N, Raghavachari N, Lou MF: Human lens thioltransferase: cloning, purification, and function. Invest Ophthalmol Vis Sci. 2001 Mar;42(3):743-51. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Papov VV, Gravina SA, Mieyal JJ, Biemann K: The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells. Protein Sci. 1994 Mar;3(3):428-34. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Sun C, Berardi MJ, Bushweller JH: The NMR solution structure of human glutaredoxin in the fully reduced form. J Mol Biol. 1998 Jul 24;280(4):687-701. [PubMed Link Image]
  11. Yang Y, Jao S, Nanduri S, Starke DW, Mieyal JJ, Qin J: Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Biochemistry. 1998 Dec 8;37(49):17145-56. [PubMed Link Image]
Enzyme 124 Metabolite References Not Available
Enzyme 125 [top]
Enzyme 125 ID 7114
Enzyme 125 Name Cytochrome b-245 heavy chain
Enzyme 125 Synonyms
  1. CGD91-phox
  2. Cytochrome b(558) subunit beta
  3. Cytochrome b558 subunit beta
  4. Heme-binding membrane glycoprotein gp91phox
  5. NADPH oxidase 2
  6. Neutrophil cytochrome b 91 kDa polypeptide
  7. Superoxide-generating NADPH oxidase heavy chain subunit
  8. gp91-1
  9. gp91-phox
  10. p22 phagocyte B-cytochrome
Enzyme 125 Gene Name CYBB
Enzyme 125 Protein Sequence >Cytochrome b-245 heavy chain 
MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACL
NFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHL
FNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGV
VITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHN
ITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKV
VTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGD
WTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASIL
KSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYL
TGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPE
ALAETLSKQSISNSESGPRGVHFIFNKENF
Enzyme 125 Number of Residues 570
Enzyme 125 Molecular Weight 65335.4
Enzyme 125 Theoretical pI 8.76
Enzyme 125 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleoside binding
  • oxidoreductase activity
  • purine nucleoside binding
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 125 General Function Involved in oxidoreductase activity
Enzyme 125 Specific Function Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc
Enzyme 125 Pathways Not Available
Enzyme 125 Reactions Not Available
Enzyme 125 Pfam Domain Function
Enzyme 125 Signals
  • None
Enzyme 125 Transmembrane Regions
  • 9-29 49-69 103-123 170-190 201-221 262-282
Enzyme 125 Essentiality Not Available
Enzyme 125 GenBank ID Protein 6996021 Link Image
Enzyme 125 UniProtKB/Swiss-Prot ID P04839 Link Image
Enzyme 125 UniProtKB/Swiss-Prot Entry Name CY24B_HUMAN Link Image
Enzyme 125 PDB ID Not Available
Enzyme 125 Cellular Location Not Available
Enzyme 125 Gene Sequence >1713 bp 
ATGGGGAACTGGGCTGTGAATGAGGGGCTCTCCATTTTTGTCATTCTGGTTTGGCTGGGG
TTGAACGTCTTCCTCTTTGTCTGGTATTACCGGGTTTATGATATTCCACCTAAGTTCTTT
TACACAAGAAAACTTCTTGGGTCAGCACTGGCACTGGCCAGGGCCCCTGCAGCCTGCCTG
AATTTCAACTGCATGCTGATTCTCTTGCCAGTCTGTCGAAATCTGCTGTCCTTCCTCAGG
GGTTCCAGTGCGTGCTGCTCAACAAGAGTTCGAAGACAACTGGACAGGAATCTCACCTTT
CATAAAATGGTGGCATGGATGATTGCACTTCACTCTGCGATTCACACCATTGCACATCTA
TTTAATGTGGAATGGTGTGTGAATGCCCGAGTCAATAATTCTGATCCTTATTCAGTAGCA
CTCTCTGAACTTGGAGACAGGCAAAATGAAAGTTATCTCAATTTTGCTCGAAAGAGAATA
AAGAACCCTGAAGGAGGCCTGTACCTGGCTGTGACCCTGTTGGCAGGCATCACTGGAGTT
GTCATCACGCTGTGCCTCATATTAATTATCACTTCCTCCACCAAAACCATCCGGAGGTCT
TACTTTGAAGTCTTTTGGTACACACATCATCTCTTTGTGATCTTCTTCATTGGCCTTGCC
ATCCATGGAGCTGAACGAATTGTACGTGGGCAGACCGCAGAGAGTTTGGCTGTGCATAAT
ATAACAGTTTGTGAACAAAAAATCTCAGAATGGGGAAAAATAAAGGAATGCCCAATCCCT
CAGTTTGCTGGAAACCCTCCTATGACTTGGAAATGGATAGTGGGTCCCATGTTTCTGTAT
CTCTGTGAGAGGTTGGTGCGGTTTTGGCGATCTCAACAGAAGGTGGTCATCACCAAGGTG
GTCACTCACCCTTTCAAAACCATCGAGCTACAGATGAAGAAGAAGGGGTTCAAAATGGAA
GTGGGACAATACATTTTTGTCAAGTGCCCAAAGGTGTCCAAGCTGGAGTGGCACCCTTTT
ACACTGACATCCGCCCCTGAGGAAGACTTCTTTAGTATCCATATCCGCATCGTTGGGGAC
TGGACAGAGGGGCTGTTCAATGCTTGTGGCTGTGATAAGCAGGAGTTTCAAGATGCGTGG
AAACTACCTAAGATAGCGGTTGATGGGCCCTTTGGCACTGCCAGTGAAGATGTGTTCAGC
TATGAGGTGGTGATGTTAGTGGGAGCAGGGATTGGGGTCACACCCTTCGCATCCATTCTC
AAGTCAGTCTGGTACAAATATTGCAATAACGCCACCAATCTGAAGCTCAAAAAGATCTAC
TTCTACTGGCTGTGCCGGGACACACATGCCTTTGAGTGGTTTGCAGATCTGCTGCAACTG
CTGGAGAGCCAGATGCAGGAAAGGAACAATGCCGGCTTCCTCAGCTACAACATCTACCTC
ACTGGCTGGGATGAGTCTCAGGCCAATCACTTTGCTGTGCACCATGATGAGGAGAAAGAT
GTGATCACAGGCCTGAAACAAAAGACTTTGTATGGACGGCCCAACTGGGATAATGAATTC
AAGACAATTGCAAGTCAACACCCTAATACCAGAATAGGAGTTTTCCTCTGTGGACCTGAA
GCCTTGGCTGAAACCCTGAGTAAACAAAGCATCTCCAACTCTGAGTCTGGCCCTCGGGGA
GTGCATTTCATTTTCAACAAGGAAAACTTCTAA
Enzyme 125 GenBank Gene ID NM_000397.3 Link Image
Enzyme 125 GeneCard ID CYBB Link Image
Enzyme 125 GenAtlas ID CYBB Link Image
Enzyme 125 HGNC ID HGNC:2578 Link Image
Enzyme 125 Chromosome Location Not Available
Enzyme 125 Locus Not Available
Enzyme 125 SNPs SNPJam Report Link Image
Enzyme 125 General References
  1. Royer-Pokora B, Kunkel LM, Monaco AP, Goff SC, Newburger PE, Baehner RL, Cole FS, Curnutte JT, Orkin SH: Cloning the gene for an inherited human disorder--chronic granulomatous disease--on the basis of its chromosomal location. Nature. 1986 Jul 3-9;322(6074):32-8. [PubMed Link Image]
  2. Jirapongsananuruk O, Niemela JE, Malech HL, Fleisher TA: CYBB mutation analysis in X-linked chronic granulomatous disease. Clin Immunol. 2002 Jul;104(1):73-6. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Dinauer MC, Orkin SH, Brown R, Jesaitis AJ, Parkos CA: The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex. Nature. 1987 Jun 25-Jul 1;327(6124):717-20. [PubMed Link Image]
  6. Kumatori A, Faizunnessa NN, Suzuki S, Moriuchi T, Kurozumi H, Nakamura M: Nonhomologous recombination between the cytochrome b558 heavy chain gene (CYBB) and LINE-1 causes an X-linked chronic granulomatous disease. Genomics. 1998 Oct 15;53(2):123-8. [PubMed Link Image]
  7. Teahan C, Rowe P, Parker P, Totty N, Segal AW: The X-linked chronic granulomatous disease gene codes for the beta-chain of cytochrome b-245. Nature. 1987 Jun 25-Jul 1;327(6124):720-1. [PubMed Link Image]
  8. Henderson LM, Meech RW: Evidence that the product of the human X-linked CGD gene, gp91-phox, is a voltage-gated H(+) pathway. J Gen Physiol. 1999 Dec;114(6):771-86. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  10. Dinauer MC, Curnutte JT, Rosen H, Orkin SH: A missense mutation in the neutrophil cytochrome b heavy chain in cytochrome-positive X-linked chronic granulomatous disease. J Clin Invest. 1989 Dec;84(6):2012-6. [PubMed Link Image]
  11. Bolscher BG, de Boer M, de Klein A, Weening RS, Roos D: Point mutations in the beta-subunit of cytochrome b558 leading to X-linked chronic granulomatous disease. Blood. 1991 Jun 1;77(11):2482-7. [PubMed Link Image]
  12. Ariga T, Sakiyama Y, Tomizawa K, Imajoh-Ohmi S, Kanegasaki S, Matsumoto S: A newly recognized point mutation in the cytochrome b558 heavy chain gene replacing alanine57 by glutamic acid, in a patient with cytochrome b positive X-linked chronic granulomatous disease. Eur J Pediatr. 1993 Jun;152(6):469-72. [PubMed Link Image]
  13. Ariga T, Sakiyama Y, Matsumoto S: Two novel point mutations in the cytochrome b 558 heavy chain gene, detected in two Japanese patients with X-linked chronic granulomatous disease. Hum Genet. 1994 Oct;94(4):441. [PubMed Link Image]
  14. Leusen JH, de Boer M, Bolscher BG, Hilarius PM, Weening RS, Ochs HD, Roos D, Verhoeven AJ: A point mutation in gp91-phox of cytochrome b558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-phox. J Clin Invest. 1994 May;93(5):2120-6. [PubMed Link Image]
  15. Hui YF, Chan SY, Lau YL: Identification of mutations in seven Chinese patients with X-linked chronic granulomatous disease. Blood. 1996 Nov 15;88(10):4021-8. [PubMed Link Image]
  16. Jendrossek V, Ritzel A, Neubauer B, Heyden S, Gahr M: An in-frame triplet deletion within the gp91-phox gene in an adult X-linked chronic granulomatous disease patient with residual NADPH-oxidase activity. Eur J Haematol. 1997 Feb;58(2):78-85. [PubMed Link Image]
  17. Rae J, Newburger PE, Dinauer MC, Noack D, Hopkins PJ, Kuruto R, Curnutte JT: X-Linked chronic granulomatous disease: mutations in the CYBB gene encoding the gp91-phox component of respiratory-burst oxidase. Am J Hum Genet. 1998 Jun;62(6):1320-31. [PubMed Link Image]
  18. Tsuda M, Kaneda M, Sakiyama T, Inana I, Owada M, Kiryu C, Shiraishi T, Kakinuma K: A novel mutation at a probable heme-binding ligand in neutrophil cytochrome b558 in atypical X-linked chronic granulomatous disease. Hum Genet. 1998 Oct;103(4):377-81. [PubMed Link Image]
  19. Dusi S, Nadalini KA, Donini M, Zentilin L, Wientjes FB, Roos D, Giacca M, Rossi F: Nicotinamide-adenine dinucleotide phosphate oxidase assembly and activation in EBV-transformed B lymphoblastoid cell lines of normal and chronic granulomatous disease patients. J Immunol. 1998 Nov 1;161(9):4968-74. [PubMed Link Image]
  20. Ariga T, Furuta H, Cho K, Sakiyama Y: Genetic analysis of 13 families with X-linked chronic granulomatous disease reveals a low proportion of sporadic patients and a high proportion of sporadic carriers. Pediatr Res. 1998 Jul;44(1):85-92. [PubMed Link Image]
  21. Roesler J, Heyden S, Burdelski M, Schafer H, Kreth HW, Lehmann R, Paul D, Marzahn J, Gahr M, Rosen-Wolff A: Uncommon missense and splice mutations and resulting biochemical phenotypes in German patients with X-linked chronic granulomatous disease. Exp Hematol. 1999 Mar;27(3):505-11. [PubMed Link Image]
  22. Patino PJ, Perez JE, Lopez JA, Condino-Neto A, Grumach AS, Botero JH, Curnutte JT, Garcia de Olarte D: Molecular analysis of chronic granulomatous disease caused by defects in gp91-phox. Hum Mutat. 1999;13(1):29-37. [PubMed Link Image]
  23. Ishibashi F, Nunoi H, Endo F, Matsuda I, Kanegasaki S: Statistical and mutational analysis of chronic granulomatous disease in Japan with special reference to gp91-phox and p22-phox deficiency. Hum Genet. 2000 May;106(5):473-81. [PubMed Link Image]
  24. Gerard B, El Benna J, Alcain F, Gougerot-Pocidalo MA, Grandchamp B, Chollet-Martin S: Characterization of 11 novel mutations in the X-linked chronic granulomatous disease (CYBB gene). Hum Mutat. 2001 Aug;18(2):163. [PubMed Link Image]
  25. Stasia MJ, Lardy B, Maturana A, Rousseau P, Martel C, Bordigoni P, Demaurex N, Morel F: Molecular and functional characterization of a new X-linked chronic granulomatous disease variant (X91+) case with a double missense mutation in the cytosolic gp91phox C-terminal tail. Biochim Biophys Acta. 2002 Apr 24;1586(3):316-30. [PubMed Link Image]
  26. Bionda C, Li XJ, van Bruggen R, Eppink M, Roos D, Morel F, Stasia MJ: Functional analysis of two-amino acid substitutions in gp91 phox in a patient with X-linked flavocytochrome b558-positive chronic granulomatous disease by means of transgenic PLB-985 cells. Hum Genet. 2004 Oct;115(5):418-27. Epub 2004 Aug 24. [PubMed Link Image]
Enzyme 125 Metabolite References Not Available
Enzyme 126 [top]
Enzyme 126 ID 7141
Enzyme 126 Name Ras-related C3 botulinum toxin substrate 2
Enzyme 126 Synonyms
  1. GX
  2. Small G protein
  3. p21-Rac2
Enzyme 126 Gene Name RAC2
Enzyme 126 Protein Sequence >Ras-related C3 botulinum toxin substrate 2 
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLR
DDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQ
PTRQQKRACSLL
Enzyme 126 Number of Residues 192
Enzyme 126 Molecular Weight 21428.6
Enzyme 126 Theoretical pI 7.70
Enzyme 126 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 126 General Function Involved in GTP binding
Enzyme 126 Specific Function Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase
Enzyme 126 Pathways Not Available
Enzyme 126 Reactions Not Available
Enzyme 126 Pfam Domain Function
Enzyme 126 Signals
  • None
Enzyme 126 Transmembrane Regions
  • None
Enzyme 126 Essentiality Not Available
Enzyme 126 GenBank ID Protein Not Available
Enzyme 126 UniProtKB/Swiss-Prot ID P15153 Link Image
Enzyme 126 UniProtKB/Swiss-Prot Entry Name RAC2_HUMAN Link Image
Enzyme 126 PDB ID 1DS6 Link Image
Enzyme 126 PDB File Show
Enzyme 126 3D Structure
Enzyme 126 Cellular Location Not Available
Enzyme 126 Gene Sequence >579 bp 
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGATGGGGCCGTGGGCAAGACCTGCCTTCTC
ATCAGCTACACCACCAACGCCTTTCCCGGAGAGTACATCCCCACCGTGTTTGACAACTAT
TCAGCCAATGTGATGGTGGACAGCAAGCCAGTGAACCTGGGGCTGTGGGACACTGCTGGG
CAGGAGGACTACGACCGTCTCCGGCCGCTCTCCTATCCACAGACGGACGTCTTCCTCATC
TGCTTCTCCCTCGTCAGCCCAGCCTCTTATGAGAACGTCCGCGCCAAGTGGTTCCCAGAA
GTGCGGCACCACTGCCCCAGCACACCCATCATCCTGGTGGGCACCAAGCTGGACCTGCGG
GACGACAAGGACACCATCGAGAAACTGAAGGAGAAGAAGCTGGCTCCCATCACCTACCCG
CAGGGCCTGGCACTGGCCAAGGAGATTGACTCGGTGAAATACCTGGAGTGCTCAGCCCTC
ACCCAGAGAGGCCTGAAAACCGTGTTCGACGAGGCCATCCGGGCCGTGCTGTGCCCTCAG
CCCACGCGGCAGCAGAAGCGCGCCTGCAGCCTCCTCTAG
Enzyme 126 GenBank Gene ID M29871 Link Image
Enzyme 126 GeneCard ID RAC2 Link Image
Enzyme 126 GenAtlas ID RAC2 Link Image
Enzyme 126 HGNC ID HGNC:9802 Link Image
Enzyme 126 Chromosome Location 2
Enzyme 126 Locus 22q13.1
Enzyme 126 SNPs SNPJam Report Link Image
Enzyme 126 General References
  1. Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R: rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989 Oct 5;264(28):16378-82. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Mizuno T, Kaibuchi K, Ando S, Musha T, Hiraoka K, Takaishi K, Asada M, Nunoi H, Matsuda I, Takai Y: Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins. J Biol Chem. 1992 May 25;267(15):10215-8. [PubMed Link Image]
  6. Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM: Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science. 1991 Dec 6;254(5037):1512-5. [PubMed Link Image]
  7. Reibel L, Dorseuil O, Stancou R, Bertoglio J, Gacon G: A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation. Biochem Biophys Res Commun. 1991 Mar 15;175(2):451-8. [PubMed Link Image]
  8. Kwong CH, Malech HL, Rotrosen D, Leto TL: Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry. 1993 Jun 1;32(21):5711-7. [PubMed Link Image]
  9. Kinsella BT, Erdman RA, Maltese WA: Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem. 1991 May 25;266(15):9786-94. [PubMed Link Image]
  10. Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P: The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat Struct Biol. 2000 Feb;7(2):122-6. [PubMed Link Image]
  13. Ambruso DR, Knall C, Abell AN, Panepinto J, Kurkchubasche A, Thurman G, Gonzalez-Aller C, Hiester A, deBoer M, Harbeck RJ, Oyer R, Johnson GL, Roos D: Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc Natl Acad Sci U S A. 2000 Apr 25;97(9):4654-9. [PubMed Link Image]
  14. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 126 Metabolite References Not Available
Enzyme 127 [top]
Enzyme 127 ID 7159
Enzyme 127 Name 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
Enzyme 127 Synonyms
  1. 24-OHase
  2. Vitamin D(3) 24-hydroxylase
  3. Cytochrome P450 24A1
  4. Cytochrome P450-CC24
Enzyme 127 Gene Name CYP24A1
Enzyme 127 Protein Sequence >1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial 
MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPG
PTSWPLLGSLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYR
TESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKIN
EVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIM
AIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSAD
FLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL
PENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGTVLMLNTQ
VLGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIV
RKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR
Enzyme 127 Number of Residues 514
Enzyme 127 Molecular Weight 58874.7
Enzyme 127 Theoretical pI 8.99
Enzyme 127 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 127 General Function Involved in monooxygenase activity
Enzyme 127 Specific Function Has a role in maintaining calcium homeostasis. Catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25- hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3)). The enzyme can perform up to 6 rounds of hydroxylation of calcitriol leading to calcitroic acid. It also shows 23- hydroxylating activity leading to 1-alpha,25-dihydroxyvitamin D(3)-26,23-lactone as end product
Enzyme 127 Pathways Not Available
Enzyme 127 Reactions Not Available
Enzyme 127 Pfam Domain Function
Enzyme 127 Signals
  • None
Enzyme 127 Transmembrane Regions
  • None
Enzyme 127 Essentiality Not Available
Enzyme 127 GenBank ID Protein 7939322 Link Image
Enzyme 127 UniProtKB/Swiss-Prot ID Q07973 Link Image
Enzyme 127 UniProtKB/Swiss-Prot Entry Name CP24A_HUMAN Link Image
Enzyme 127 PDB ID Not Available
Enzyme 127 Cellular Location Not Available
Enzyme 127 Gene Sequence >1545 bp 
ATGAGCTCCCCCATCAGCAAGAGCCGCTCGCTTGCCGCCTTCCTGCAGCAGCTGCGCAGT
CCGAGGCAGCCCCCGAGACTGGTGACATCTACGGCGTACACGTCCCCTCAGCCGCGAGAG
GTGCCAGTCTGCCCGCTGACAGCTGGTGGCGAGACTCAGAACGCGGCCGCCCTGCCGGGC
CCCACCAGCTGGCCACTGCTGGGCAGCCTGCTGCAGATTCTCTGGAAAGGGGGTCTCAAG
AAACAGCACGACACCCTGGTGGAGTACCACAAGAAGTATGGCAAGATTTTCCGCATGAAG
TTGGGTTCCTTTGAGTCGGTGCACCTGGGCTCGCCATGCCTGCTGGAAGCGCTGTACCGC
ACCGAGAGCGCGTACCCGCAGCGGCTGGAGATCAAACCGTGGAAGGCCTATCGCGACTAC
CGCAAAGAAGGCTACGGGCTGCTGATCCTGGAAGGGGAAGACTGGCAGCGGGTCCGGAGT
GCCTTTCAAAAGAAACTAATGAAACCAGGGGAAGTGATGAAGCTGGACAACAAAATCAAT
GAGGTCTTGGCCGATTTTATGGGCAGAATAGATGAGCTCTGTGATGAAAGAGGCCACGTT
GAAGACTTGTACAGCGAACTGAACAAATGGTCGTTTGAAAGTATCTGCCTCGTGTTGTAT
GAGAAGAGATTTGGGCTTCTCCAGAAGAATGCAGGGGATGAAGCTGTGAACTTCATCATG
GCCATCAAAACAATGATGAGCACGTTTGGGAGGATGATGGTCACTCCAGTCGAGCTGCAC
AAGAGCCTCAACACCAAGGTCTGGCAGGACCACACTCTGGCCTGGGACACCATTTTCAAA
TCAGTCAAAGCTTGTATCGACAACCGGTTAGAGAAGTATTCTCAGCAGCCTAGTGCAGAT
TTCCTTTGTGACATTTATCACCAGAATCGGCTTTCAAAGAAAGAATTGTATGCTGCTGTC
ACAGAGCTCCAGCTGGCTGCGGTGGAAACGACAGCAAACAGTCTAATGTGGATTCTCTAC
AATTTATCCCGTAATCCCCAAGTGCAACAAAAGCTTCTTAAGGAAATTCAAAGTGTATTA
CCTGAGAATCAGGTGCCACGGGCAGAAGATTTGAGGAATATGCCGTATTTAAAAGCCTGT
CTGAAAGAATCTATGAGGCTTACGCCGAGTGTACCATTTACAACTCGGACTCTTGACAAG
GCAACAGTTCTGGGTGAATATGCTTTACCCAAAGGAACAGTGCTCATGCTAAATACCCAG
GTGTTGGGATCCAGTGAAGACAATTTTGAAGATTCAAGTCAGTTTAGACCTGAACGTTGG
CTTCAGGAGAAGGAAAAAATTAATCCTTTTGCGCATCTTCCATTTGGCGTTGGAAAAAGA
ATGTGCATTGGTCGCCGATTAGCAGAGCTTCAACTGCATTTGGCTCTTTGTTGGATTGTC
CGCAAATACGACATCCAGGCCACAGACAATGAGCCTGTTGAGATGCTACACTCAGGCACC
CTGGTGCCCAGCCGGGAACTCCCCATCGCGTTTTGCCAGCGATAA
Enzyme 127 GenBank Gene ID AL138805 Link Image
Enzyme 127 GeneCard ID CYP24A1 Link Image
Enzyme 127 GenAtlas ID CYP24A1 Link Image
Enzyme 127 HGNC ID HGNC:2602 Link Image
Enzyme 127 Chromosome Location 2
Enzyme 127 Locus 20q13
Enzyme 127 SNPs SNPJam Report Link Image
Enzyme 127 General References
  1. Chen KS, Prahl JM, DeLuca HF: Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase cDNA. Proc Natl Acad Sci U S A. 1993 May 15;90(10):4543-7. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Chen KS, DeLuca HF: Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene promoter and identification of two vitamin D-responsive elements. Biochim Biophys Acta. 1995 Jul 25;1263(1):1-9. [PubMed Link Image]
  4. Labuda M, Lemieux N, Tihy F, Prinster C, Glorieux FH: Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets. J Bone Miner Res. 1993 Nov;8(11):1397-406. [PubMed Link Image]
  5. Sakaki T, Kagawa N, Yamamoto K, Inouye K: Metabolism of vitamin D3 by cytochromes P450. Front Biosci. 2005 Jan 1;10:119-34. Print 2005 Jan 1. [PubMed Link Image]
Enzyme 127 Metabolite References Not Available
Enzyme 128 [top]
Enzyme 128 ID 7310
Enzyme 128 Name Putative dimethylaniline monooxygenase [N-oxide-forming] 6
Enzyme 128 Synonyms
  1. Dimethylaniline oxidase 6
  2. Flavin-containing monooxygenase 6
  3. FMO 6
Enzyme 128 Gene Name FMO6P
Enzyme 128 Protein Sequence >Putative dimethylaniline monooxygenase [N-oxide-forming] 6 
MSKRVGIIGAGVSGLAAIWCCLEEGLEPTCFERSDDVGGLWKFSDHTEEGRASIYQSVFT
NSSKEMMCFPDFPYPDDYPNYIHHSKLQEYIKTYAQKKDLLRYIQFETLVSGIKKCPSFL
VTGQWVVVTEKDGKQESTIFDAVMICSGHHVYPNLPTDSFPGLDQFRGNYLHSRDYKNPE
AFKGKRVLVIGLGNSGSDIAVELSRLATQVIISTRSASWVMSRVWDDGYPWDMMYVTRFA
SFLRNVLPSFISDWLYVQKMNTWFKHENYGLMPLNGSLRKEPVFNDELPSRILCGTLSIK
PSVKEFTETSAVFEDGTMFEAIDSVIFATGYDYSYPFLDETIMKSRNNEVTLFKGIFPPL
MEKPTLAVIGLVQSLGAAIPTADLQAWWAAKVFANSCTLPTTNEMMDDTDEKMGKKLKCM
FSSFFMFGQSQTLQTDYITYVDELGSFIGAKPNIPWLFLTDPRLALEVYFGPCSPYQFRL
MGPGKWDGARNAILTQWNRTVKPTRTRVVSEVQRPHPFYNLLKMLSFPLLLLAVTLTFY
Enzyme 128 Number of Residues 539
Enzyme 128 Molecular Weight 61290.9
Enzyme 128 Theoretical pI 6.32
Enzyme 128 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • flavin-containing monooxygenase activity
  • monooxygenase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 128 General Function Involved in flavin-containing monooxygenase activity
Enzyme 128 Specific Function It is probable that this protein is only produced in very small quantity or not at all as the gene coding for it seems to be unable to produce full length transcripts
Enzyme 128 Pathways Not Available
Enzyme 128 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
Enzyme 128 Pfam Domain Function
Enzyme 128 Signals
  • None
Enzyme 128 Transmembrane Regions
  • 518-538
Enzyme 128 Essentiality Not Available
Enzyme 128 GenBank ID Protein Not Available
Enzyme 128 UniProtKB/Swiss-Prot ID O60774 Link Image
Enzyme 128 UniProtKB/Swiss-Prot Entry Name FMO6_HUMAN Link Image
Enzyme 128 PDB ID Not Available
Enzyme 128 Cellular Location Not Available
Enzyme 128 Gene Sequence Not Available
Enzyme 128 GenBank Gene ID Not Available
Enzyme 128 GeneCard ID FMO6P Link Image
Enzyme 128 GenAtlas ID FMO6P Link Image
Enzyme 128 HGNC ID HGNC:24024 Link Image
Enzyme 128 Chromosome Location 1
Enzyme 128 Locus 1q24.3
Enzyme 128 SNPs SNPJam Report Link Image
Enzyme 128 General References
  1. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  2. Hines RN, Hopp KA, Franco J, Saeian K, Begun FP: Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase. Mol Pharmacol. 2002 Aug;62(2):320-5. [PubMed Link Image]
  3. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
Enzyme 128 Metabolite References Not Available
Enzyme 129 [top]
Enzyme 129 ID 7345
Enzyme 129 Name 24-dehydrocholesterol reductase
Enzyme 129 Synonyms
  1. 3-beta-hydroxysterol delta-24-reductase
  2. Diminuto/dwarf1 homolog
  3. Seladin-1
Enzyme 129 Gene Name DHCR24
Enzyme 129 Protein Sequence >24-dehydrocholesterol reductase 
MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKL
SSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMD
ILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKY
GLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKL
RFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYY
KPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVP
PKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQ
PGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREE
FWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH
Enzyme 129 Number of Residues 516
Enzyme 129 Molecular Weight 60100.8
Enzyme 129 Theoretical pI 8.24
Enzyme 129 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • purine nucleoside binding
Process
—
Component
—
Enzyme 129 General Function Energy production and conversion
Enzyme 129 Specific Function Catalyzes the reduction of the delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis
Enzyme 129 Pathways Not Available
Enzyme 129 Reactions Not Available
Enzyme 129 Pfam Domain Function
Enzyme 129 Signals
  • 1-22
Enzyme 129 Transmembrane Regions
  • 32-52
Enzyme 129 Essentiality Not Available
Enzyme 129 GenBank ID Protein 10442025 Link Image
Enzyme 129 UniProtKB/Swiss-Prot ID Q15392 Link Image
Enzyme 129 UniProtKB/Swiss-Prot Entry Name DHC24_HUMAN Link Image
Enzyme 129 PDB ID Not Available
Enzyme 129 Cellular Location Not Available
Enzyme 129 Gene Sequence >1551 bp 
ATGGAGCCCGCCGTGTCGCTGGCCGTGTGCGCGCTGCTCTTCCTGCTGTGGGTGCGCCTG
AAGGGGCTGGAGTTCGTGCTCATCCACCAGCGCTGGGTGTTCGTGTGCCTCTTCCTCCTG
CCGCTCTCGCTTATCTTCGATATCTACTACTACGTGCGCGCCTGGGTGGTGTTCAAGCTC
AGCAGCGCTCCGCGCCTGCACGAGCAGCGCGTGCGGGACATCCAGAAGCAGGTGCGGGAA
TGGAAGGAGCAGGGTAGCAAGACCTTCATGTGCACGGGGCGCCCTGGCTGGCTCACTGTC
TCACTACGTGTCGGGAAGTACAAGAAGACACACAAAAACATCATGATCAACCTGATGGAC
ATTCTGGAAGTGGACACCAAGAAACAGATTGTCCGTGTGGAGCCCTTGGTGACCATGGGC
CAGGTGACTGCCCTGCTGACCTCCATTGGCTGGACTCTCCCCGTGTTGCCTGAGCTTGAT
GACCTCACAGTGGGGGGCTTGATCATGGGCACAGGCATCGAGTCATCATCCCACAAGTAC
GGCCTGTTCCAACACATCTGCACTGCTTACGAGCTGGTCCTGGCTGATGGCAGCTTTGTG
CGATGCACTCCGTCCGAAAACTCAGACCTGTTCTATGCCGTACCCTGGTCCTGTGGGACG
CTGGGTTTCCTGGTGGCCGCTGAGATCCGCATCATCCCTGCCAAGAAGTACGTCAAGCTG
CGTTTCGAGCCAGTGCGGGGCCTGGAGGCTATCTGTGCCAAGTTCACCCACGAGTCCCAG
CGGCAGGAGAACCACTTCGTGGAAGGGCTGCTCTACTCCCTGGATGAGGCTGTCATTATG
ACAGGGGTCATGACAGATGAGGCAGAGCCCAGCAAGCTGAATAGCATTGGCAATTACTAC
AAGCCGTGGTTCTTTAAGCATGTGGAGAACTATCTGAAGACAAACCGAGAGGGCCTGGAG
TACATTCCCTTGAGACACTACTACCACCGCCACACGCGCAGCATCTTCTGGGAGCTCCAG
GACATCATCCCCTTTGGCAACAACCCCATCTTCCGCTACCTCTTTGGCTGGATGGTGCCT
CCCAAGATCTCCCTCCTGAAGCTGACCCAGGGTGAGACCCTGCGCAAGCTGTACGAGCAG
CACCACGTGGTGCAGGACATGCTGGTGCCCATGAAGTGCCTGCAGCAGGCCCTGCACACC
TTCCAAAACGACATCCACGTCTACCCCATCTGGCTGTGTCCGTTCATCCTGCCCAGCCAG
CCAGGCCTAGTGCACCCCAAAGGAAATGAGGCAGAGCTCTACATCGACATTGGAGCATAT
GGGGAGCCGCGTGTGAAACACTTTGAAGCCAGGTCCTGCATGAGGCAGCTGGAGAAGTTT
GTCCGCAGCGTGCATGGCTTCCAGATGCTGTATGCCGACTGCTACATGAACCGGGAGGAG
TTCTGGGAGATGTTTGATGGCTCCTTGTACCACAAGCTGCGAGAGAAGCTGGGTTGCCAG
GACGCCTTCCCCGAGGTGTACGACAAGATCTGCAAGGCCGCCAGGCACTGA
Enzyme 129 GenBank Gene ID AF261758 Link Image
Enzyme 129 GeneCard ID DHCR24 Link Image
Enzyme 129 GenAtlas ID Not Available
Enzyme 129 HGNC ID Not Available
Enzyme 129 Chromosome Location 1
Enzyme 129 Locus 1p32.3
Enzyme 129 SNPs SNPJam Report Link Image
Enzyme 129 General References
  1. Greeve I, Hermans-Borgmeyer I, Brellinger C, Kasper D, Gomez-Isla T, Behl C, Levkau B, Nitsch RM: The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to Alzheimer's disease-associated neurodegeneration and oxidative stress. J Neurosci. 2000 Oct 1;20(19):7345-52. [PubMed Link Image]
  2. Waterham HR, Koster J, Romeijn GJ, Hennekam RC, Vreken P, Andersson HC, FitzPatrick DR, Kelley RI, Wanders RJ: Mutations in the 3beta-hydroxysterol Delta24-reductase gene cause desmosterolosis, an autosomal recessive disorder of cholesterol biosynthesis. Am J Hum Genet. 2001 Oct;69(4):685-94. Epub 2001 Aug 22. [PubMed Link Image]
  3. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
Enzyme 129 Metabolite References Not Available
Enzyme 130 [top]
Enzyme 130 ID 7608
Enzyme 130 Name Neutrophil cytosol factor 1
Enzyme 130 Synonyms
  1. NCF-1
  2. 47 kDa autosomal chronic granulomatous disease protein
  3. 47 kDa neutrophil oxidase factor
  4. NCF-47K
  5. Neutrophil NADPH oxidase factor 1
  6. Nox organizer 2
  7. Nox-organizing protein 2
  8. SH3 and PX domain-containing protein 1A
  9. p47-phox
Enzyme 130 Gene Name NCF1
Enzyme 130 Protein Sequence >Neutrophil cytosol factor 1 
MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPI
EAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKV
RPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIADYEKTSGSEMALSTG
DVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAV
EGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPP
RRSSIRNAHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSK
PQPAVPPRPSADLILNRCSESTKRKLASAV
Enzyme 130 Number of Residues 390
Enzyme 130 Molecular Weight 44682.4
Enzyme 130 Theoretical pI 9.43
Enzyme 130 GO Classification
Function
  • binding
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
Component
—
Enzyme 130 General Function Involved in protein binding
Enzyme 130 Specific Function NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production)
Enzyme 130 Pathways Not Available
Enzyme 130 Reactions Not Available
Enzyme 130 Pfam Domain Function
Enzyme 130 Signals
  • None
Enzyme 130 Transmembrane Regions
  • None
Enzyme 130 Essentiality Not Available
Enzyme 130 GenBank ID Protein 115298672 Link Image
Enzyme 130 UniProtKB/Swiss-Prot ID P14598 Link Image
Enzyme 130 UniProtKB/Swiss-Prot Entry Name NCF1_HUMAN Link Image
Enzyme 130 PDB ID 1UEC Link Image
Enzyme 130 PDB File Show
Enzyme 130 3D Structure
Enzyme 130 Cellular Location Not Available
Enzyme 130 Gene Sequence >1173 bp 
ATGGGGGACACCTTCATCCGTCACATCGCCCTGCTGGGCTTTGAGAAGCGCTTCGTACCC
AGCCAGCACTATGTGTACATGTTCCTGGTGAAATGGCAGGACCTGTCGGAGAAGGTGGTC
TACCGGCGCTTCACCGAGATCTACGAGTTCCATAAAACCTTAAAAGAAATGTTCCCTATT
GAGGCAGGGGCGATCAATCCAGAGAACAGGATCATCCCCCACCTCCCAGCTCCCAAGTGG
TTTGACGGGCAGCGGGCCGCCGAGAACCGCCAGGGCACACTTACCGAGTACTGCGGCACG
CTCATGAGCCTGCCCACCAAGATCTCCCGCTGTCCCCACCTCCTCGACTTCTTCAAGGTG
CGCCCTGATGACCTCAAGCTCCCCACGGACAACCAGACAAAAAAGCCAGAGACATACTTG
ATGCCCAAAGATGGCAAGAGTACCGCGACAGACATCACCGGCCCCATCATCCTGCAGACG
TACCGCGCCATTGCCAACTACGAGAAGACCTCGGGCTCCGAGATGGCTCTGTCCACGGGG
GACGTGGTGGAGGTCGTAGAGAAGAGCGAGAGCGGTTGGTGGTTCTGTCAGATGAAAGCA
AAGCGAGGCTGGATCCCAGCGTCCTTCCTCGAGCCCCTGGACAGTCCTGACGAGACGGAA
GACCCTGAGCCCAACTATGCAGGTGAGCCATACGTCGCCATCAAGGCCTACACTGCTGTG
GAGGGGGACGAGGTGTCCCTGCTCGAGGGTGAAGCTGTTGAGGTCATTCACAAGCTCCTG
GACGGCTGGTGGGTCATCAGGAAAGACGACGTCACAGGCTACTTCCCGTCCATGTACCTG
CAAAAGTCAGGGCAAGACGTGTCCCAGGCCCAACGCCAGATCAAGCGGGGGGCGCCGCCC
CGCAGGTCGTCCATCCGCAACGCGCACAGCATCCACCAGCGGTCGCGGAAGCGCCTCAGC
CAGGACGCCTATCGCCGCAACAGCGTCCGTTTTCTGCAGCAGCGACGCCGCCAGGCGCGG
CCGGGACCGCAGAGCCCCGGGAGCCCGCTCGAGGAGGAGCGGCAGACGCAGCGCTCTAAA
CCGCAGCCGGCGGTGCCCCCGCGGCCGAGCGCCGACCTCATCCTGAACCGCTGCAGCGAG
AGCACCAAGCGGAAGCTGGCGTCTGCCGTCTGA
Enzyme 130 GenBank Gene ID NM_000265.4 Link Image
Enzyme 130 GeneCard ID NCF1 Link Image
Enzyme 130 GenAtlas ID NCF1 Link Image
Enzyme 130 HGNC ID HGNC:7660 Link Image
Enzyme 130 Chromosome Location Not Available
Enzyme 130 Locus Not Available
Enzyme 130 SNPs SNPJam Report Link Image
Enzyme 130 General References
  1. Volpp BD, Nauseef WM, Donelson JE, Moser DR, Clark RA: Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase. Proc Natl Acad Sci U S A. 1989 Sep;86(18):7195-9. [PubMed Link Image]
  2. Lomax KJ, Leto TL, Nunoi H, Gallin JI, Malech HL: Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease. Science. 1989 Jul 28;245(4916):409-12. [PubMed Link Image]
  3. Rodaway AR, Teahan CG, Casimir CM, Segal AW, Bentley DL: Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: tissue-specific expression and transcriptional control by retinoic acid. Mol Cell Biol. 1990 Oct;10(10):5388-96. [PubMed Link Image]
  4. Gorlach A, Lee PL, Roesler J, Hopkins PJ, Christensen B, Green ED, Chanock SJ, Curnutte JT: A p47-phox pseudogene carries the most common mutation causing p47-phox- deficient chronic granulomatous disease. J Clin Invest. 1997 Oct 15;100(8):1907-18. [PubMed Link Image]
  5. Chanock SJ, Roesler J, Zhan S, Hopkins P, Lee P, Barrett DT, Christensen BL, Curnutte JT, Gorlach A: Genomic structure of the human p47-phox (NCF1) gene. Blood Cells Mol Dis. 2000 Feb;26(1):37-46. [PubMed Link Image]
  6. Gu Y, Xu YC, Wu RF, Souza RF, Nwariaku FE, Terada LS: TNFalpha activates c-Jun amino terminal kinase through p47(phox). Exp Cell Res. 2002 Jan 1;272(1):62-74. [PubMed Link Image]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. Harshman K, Bell R, Rosenthal J, Katcher H, Miki Y, Swenson J, Gholami Z, Frye C, Ding W, Dayananth P, et al.: Comparison of the positional cloning methods used to isolate the BRCA1 gene. Hum Mol Genet. 1995 Aug;4(8):1259-66. [PubMed Link Image]
  11. Casimir CM, Bu-Ghanim HN, Rodaway AR, Bentley DL, Rowe P, Segal AW: Autosomal recessive chronic granulomatous disease caused by deletion at a dinucleotide repeat. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2753-7. [PubMed Link Image]
  12. el Benna J, Faust LP, Babior BM: The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J Biol Chem. 1994 Sep 23;269(38):23431-6. [PubMed Link Image]
  13. Xu YC, Wu RF, Gu Y, Yang YS, Yang MC, Nwariaku FE, Terada LS: Involvement of TRAF4 in oxidative activation of c-Jun N-terminal kinase. J Biol Chem. 2002 Aug 2;277(31):28051-7. Epub 2002 May 22. [PubMed Link Image]
  14. Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H: Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003 Jul 4;278(27):25234-46. Epub 2003 Apr 25. [PubMed Link Image]
  15. Takeshita F, Ishii KJ, Kobiyama K, Kojima Y, Coban C, Sasaki S, Ishii N, Klinman DM, Okuda K, Akira S, Suzuki K: TRAF4 acts as a silencer in TLR-mediated signaling through the association with TRAF6 and TRIF. Eur J Immunol. 2005 Aug;35(8):2477-85. [PubMed Link Image]
  16. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed Link Image]
  17. Kleino I, Ortiz RM, Yritys M, Huovila AP, Saksela K: Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins. J Cell Biochem. 2009 Nov 1;108(4):877-85. [PubMed Link Image]
  18. Hiroaki H, Ago T, Ito T, Sumimoto H, Kohda D: Solution structure of the PX domain, a target of the SH3 domain. Nat Struct Biol. 2001 Jun;8(6):526-30. [PubMed Link Image]
  19. Noack D, Rae J, Cross AR, Ellis BA, Newburger PE, Curnutte JT, Heyworth PG: Autosomal recessive chronic granulomatous disease caused by defects in NCF-1, the gene encoding the phagocyte p47-phox: mutations not arising in the NCF-1 pseudogenes. Blood. 2001 Jan 1;97(1):305-11. [PubMed Link Image]
Enzyme 130 Metabolite References Not Available
Enzyme 131 [top]
Enzyme 131 ID 8095
Enzyme 131 Name Cytochrome b-245 light chain
Enzyme 131 Synonyms
  1. Cytochrome b(558) alpha chain
  2. Cytochrome b558 subunit alpha
  3. Neutrophil cytochrome b 22 kDa polypeptide
  4. Superoxide-generating NADPH oxidase light chain subunit
  5. p22 phagocyte B-cytochrome
  6. p22-phox
  7. p22phox
Enzyme 131 Gene Name CYBA
Enzyme 131 Protein Sequence >Cytochrome b-245 light chain 
MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVFVCLLEYPRGKRK
KGSTMERWGQKHMTAVVKLFGPFTRNYYVRAVLHLLLSVPAGFLLATILGTACLAIASGI
YLLAAVRGEQWTPIEPKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAAAAGGPP
GGPQVNPIPVTDEVV
Enzyme 131 Number of Residues 195
Enzyme 131 Molecular Weight 20958.3
Enzyme 131 Theoretical pI 10.03
Enzyme 131 GO Classification
Function
  • binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • transition metal ion binding
Process
—
Component
—
Enzyme 131 General Function Involved in heme binding
Enzyme 131 Specific Function Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide
Enzyme 131 Pathways Not Available
Enzyme 131 Reactions Not Available
Enzyme 131 Pfam Domain Function
Enzyme 131 Signals
  • None
Enzyme 131 Transmembrane Regions
  • None
Enzyme 131 Essentiality Not Available
Enzyme 131 GenBank ID Protein 68509914 Link Image
Enzyme 131 UniProtKB/Swiss-Prot ID P13498 Link Image
Enzyme 131 UniProtKB/Swiss-Prot Entry Name CY24A_HUMAN Link Image
Enzyme 131 PDB ID 1OV3 Link Image
Enzyme 131 PDB File Show
Enzyme 131 3D Structure
Enzyme 131 Cellular Location Not Available
Enzyme 131 Gene Sequence >588 bp 
ATGGGGCAGATCGAGTGGGCCATGTGGGCCAACGAACAGGCGCTGGCGTCCGGCCTGATC
CTCATCACCGGGGGCATCGTGGCCACAGCTGGGCGCTTCACCCAGTGGTACTTTGGTGCC
TACTCCATTGTGGCGGGCGTGTTTGTGTGCCTGCTGGAGTACCCCCGGGGGAAGAGGAAG
AAGGGCTCCACCATGGAGCGCTGGGGACAGAAGTACATGACCGCCGTGGTGAAGCTGTTC
GGGCCCTTTACCAGGAATTACTATGTTCGGGCCGTCCTGCATCTCCTGCTCTCGGTGCCC
GCCGGCTTCCTGCTGGCCACCATCCTTGGGACCGCCTGCCTGGCCATTGCGAGCGGCATC
TACCTACTGGCGGCTGTGCGTGGCGAGCAGTGGACGCCCATCGAGCCCAAGCCCCGGGAG
CGGCCGCAGATCGGAGGCACCATCAAGCAGCCGCCCAGCAACCCCCCGCCGCGGCCCCCG
GCCGAGGCCCGCAAGAAGCCCAGCGAGGAGGAGGCTGCGGTGGCGGCGGGGGGACCCCCG
GGAGGTCCCCAGGTCAACCCCATCCCGGTGACCGACGAGGTCGTGTGA
Enzyme 131 GenBank Gene ID NM_000101.2 Link Image
Enzyme 131 GeneCard ID CYBA Link Image
Enzyme 131 GenAtlas ID CYBA Link Image
Enzyme 131 HGNC ID HGNC:2577 Link Image
Enzyme 131 Chromosome Location 1
Enzyme 131 Locus 16q24
Enzyme 131 SNPs SNPJam Report Link Image
Enzyme 131 General References
  1. Parkos CA, Dinauer MC, Walker LE, Allen RA, Jesaitis AJ, Orkin SH: Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b. Proc Natl Acad Sci U S A. 1988 May;85(10):3319-23. [PubMed Link Image]
  2. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Dinauer MC, Pierce EA, Bruns GA, Curnutte JT, Orkin SH: Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease. J Clin Invest. 1990 Nov;86(5):1729-37. [PubMed Link Image]
  5. Verhoeven AJ, Bolscher BG, Meerhof LJ, van Zwieten R, Keijer J, Weening RS, Roos D: Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils. Blood. 1989 May 1;73(6):1686-94. [PubMed Link Image]
  6. Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H: Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003 Jul 4;278(27):25234-46. Epub 2003 Apr 25. [PubMed Link Image]
  7. Wang D, De Deken X, Milenkovic M, Song Y, Pirson I, Dumont JE, Miot F: Identification of a novel partner of duox: EFP1, a thioredoxin-related protein. J Biol Chem. 2005 Jan 28;280(4):3096-103. Epub 2004 Nov 22. [PubMed Link Image]
  8. Ueno N, Takeya R, Miyano K, Kikuchi H, Sumimoto H: The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators. J Biol Chem. 2005 Jun 17;280(24):23328-39. Epub 2005 Apr 11. [PubMed Link Image]
  9. Martyn KD, Frederick LM, von Loehneysen K, Dinauer MC, Knaus UG: Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell Signal. 2006 Jan;18(1):69-82. Epub 2005 May 31. [PubMed Link Image]
  10. de Boer M, de Klein A, Hossle JP, Seger R, Corbeel L, Weening RS, Roos D: Cytochrome b558-negative, autosomal recessive chronic granulomatous disease: two new mutations in the cytochrome b558 light chain of the NADPH oxidase (p22-phox). Am J Hum Genet. 1992 Nov;51(5):1127-35. [PubMed Link Image]
  11. Dinauer MC, Pierce EA, Erickson RW, Muhlebach TJ, Messner H, Orkin SH, Seger RA, Curnutte JT: Point mutation in the cytoplasmic domain of the neutrophil p22-phox cytochrome b subunit is associated with a nonfunctional NADPH oxidase and chronic granulomatous disease. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11231-5. [PubMed Link Image]
  12. Hossle JP, de Boer M, Seger RA, Roos D: Identification of allele-specific p22-phox mutations in a compound heterozygous patient with chronic granulomatous disease by mismatch PCR and restriction enzyme analysis. Hum Genet. 1994 Apr;93(4):437-42. [PubMed Link Image]
  13. Leusen JH, Bolscher BG, Hilarius PM, Weening RS, Kaulfersch W, Seger RA, Roos D, Verhoeven AJ: 156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox. J Exp Med. 1994 Dec 1;180(6):2329-34. [PubMed Link Image]
  14. Rae J, Noack D, Heyworth PG, Ellis BA, Curnutte JT, Cross AR: Molecular analysis of 9 new families with chronic granulomatous disease caused by mutations in CYBA, the gene encoding p22(phox). Blood. 2000 Aug 1;96(3):1106-12. [PubMed Link Image]
  15. Yamada M, Ariga T, Kawamura N, Ohtsu M, Imajoh-Ohmi S, Ohshika E, Tatsuzawa O, Kobayashi K, Sakiyama Y: Genetic studies of three Japanese patients with p22-phox-deficient chronic granulomatous disease: detection of a possible common mutant CYBA allele in Japan and a genotype-phenotype correlation in these patients. Br J Haematol. 2000 Mar;108(3):511-7. [PubMed Link Image]
  16. Ishibashi F, Nunoi H, Endo F, Matsuda I, Kanegasaki S: Statistical and mutational analysis of chronic granulomatous disease in Japan with special reference to gp91-phox and p22-phox deficiency. Hum Genet. 2000 May;106(5):473-81. [PubMed Link Image]
  17. Teimourian S, Zomorodian E, Badalzadeh M, Pouya A, Kannengiesser C, Mansouri D, Cheraghi T, Parvaneh N: Characterization of six novel mutations in CYBA: the gene causing autosomal recessive chronic granulomatous disease. Br J Haematol. 2008 Jun;141(6):848-51. Epub 2008 Apr 18. [PubMed Link Image]
  18. Bedard K, Attar H, Bonnefont J, Jaquet V, Borel C, Plastre O, Stasia MJ, Antonarakis SE, Krause KH: Three common polymorphisms in the CYBA gene form a haplotype associated with decreased ROS generation. Hum Mutat. 2009 Jul;30(7):1123-33. [PubMed Link Image]
Enzyme 131 Metabolite References Not Available
Enzyme 132 [top]
Enzyme 132 ID 8105
Enzyme 132 Name Kynurenine 3-monooxygenase
Enzyme 132 Synonyms
  1. Kynurenine 3-hydroxylase
Enzyme 132 Gene Name KMO
Enzyme 132 Protein Sequence >Kynurenine 3-monooxygenase 
MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSH
RGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLT
AAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKK
PRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMP
FEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCV
LLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLS
MYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKK
VINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQI
SNLISR
Enzyme 132 Number of Residues 486
Enzyme 132 Molecular Weight 55809.4
Enzyme 132 Theoretical pI 9.34
Enzyme 132 GO Classification
Function
  • catalytic activity
  • monooxygenase activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 132 General Function Involved in monooxygenase activity
Enzyme 132 Specific Function Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract
Enzyme 132 Pathways
Enzyme 132 Reactions
  • L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O [RN:R01960]
Enzyme 132 Pfam Domain Function
Enzyme 132 Signals
  • None
Enzyme 132 Transmembrane Regions
  • 385-404 425-445
Enzyme 132 Essentiality Not Available
Enzyme 132 GenBank ID Protein 2239124 Link Image
Enzyme 132 UniProtKB/Swiss-Prot ID O15229 Link Image
Enzyme 132 UniProtKB/Swiss-Prot Entry Name KMO_HUMAN Link Image
Enzyme 132 PDB ID Not Available
Enzyme 132 Cellular Location Not Available
Enzyme 132 Gene Sequence >1461 bp 
ATGGACTCATCTGTCATTCAAAGGAAAAAAGTAGCTGTCATTGGTGGTGGCTTGGTTGGC
TCATTACAAGCATGCTTTCTTGCAAAGAGGAATTTCCAGATTGATGTATATGAAGCTAGG
GAAGATACTCGAGTGGCTACCTTCACACGTGGAAGAAGCATTAACTTAGCCCTTTCTCAT
AGAGGACGACAAGCCTTGAAAGCTGTTGGCCTGGAAGATCAGATTGTATCCCAAGGTATT
CCCATGAGAGCAAGAATGATCCACTCTCTTTCAGGAAAAAAGTCTGCAATTCCCTATGGG
ACAAAGTCTCAGTATATTCTTTCTGTAAGCAGAGAAAATCTAAACAAGGATCTATTGACT
GCTGCTGAGAAATACCCCAATGTGAAAATGCACTTTAACCACAGGCTGTTGAAATGTAAT
CCAGAGGAAGGAATGATCACAGTGCTTGGATCTGACAAAGTTCCCAAAGATGTCACTTGT
GACCTCATTGTAGGATGTGATGGAGCCTATTCAACTGTCAGATCTCACCTGATGAAGAAA
CCTCGCTTTGATTACAGTCAGCAGTACATTCCTCATGGGTACATGGAGTTGACTATTCCA
CCTAAGAACGGAGATTATGCCATGGAACCTAATTATCTGCATATTTGGCCTAGAAATACC
TTTATGATGATTGCACTTCCTAACATGAACAAATCATTCACATGTACTTTGTTCATGCCC
TTTGAAGAGTTTGAAAAACTTCTAACCAGTAATGATGTGGTAGATTTCTTCCAGAAATAC
TTTCCGGATGCCATCCCTCTAATTGGAGAGAAACTCCTAGTGCAAGATTTCTTCCTGTTG
CCTGCCCAGCCCATGATATCTGTAAAGTGCTCTTCATTTCACTTTAAATCTCACTGTGTA
CTGCTGGGAGATGCAGCTCATGCTATAGTGCCGTTTTTTGGGCAAGGAATGAATGCGGGC
TTTGAAGACTGCTTGGTATTTGATGAGTTAATGGATAAATTCAGTAACGACCTTAGTTTG
TGTCTTCCTGTGTTCTCAAGATTGAGAATCCCAGATGATCACGCGATTTCAGACCTATCC
ATGTACAATTACATAGAGATGCGAGCACATGTCAACTCAAGCTGGTTCATTTTTCAGAAG
AACATGGAGAGATTTCTTCATGCGATTATGCCATCGACCTTTATCCCTCTCTATACAATG
GTCACTTTTTCCAGAATAAGATACCATGAGGCTGTGCAGCGTTGGCATTGGCAAAAAAAG
GTGATAAACAAAGGACTCTTTTTCTTGGGATCACTGATAGCCATCAGCAGTACCTACCTA
CTTATACACTACATGTCACCACGATCTTTCCTCTGCTTGAGAAGACCATGGAACTGGATA
GCTCACTTCCGGAATACAACATGTTTCCCCGCAAAGGCCGTGGACTCCCTAGAACAAATT
TCCAATCTCATTAGCAGGTGA
Enzyme 132 GenBank Gene ID Y13153 Link Image
Enzyme 132 GeneCard ID KMO Link Image
Enzyme 132 GenAtlas ID KMO Link Image
Enzyme 132 HGNC ID HGNC:6381 Link Image
Enzyme 132 Chromosome Location 1
Enzyme 132 Locus 1q42-q44
Enzyme 132 SNPs SNPJam Report Link Image
Enzyme 132 General References
  1. Alberati-Giani D, Cesura AM, Broger C, Warren WD, Rover S, Malherbe P: Cloning and functional expression of human kynurenine 3-monooxygenase. FEBS Lett. 1997 Jun 30;410(2-3):407-12. [PubMed Link Image]
  2. Breton J, Avanzi N, Magagnin S, Covini N, Magistrelli G, Cozzi L, Isacchi A: Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase. Eur J Biochem. 2000 Feb;267(4):1092-9. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Stone TW, Darlington LG: Endogenous kynurenines as targets for drug discovery and development. Nat Rev Drug Discov. 2002 Aug;1(8):609-20. [PubMed Link Image]
Enzyme 132 Metabolite References Not Available
Enzyme 133 [top]
Enzyme 133 ID 8106
Enzyme 133 Name Dehydrogenase/reductase SDR family member 9
Enzyme 133 Synonyms
  1. 3-alpha hydroxysteroid dehydrogenase
  2. 3-alpha-HSD
  3. NADP-dependent retinol dehydrogenase/reductase
  4. RDH-E2
  5. RDHL
  6. Short-chain dehydrogenase/reductase retSDR8
Enzyme 133 Gene Name DHRS9
Enzyme 133 Protein Sequence >Dehydrogenase/reductase SDR family member 9 
MLFWVLGLLILCGFLWTRKGKLKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAC
LTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWGLINNAGVPGVLA
PTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGYTPSK
YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGE
GYIEKSLDKLKGNKSYVNMDLSPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAA
LQDFLLLKQKAELANPKAV
Enzyme 133 Number of Residues 319
Enzyme 133 Molecular Weight 35226.8
Enzyme 133 Theoretical pI 8.89
Enzyme 133 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 133 General Function Involved in oxidoreductase activity
Enzyme 133 Specific Function 3-alpha-hydroxysteroid dehydrogenase that converts 3- alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. May play a role in the biosynthesis of retinoic acid from retinaldehyde, but seems to have low activity with retinoids. Can utilize both NADH and NADPH
Enzyme 133 Pathways Not Available
Enzyme 133 Reactions Not Available
Enzyme 133 Pfam Domain Function
Enzyme 133 Signals
  • 1-17
Enzyme 133 Transmembrane Regions
  • None
Enzyme 133 Essentiality Not Available
Enzyme 133 GenBank ID Protein Not Available
Enzyme 133 UniProtKB/Swiss-Prot ID Q9BPW9 Link Image
Enzyme 133 UniProtKB/Swiss-Prot Entry Name DHRS9_HUMAN Link Image
Enzyme 133 PDB ID Not Available
Enzyme 133 Cellular Location Not Available
Enzyme 133 Gene Sequence >960 bp 
ATGCTCTTTTGGGTGCTAGGCCTCCTAATCCTCTGTGGTTTTCTGTGGACTCGTAAAGGA
AAACTAAAGATTGAAGACATCACTGATAAGTACATTTTTATCACTGGATGTGACTCGGGC
TTTGGAAACTTGGCAGCCAGAACTTTTGATAAAAAGGGATTTCATGTAATCGCTGCCTGT
CTGACTGAATCAGGATCAACAGCTTTAAAGGCAGAAACCTCAGAGAGACTTCGTACTGTG
CTTCTGGATGTGACCGACCCAGAGAATGTCAAGAGGACTGCCCAGTGGGTGAAGAACCAA
GTTGGGGAGAAAGGTCTCTGGGGTCTGATCAATAATGCTGGTGTTCCCGGCGTGCTGGCT
CCCACTGACTGGCTGACACTAGAGGACTACAGAGAACCTATTGAAGTGAACCTGTTTGGA
CTCATCAGTGTGACACTAAATATGCTTCCTTTGGTCAAGAAAGCTCAAGGGAGAGTTATT
AATGTCTCCAGTGTTGGAGGTCGCCTTGCAATCGTTGGAGGGGGCTATACTCCATCCAAA
TATGCAGTGGAAGGTTTCAATGACAGCTTAAGACGGGACATGAAAGCTTTTGGTGTGCAC
GTCTCATGCATTGAACCAGGATTGTTCAAAACAAACTTGGCAGATCCAGTAAAGGTAATT
GAAAAAAAACTCGCCATTTGGGAGCAGCTGTCTCCAGACATCAAACAACAATATGGAGAA
GGTTACATTGAAAAAAGTCTAGACAAACTGAAAGGCAATAAATCCTATGTGAACATGGAC
CTCTCTCCGGTGGTAGAGTGCATGGACCACGCTCTAACAAGTCTCTTCCCTAAGACTCAT
TATGCCGCTGGAAAAGATGCCAAAATTTTCTGGATACCTCTGTCTCACATGCCAGCAGCT
TTGCAAGACTTTTTATTGTTGAAACAGAAAGCAGAGCTGGCTAATCCCAAGGCAGTGTGA
Enzyme 133 GenBank Gene ID AF343729 Link Image
Enzyme 133 GeneCard ID DHRS9 Link Image
Enzyme 133 GenAtlas ID DHRS9 Link Image
Enzyme 133 HGNC ID HGNC:16888 Link Image
Enzyme 133 Chromosome Location 2
Enzyme 133 Locus 2q31.1
Enzyme 133 SNPs SNPJam Report Link Image
Enzyme 133 General References
  1. Chetyrkin SV, Belyaeva OV, Gough WH, Kedishvili NY: Characterization of a novel type of human microsomal 3alpha -hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties. J Biol Chem. 2001 Jun 22;276(25):22278-86. Epub 2001 Apr 9. [PubMed Link Image]
  2. Soref CM, Di YP, Hayden L, Zhao YH, Satre MA, Wu R: Characterization of a novel airway epithelial cell-specific short chain alcohol dehydrogenase/reductase gene whose expression is up-regulated by retinoids and is involved in the metabolism of retinol. J Biol Chem. 2001 Jun 29;276(26):24194-202. Epub 2001 Apr 13. [PubMed Link Image]
  3. Markova NG, Pinkas-Sarafova A, Karaman-Jurukovska N, Jurukovski V, Simon M: Expression pattern and biochemical characteristics of a major epidermal retinol dehydrogenase. Mol Genet Metab. 2003 Feb;78(2):119-35. [PubMed Link Image]
  4. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  5. Haeseleer F, Palczewski K: Short-chain dehydrogenases/reductases in retina. Methods Enzymol. 2000;316:372-83. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 133 Metabolite References Not Available
Enzyme 134 [top]
Enzyme 134 ID 8179
Enzyme 134 Name Vitamin D 25-hydroxylase
Enzyme 134 Synonyms
  1. Cytochrome P450 2R1
Enzyme 134 Gene Name CYP2R1
Enzyme 134 Protein Sequence >Vitamin D 25-hydroxylase 
MWKLWRAEEGAAALGGALFLLLFALGVRQLLKQRRPMGFPPGPPGLPFIGNIYSLAASSE
LPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTK
MGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQKSFESKILEETKFFNDAIETYKGRPFDFK
QLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWIGILPF
GKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENL
IFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPY
TEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVF
HPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPD
LKPRLGMTLQPQPYLICAERR
Enzyme 134 Number of Residues 501
Enzyme 134 Molecular Weight 57358.8
Enzyme 134 Theoretical pI 7.67
Enzyme 134 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 134 General Function Involved in monooxygenase activity
Enzyme 134 Specific Function Has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3)
Enzyme 134 Pathways Not Available
Enzyme 134 Reactions
  • 5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ + H2O [RN:R04807]
Enzyme 134 Pfam Domain Function
Enzyme 134 Signals
  • None
Enzyme 134 Transmembrane Regions
  • None
Enzyme 134 Essentiality Not Available
Enzyme 134 GenBank ID Protein 33591222 Link Image
Enzyme 134 UniProtKB/Swiss-Prot ID Q6VVX0 Link Image
Enzyme 134 UniProtKB/Swiss-Prot Entry Name CP2R1_HUMAN Link Image
Enzyme 134 PDB ID Not Available
Enzyme 134 Cellular Location Not Available
Enzyme 134 Gene Sequence >1506 bp 
ATGTGGAAGCTTTGGAGAGCTGAAGAGGGCGCGGCGGCGCTCGGCGGCGCGCTCTTCCTG
CTGCTCTTCGCGCTAGGGGTCCGCCAGCTGCTGAAGCAGAGGCGGCCGATGGGCTTCCCC
CCGGGGCCGCCGGGGCTGCCATTTATCGGCAACATCTATTCCCTGGCAGCCTCATCCGAG
CTTCCCCATGTCTACATGAGAAAGCAGAGCCAGGTGTACGGAGAGATCTTCAGTTTAGAT
CTTGGAGGCATATCAACTGTGGTTCTAAATGGCTATGATGTAGTAAAGGAATGCCTTGTT
CATCAAAGCGAAATTTTTGCAGACAGACCATGCCTTCCTTTATTCATGAAGATGACAAAA
ATGGGAGGCTTACTCAATTCCAGATATGGCCGAGGATGGGTTGATCACAGACGATTAGCT
GTAAACAGTTTTCGATATTTTGGATATGGCCAAAAGTCTTTTGAATCTAAAATCTTGGAA
GAAACCAAATTTTTCAATGATGCTATTGAAACATACAAAGGTAGACCTTTTGACTTTAAA
CAGTTAATAACGAATGCTGTTTCAAACATAACCAATCTGATCATTTTTGGAGAACGATTC
ACTTATGAAGACACCGATTTTCAGCACATGATTGAGTTATTTAGTGAAAATGTGGAACTA
GCTGCCAGTGCCTCAGTCTTCTTGTATAATGCCTTTCCATGGATTGGCATCCTGCCTTTT
GGAAAACATCAACAGCTGTTTAGAAATGCAGCTGTAGTCTATGATTTTCTCTCCAGACTC
ATTGAAAAAGCTTCAGTCAACAGAAAGCCTCAGCTACCTCAGCATTTTGTTGATGCTTAT
TTAGATGAGATGGATCAAGGTAAAAATGACCCATCATCTACTTTCTCCAAAGAAAACCTA
ATTTTCTCAGTGGGTGAACTCATCATTGCTGGAACTGAAACTACAACCAATGTGCTACGG
TGGGCGATTCTTTTCATGGCCCTTTATCCTAATATTCAAGGACAAGTTCAGAAAGAGATT
GATTTAATTATGGGCCCTAATGGGAAGCCTTCTTGGGACGACAAATGCAAAATGCCTTAT
ACTGAGGCAGTTTTGCATGAAGTTTTAAGATTCTGTAATATAGTTCCATTAGGGATTTTC
CATGCAACCTCTGAAGATGCAGTTGTACGTGGTTATTCCATTCCTAAAGGCACAACAGTA
ATTACAAATCTTTATTCTGTACACTTTGATGAAAAGTACTGGAGAGACCCAGAAGTGTTC
CATCCTGAGCGATTTCTGGACAGCAGTGGATATTTTGCCAAGAAGGAAGCTTTGGTTCCT
TTTTCCCTAGGAAGAAGACATTGTCTTGGAGAACACTTGGCTCGGATGGAAATGTTCTTG
TTTTTTACAGCATTGCTTCAGAGGTTTCATTTGCATTTTCCACATGAACTAGTTCCAGAT
CTGAAGCCCAGGTTAGGCATGACATTGCAGCCCCAACCCTACCTCATCTGTGCTGAAAGA
CGCTGA
Enzyme 134 GenBank Gene ID AY323817 Link Image
Enzyme 134 GeneCard ID CYP2R1 Link Image
Enzyme 134 GenAtlas ID CYP2R1 Link Image
Enzyme 134 HGNC ID HGNC:20580 Link Image
Enzyme 134 Chromosome Location 1
Enzyme 134 Locus 11p15.2
Enzyme 134 SNPs SNPJam Report Link Image
Enzyme 134 General References
  1. Cheng JB, Motola DL, Mangelsdorf DJ, Russell DW: De-orphanization of cytochrome P450 2R1: a microsomal vitamin D 25-hydroxilase. J Biol Chem. 2003 Sep 26;278(39):38084-93. Epub 2003 Jul 16. [PubMed Link Image]
  2. Shinkyo R, Sakaki T, Kamakura M, Ohta M, Inouye K: Metabolism of vitamin D by human microsomal CYP2R1. Biochem Biophys Res Commun. 2004 Nov 5;324(1):451-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Strushkevich N, Usanov SA, Plotnikov AN, Jones G, Park HW: Structural analysis of CYP2R1 in complex with vitamin D3. J Mol Biol. 2008 Jun 27;380(1):95-106. Epub 2008 Apr 8. [PubMed Link Image]
  5. Cheng JB, Levine MA, Bell NH, Mangelsdorf DJ, Russell DW: Genetic evidence that the human CYP2R1 enzyme is a key vitamin D 25-hydroxylase. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7711-5. Epub 2004 May 5. [PubMed Link Image]
Enzyme 134 Metabolite References Not Available
Enzyme 135 [top]
Enzyme 135 ID 8560
Enzyme 135 Name Retinol dehydrogenase 12
Enzyme 135 Synonyms
  1. All-trans and 9-cis retinol dehydrogenase
Enzyme 135 Gene Name RDH12
Enzyme 135 Protein Sequence >Retinol dehydrogenase 12 
MLVTLGLLTSFFSFLYMVAPSIRKFFAGGVCRTNVQLPGKVVVITGANTGIGKETARELA
SRGARVYIACRDVLKGESAASEIRVDTKNSQVLVRKLDLSDTKSIRAFAEGFLAEEKQLH
ILINNAGVMMCPYSKTADGFETHLGVNHLGHFLLTYLLLERLKVSAPARVVNVSSVAHHI
GKIPFHDLQSEKRYSRGFAYCHSKLANVLFTRELAKRLQGTGVTTYAVHPGVVRSELVRH
SSLLCLLWRLFSPFVKTAREGAQTSLHCALAEGLEPLSGKYFSDCKRTWVSPRARNNKTA
ERLWNVSCELLGIRWE
Enzyme 135 Number of Residues 316
Enzyme 135 Molecular Weight 35093.5
Enzyme 135 Theoretical pI 10.20
Enzyme 135 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 135 General Function Involved in oxidoreductase activity
Enzyme 135 Specific Function Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. Might be the key enzyme in the formation of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments
Enzyme 135 Pathways Not Available
Enzyme 135 Reactions Not Available
Enzyme 135 Pfam Domain Function
Enzyme 135 Signals
  • None
Enzyme 135 Transmembrane Regions
  • None
Enzyme 135 Essentiality Not Available
Enzyme 135 GenBank ID Protein Not Available
Enzyme 135 UniProtKB/Swiss-Prot ID Q96NR8 Link Image
Enzyme 135 UniProtKB/Swiss-Prot Entry Name RDH12_HUMAN Link Image
Enzyme 135 PDB ID Not Available
Enzyme 135 Cellular Location Not Available
Enzyme 135 Gene Sequence >951 bp 
ATGCTGGTCACCTTGGGACTGCTCACCTCCTTCTTCTCGTTCCTGTATATGGTAGCTCCA
TCCATCAGGAAGTTCTTTGCTGGTGGAGTGTGTAGAACAAATGTGCAGCTTCCTGGCAAG
GTAGTGGTGATCACTGGCGCCAACACGGGCATTGGCAAGGAGACGGCCAGAGAGCTCGCT
AGCCGAGGAGCCCGAGTCTATATTGCCTGCAGAGATGTACTGAAGGGGGAGTCTGCTGCC
AGTGAAATCCGAGTGGATACAAAGAACTCCCAGGTGCTGGTGCGGAAATTGGACCTATCC
GACACCAAATCTATCCGAGCCTTTGCTGAGGGCTTTCTGGCAGAGGAAAAGCAGCTCCAT
ATTCTGATCAACAATGCGGGAGTAATGATGTGTCCATATTCCAAGACAGCTGATGGCTTT
GAAACCCACCTGGGAGTCAACCACCTGGGCCACTTCCTCCTCACCTACCTGCTCCTGGAG
CGGCTAAAGGTGTCTGCCCCTGCACGGGTGGTTAATGTGTCCTCGGTGGCTCACCACATT
GGCAAGATTCCCTTCCACGACCTCCAGAGCGAGAAGCGCTACAGCAGGGGTTTTGCCTAT
TGCCACAGCAAGCTGGCCAATGTGCTTTTTACTCGTGAGCTGGCCAAGAGGCTCCAAGGC
ACCGGGGTCACCACCTACGCAGTGCACCCAGGCGTCGTCCGCTCTGAGCTGGTCCGGCAC
TCCTCCCTGCTCTGCCTGCTCTGGCGGCTCTTCTCCCCCTTTGTCAAGACGGCACGGGAG
GGGGCGCAGACCAGCCTGCACTGCGCCCTGGCTGAGGGCCTGGAGCCCCTGAGTGGCAAG
TACTTCAGTGACTGCAAGAGGACCTGGGTGTCTCCAAGGGCCCGAAATAACAAAACAGCT
GAGCGCCTATGGAATGTCAGCTGTGAGCTTCTAGGAATCCGGTGGGAGTAG
Enzyme 135 GenBank Gene ID AK054835 Link Image
Enzyme 135 GeneCard ID RDH12 Link Image
Enzyme 135 GenAtlas ID RDH12 Link Image
Enzyme 135 HGNC ID HGNC:19977 Link Image
Enzyme 135 Chromosome Location 1
Enzyme 135 Locus 14q24.1
Enzyme 135 SNPs SNPJam Report Link Image
Enzyme 135 General