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Human Metabolome Database Version 2.5

 

Showing metabocard for Hydrogen peroxide (HMDB03125)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 16:12:34
Update Date 2009-05-05 20:59:37
Accession Number HMDB03125
Secondary Accession Numbers HMDB06491
Common Name Hydrogen peroxide
Description Hydrogen peroxide (H2O2) is a very pale blue liquid which appears colourless in a dilute solution, slightly more viscous than water. It is a weak acid. It has strong oxidizing properties and is therefore a powerful bleaching agent that is mostly used for bleaching paper, but has also found use as a disinfectant and as an oxidizer. Hydrogen peroxide in the form of carbamide peroxide is widely used for tooth whitening (bleaching), both in professionally- and in self-administered products. Hydrogen peroxide (H2O2) is a well-documented component of living cells. It plays important roles in host defense and oxidative biosynthetic reactions. In addition there is growing evidence that at low levels, H2O2 also functions as a signaling agent, particularly in higher organisms. H2O2 has increasingly been viewed as an important cellular signaling agent in its own right, capable of modulating both contractile and growth-promoting pathways with more far-reaching effects. Due to the accumulation of hydrogen peroxide in the skin of patients with the depigmentation disorder vitiligo, the human epidermis cannot have the normal capacity for autocrine synthesis, transport and degradation of acetylcholine as well as the muscarinic (m1-m5) and nicotinic signal transduction in keratinocytes and melanocytes. Accumulating evidence suggests that hydrogen peroxide (H(2)O(2)) plays an important role in cancer development. Experimental data have shown that cancer cells produce high amounts of H(2)O(2). An increase in the cellular levels of H(2)O(2) has been linked to several key alterations in cancer, including DNA alterations, cell proliferation, apoptosis resistance, metastasis, angiogenesis and hypoxia-inducible factor 1 (HIF-1) activation. (PMID: 17150302, 17335854, 16677071, 16607324, 16514169)
Synonyms
  1. Hydrogen peroxide
  2. Adeka Super EL
  3. Albone
  4. Albone 35
  5. Albone DS
  6. Anti-Keim 50
  7. Asepticper
  8. Baquashock
  9. CIX
  10. Clarigel Gold
  11. Crestal Whitestrips
  12. Crystacide
  13. Dentasept
  14. Deslime LP
  15. Hioxyl
  16. Hipox
  17. Hybrite
  18. Hydrogen dioxide
  19. Inhibine
  20. Lase Peroxide
  21. Lensan A
  22. Magic Bleaching
  23. Metrokur
  24. Mirasept
  25. Nite White Excel 2
  26. Odosat D
  27. Opalescence Xtra
  28. Oxigenal
  29. Oxydol
  30. Oxyfull
  31. Oxysept
  32. Oxysept I
  33. Pegasyl
  34. Perhydrol
  35. Perone
  36. Peroxaan
  37. Peroxclean
  38. Quasar Brite
  39. Select Bleach
  40. Superoxol
  41. T-Stuff
  42. Whiteness HP
  43. Whitespeed
  44. Xtra White
Chemical IUPAC Name hydrogen peroxide
Chemical Formula H2O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Inorganic
Super Class
  • Miscellanous
Class
  • Inorganic Ions and Gases
Sub Class
  • Unclassified compounds
Family
  • Mammalian Metabolite
Species
  • hydroperoxide
Biofunction
  • Host defense, signalling
Application
Source
  • Endogenous
Average Molecular Weight 34.015
Monoisotopic Molecular Weight 34.005478
Isomeric SMILES OO
Canonical SMILES OO
KEGG Compound ID C00027 Link Image
BioCyc ID HYDROGEN-PEROXIDE Link Image
BiGG ID 33570 Link Image
Wikipedia Link Hydrogen peroxide Link Image
NuGOwiki Link HMDB03125 Link Image
Metagene Link HMDB03125 Link Image
METLIN ID Not Available
PubChem Compound 784 Link Image
PubChem Substance 8150789 Link Image
ChEBI ID 16240 Link Image
CAS Registry Number 7722-84-1
InChI Identifier InChI=1/H2O2/c1-2/h1-2H
Synthesis Reference Not Available
Melting Point (Experimental) -0.43 oC
Experimental Water Solubility 1000 mg/mL at 25 oC [RADDING,SB et al. (1977)] Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Physiological Charge 0
State Liquid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1 [Predicted by PubChem via XLOGP]; -1.57 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
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 Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 10.5 +/- 3.6 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Rao PS, Rujikarn N, Luber JM Jr: High-performance liquid chromatographic method for the direct quantitation of oxy radicals in myocardium and blood by means of 1,3-dimethylthiourea and dimethyl sulfoxide. J Chromatogr. 1988 Dec 28;459:269-73. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 30.5 +/- 4.6 uM
Age Adult:>18 yrs old
Sex Both
Condition Coronary heart disease
Comments Measured in plasma (positive single photon emission computed tomography test)
References
  • Kazmierczak M, Wysocki H, Wykretowicz A, Minczykowski A: Estimation of hydrogen peroxide plasma levels in patients evaluated for coronary heart disease using dipyridamole infusion followed by SPECT. Coron Artery Dis. 1995 Jan;6(1):65-9. [PubMed Link Image]
Biofluid Blood
Value 23.5 +/- 3.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Coronary heart disease
Comments Measured in plasma (negative single photon emission computed tomography test)
References
  • Kazmierczak M, Wysocki H, Wykretowicz A, Minczykowski A: Estimation of hydrogen peroxide plasma levels in patients evaluated for coronary heart disease using dipyridamole infusion followed by SPECT. Coron Artery Dis. 1995 Jan;6(1):65-9. [PubMed Link Image]
Biofluid Blood
Value 21.0 +/- 2.9 uM
Age Adult:>18 yrs old
Sex Both
Condition Coronary heart disease
Comments Measured in plasma (negative single photon emission computed tomography test and after dipyridamole infusion)
References
  • Kazmierczak M, Wysocki H, Wykretowicz A, Minczykowski A: Estimation of hydrogen peroxide plasma levels in patients evaluated for coronary heart disease using dipyridamole infusion followed by SPECT. Coron Artery Dis. 1995 Jan;6(1):65-9. [PubMed Link Image]
Biofluid Blood
Value 50.3 +/- 5.4 uM
Age Adult:>18 yrs old
Sex Both
Condition Coronary heart disease
Comments Measured in plasma (positive single photon emission computed tomography test and after dipyridamole infusion)
References
  • Kazmierczak M, Wysocki H, Wykretowicz A, Minczykowski A: Estimation of hydrogen peroxide plasma levels in patients evaluated for coronary heart disease using dipyridamole infusion followed by SPECT. Coron Artery Dis. 1995 Jan;6(1):65-9. [PubMed Link Image]
Associated Disorders
Condition References
Coronary heart disease
  • Kazmierczak M, Wysocki H, Wykretowicz A, Minczykowski A: Estimation of hydrogen peroxide plasma levels in patients evaluated for coronary heart disease using dipyridamole infusion followed by SPECT. Coron Artery Dis. 1995 Jan;6(1):65-9. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
D-Arginine and D-Ornithine Metabolism SMP00036 Link Image map00472 Link Image
Degradation of Superoxides SMP00468 Link Image
Ethanol Degradation SMP00449 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Histidine Metabolism SMP00044 Link Image map00340 Link Image
Phenylalanine and Tyrosine Metabolism SMP00008 Link Image map00360 Link Image
Plasmalogen Synthesis SMP00479 Link Image
Riboflavin Metabolism SMP00070 Link Image map00740 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Peroxisomal sarcosine oxidase
  2. Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
  3. Aldehyde oxidase
  4. Peroxisomal acyl-coenzyme A oxidase 1
  5. Amine oxidase [flavin-containing] B
  6. Amine oxidase [flavin-containing] A
  7. Xanthine dehydrogenase/oxidase
  8. Dihydroorotate dehydrogenase, mitochondrial
  9. Peroxisomal acyl-coenzyme A oxidase 3
  10. D-amino-acid oxidase
  11. Thyroid peroxidase
  12. Lactoperoxidase
  13. Myeloperoxidase
  14. Eosinophil peroxidase
  15. Amiloride-sensitive amine oxidase [copper-containing]
  16. Membrane primary amine oxidase
  17. Retina-specific copper amine oxidase
  18. Pyridoxine-5'-phosphate oxidase
  19. Protein-lysine 6-oxidase
  20. Hydroxyacid oxidase 2
  21. Glutathione peroxidase 7
  22. Epididymal secretory glutathione peroxidase
  23. Glutathione peroxidase 6
  24. Glutathione peroxidase 1
  25. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
  26. Glutathione peroxidase 3
  27. Glutathione peroxidase 2
  28. Sulfite oxidase, mitochondrial
  29. Catalase
  30. Superoxide dismutase [Mn], mitochondrial
  31. Amyloid beta A4 protein
  32. Superoxide dismutase [Cu-Zn]
  33. Peroxiredoxin-5, mitochondrial
  34. Dual oxidase 2
  35. Extracellular superoxide dismutase [Cu-Zn]
  36. OTTHUMP00000017001
  37. Dual oxidase 1
  38. Growth-inhibiting protein 16
  39. Prenylcysteine oxidase 1
  40. NADPH oxidase activator 1
  41. NADPH oxidase organizer 1
  42. Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a
  43. Myeloperoxidase (Myeloperoxidase, isoform CRA_a)
  44. cDNA FLJ76595, highly similar to Homo sapiens peroxiredoxin 6 (PRDX6), mRNA (Peroxiredoxin 6, isoform CRA_a)
  45. Peroxisomal N1-acetyl-spermine/spermidine oxidase (PAO) (Polyamine oxidase (Exo-N4-amino), isoform CRA_a)
  46. cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
  47. cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c)
  48. cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
  49. cDNA, FLJ95254, highly similar to Homo sapiens prenylcysteine lyase (PCL1), mRNA (Prenylcysteine oxidase 1)
  50. cDNA, FLJ93564, highly similar to Homo sapiens superoxide dismutase 2, mitochondrial (SOD2), mRNA (Superoxide dismutase 2, mitochondrial, isoform CRA_b)
Enzyme 1 [top]
Enzyme 1 ID 5354
Enzyme 1 Name Peroxisomal sarcosine oxidase
Enzyme 1 Synonyms
  1. PSO
  2. L-pipecolate oxidase
  3. L-pipecolic acid oxidase
Enzyme 1 Gene Name PIPOX
Enzyme 1 Protein Sequence >Peroxisomal sarcosine oxidase
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL
Enzyme 1 Number of Residues 390
Enzyme 1 Molecular Weight 44065.5
Enzyme 1 Theoretical pI 8.54
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
  • sarcosine oxidase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
  • oxidation reduction
  • tetrahydrofolate metabolic process
Component
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Metabolizes sarcosine, L-pipecolic acid and L-proline
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 [RN:R02204]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 7157903 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9P0Z9 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SOX_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1173 bp
ATGGCGGCTCAGAAAGATCTCTGGGACGCCATTGTGATTGGGGCGGGGATCCAGGGCTGC
TTCACTGCATACCACCTCGCCAAACACAGGAAGAGGATCCTCCTGCTGGAGCAGTTCTTT
CTACCACACTCCCGAGGAAGCTCCCATGGACAAAGCCGGATAATCCGAAAGGCGTACCTG
GAAGACTTTTACACCCGGATGATGCATGAGTGCTATCAGATATGGGCCCAGCTGGAGCAC
GAGGCTGGAACCCAATTGCACAGGCAGACTGGATTACTGCTGCTGGGAATGAAAGAGAAT
CAAGAATTAAAGACAATCCAGGCCAATCTGTCGAGGCAGAGGGTAGAACACCAGTGTCTT
TCATCTGAGGAACTGAAGCAACGTTTCCCAAATATTCGGTTGCCCAGGGGAGAAGTGGGG
CTCTTGGACAATTCCGGAGGAGTTATCTATGCATATAAGGCCCTCAGAGCCCTGCAGGAT
GCAATTCGACAGCTAGGAGGCATAGTGCGTGACGGAGAGAAGGTGGTGGAGATAAACCCA
GGGCTACTGGTCACGGTGAAAACCACCTCCAGGAGCTACCAAGCTAAGAGCTTGGTCATC
ACAGCAGGTCCTTGGACCAACCAGCTCCTCCGTCCCCTGGGCATTGAGATGCCTCTCCAG
ACCCTGCGGATCAACGTGTGTTACTGGCGAGAGATGGTTCCTGGGAGCTATGGTGTGTCC
CAGGCCTTTCCGTGCTTCCTGTGGCTGGGCTTGTGTCCCCACCACATCTACGGACTGCCC
ACAGGAGAGTACCCAGGGCTGATGAAGGTCAGCTATCACCACGGCAACCACGCAGACCCT
GAGGAGCGGGACTGCCCCACAGCACGCACAGACATCGGAGACGTCCAGATCCTGAGCAGC
TTTGTCAGAGATCACTTACCTGATCTGAAGCCCGAGCCTGCTGTCATTGAGAGCTGCATG
TACACGAATACCCCTGATGAGCAGTTCATTCTCGATCGCCACCCAAAGTATGACAACATT
GTCATTGGTGCTGGATTCTCTGGGCACGGGTTCAAGCTGGCCCCTGTGGTGGGGAAGATC
CTGTATGAATTAAGCATGAAATTAACACCATCTTATGACTTGGCACCTTTTCGAATCAGC
CGTTTCCCAAGCCTGGCCAAAGCCCACCTGTGA
Enzyme 1 GenBank Gene ID AF134593 Link Image
Enzyme 1 GeneCard ID PIPOX Link Image
Enzyme 1 GenAtlas ID PIPOX Link Image
Enzyme 1 HGNC ID HGNC:17804 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17q11.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. IJlst L, de Kromme I, Oostheim W, Wanders RJ: Molecular cloning and expression of human L-pipecolate oxidase. Biochem Biophys Res Commun. 2000 Apr 21;270(3):1101-5. [PubMed Link Image]
  2. Dodt G, Kim DG, Reimann SA, Reuber BE, McCabe K, Gould SJ, Mihalik SJ: L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases. Biochem J. 2000 Feb 1;345 Pt 3:487-94. [PubMed Link Image]
  3. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [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. 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5355
Enzyme 2 Name Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
Enzyme 2 Synonyms
  1. Polyamine oxidase
Enzyme 2 Gene Name PAOX
Enzyme 2 Protein Sequence >Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
MESTGSVGEAPGGPRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCF
GGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLVETGGHVGLPSVSYASSGT
SVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKEIGQHVARLCGHSAFPHLR
VLEATARAGGRIRSERCFGGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLV
ETGGHVGLPSVSYASSGASVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKE
IGQHVAGWTEDEETRKLKLAVLNSFFNLECCVSGTHSMDLVALAPFGEYTVLPGLDCTFS
KGYQGLTNCMMAALPEDTVVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAHH
VIVTVPLGFLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFLEFEEPFWEPDCQLIQLV
WEDTSPLEDAAPELQDAWFRKLIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLC
LTQVLRRVTGNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAG
AQLQILFAGEATHRTFYSTTHGALLSGWREADRLLSLWAPQVQQPRPRL
Enzyme 2 Number of Residues 649
Enzyme 2 Molecular Weight 70289.3
Enzyme 2 Theoretical pI 5.27
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Flavoenzyme which catalyzes the oxidation of N(1)- acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity:N(1)-acetylspermine = N(1)- acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • (1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2 [RN:R09074]
  • (2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2 [RN:R03899]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 45439842 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q6QHF9 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PAOX_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1950 bp
ATGGAGTCGACCGGCAGCGTCGGGGAGGCCCCGGGCGGACCCCGGGTGCTGGTGGTGGGC
GGCGGCATCGCGGGGCTGGGCGCGGCGCAGAGGCTCTGCGGCCACTCCGCCTTCCCGCAC
CTACGGGTCCTGGAGGCCACGGCCCGTGCCGGGGGCCGCATCCGCTCGGAGCGCTGCTTC
GGTGGCGTGGTGGAGGTGGGCGCGCACTGGATCCATGGGCCCTCCCGGGGTAACCCCGTC
TTCCAGCTGGCTGCTGAGTACGGGCTGCTGGGGGAGAAGGAGCTGTCCCAGGAGAACCAG
CTGGTGGAGACCGGGGGTCACGTGGGCCTGCCCTCCGTGAGCTACGCCAGCTCCGGGACC
AGCGTGAGCCTCCAGCTGGTGGCGGAGATGGCGACTCTGTTCTACGGCCTGATAGACCAG
ACCCGGGAGTTCCTGCACGCTGCAGAGACCCCGGTGCCCAGCGTCGGGGAGTACCTCAAG
AAGGAGATTGGCCAGCACGTGGCGAGGCTCTGCGGCCACTCCGCCTTCCCACACCTGCGG
GTCCTGGAGGCCACGGCCCGCGCCGGGGGCCGCATCCGCTCGGAGCGCTGCTTCGGTGGC
GTGGTGGAGGTGGGCGCGCACTGGATCCATGGGCCCTCCCGGGGTAACCCCGTCTTCCAG
CTGGCTGCTGAGTACGGGCTGCTGGGGGAGAAGGAGCTGTCCCAGGAGAACCAGCTGGTG
GAGACCGGGGGTCACGTGGGCCTGCCCTCCGTGAGCTACGCCAGCTCCGGAGCCAGCGTG
AGCCTCCAGCTGGTGGCGGAGATGGCGACTCTGTTCTACGGCCTGATAGACCAGACCCGG
GAGTTCCTGCACGCTGCAGAGACCCCGGTGCCCAGCGTCGGGGAGTACCTCAAGAAGGAG
ATTGGCCAGCACGTGGCCGGCTGGACAGAGGATGAGGAGACCAGGAAGCTGAAGCTGGCC
GTCCTGAACTCCTTCTTCAACCTGGAATGCTGTGTGAGCGGCACCCACAGCATGGACCTG
GTGGCCCTGGCACCCTTTGGGGAGTATACCGTGCTGCCGGGGCTGGACTGCACCTTTTCT
AAGGGCTATCAAGGACTCACAAACTGCATGATGGCCGCCCTGCCGGAGGACACTGTAGTT
TTTGAGAAGCCTGTGAAGACCATCCACTGGAACGGGTCCTTCCAGGAGGCAGCCTTTCCC
GGGGAGACCTTTCCAGTGTCGGTAGAGTGTGAGGATGGAGACCGGTTCCCGGCGCACCAT
GTCATCGTCACCGTGCCCTTAGGTTTTCTTAGGGAACATTTGGACACCTTCTTTGACCCT
CCCCTGCCGGCTGAGAAGGCAGAAGCAATCAGGAAGATAGGCTTTGGGACCAACAACAAA
ATCTTCCTGGAGTTTGAGGAGCCCTTCTGGGAGCCAGACTGCCAGCTGATCCAGCTGGTG
TGGGAGGACACGTCGCCCCTGGAGGATGCTGCCCCTGAGCTACAGGACGCCTGGTTCCGG
AAGCTCATTGGCTTTGTGGTCCTGCCTGCCTTTGCGTCTGTCCACGTTCTCTGTGGGTTC
ATTGCCGGACTTGAGTCTGAGTTCATGGAGACTCTGTCGGATGAAGAAGTACTTCTGTGT
CTCACCCAAGTGCTCCGGAGAGTGACAGGAAACCCACGGCTCCCCGCGCCCAAGAGCGTC
CTGCGGTCTCGCTGGCACAGCGCCCCGTACACTAGGGGGTCCTACAGCTACGTGGCCGTG
GGCAGTACTGGGGGCGACCTGGACCTGCTGGCTCAGCCCCTCCCTGCAGACGGCGCCGGC
GCCCAGCTCCAGATCCTGTTTGCGGGGGAAGCCACACATCGCACGTTTTACTCCACGACG
CACGGGGCTCTGCTGTCGGGATGGAGGGAGGCCGACCGCCTCCTCAGTCTGTGGGCCCCG
CAGGTGCAGCAGCCCAGGCCGAGGCTCTAG
Enzyme 2 GenBank Gene ID AY541520 Link Image
Enzyme 2 GeneCard ID PAOX Link Image
Enzyme 2 GenAtlas ID PAOX Link Image
Enzyme 2 HGNC ID HGNC:20837 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 10q26.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Wu T, Yankovskaya V, McIntire WS: Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. J Biol Chem. 2003 Jun 6;278(23):20514-25. Epub 2003 Mar 26. [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. 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. 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. 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]
  6. Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochem J. 2003 Feb 15;370(Pt 1):19-28. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5358
Enzyme 3 Name Aldehyde oxidase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name AOX1
Enzyme 3 Protein Sequence >Aldehyde oxidase
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSER
MMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHA
YNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
Enzyme 3 Number of Residues 1338
Enzyme 3 Molecular Weight 147916.7
Enzyme 3 Theoretical pI 7.17
Enzyme 3 GO Classification
Function
  • FAD or FADH2 binding
  • NAD or NADH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • purine nucleoside binding
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 71773480 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q06278 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ADO_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >4017 bp
ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
AAGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACACGCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCACTGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGAGAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGAACTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGTTATAATTTCTCCTGATAGAATTGAAGAACTGAGTGTTGTAAACCATGCA
TATAATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCTACTCAAGG
AAGTGGGAATTTGTGTCAGCCTTCCGACAAGCCCAGCGACAGGAGAATGCGCTAGCGATA
GTCAATTCAGGAATGAGAGTCTTTTTTGGAGAAGGGGATGGCATTATTAGAGAGTTATGC
ATCTCATATGGAGGCGTTGGTCCAGCCACCATCTGTGCCAAGAATTCCTGCCAGAAACTC
ATTGGAAGGCACTGGAACGAACAGATGCTGGATATAGCCTGCAGGCTTATTCTGAATGAA
GTCTCCCTTTTGGGCTCGGCGCCAGGTGGGAAAGTGGAGTTCAAGAGGACTCTCATCATC
AGCTTCCTCTTCAAGTTCTACCTGGAAGTGTCACAGATTTTGAAAAAGATGGATCCAGTT
CACTATCCTAGCCTTGCAGACAAGTATGAAAGTGCTTTAGAAGATCTTCATTCCAAACAT
CACTGCAGTACATTAAAGTACCAGAATATAGGCCCAAAGCAGCATCCTGAAGACCCAATT
GGCCACCCCATCATGCATCTGTCTGGTGTGAAGCATGCCACGGGGGAGGCCATCTACTGT
GATGACATGCCTCTGGTGGACCAGGAACTTTTCTTGACTTTTGTGACTAGTTCAAGAGCT
CATGCTAAGATTGTGTCTATTGATCTGTCAGAAGCTCTCAGCATGCCCGGTGTGGTGGAC
ATCATGACAGCAGAACATCTTAGTGACGTCAACTCCTTCTGCTTTTTTACTGAAGCTGAG
AAATTTCTGGCGACAGATAAGGTGTTCTGTGTGGGTCAGCTTGTCTGTGCTGTGCTTGCC
GATTCTGAGGTTCAGGCAAAGCGAGCTGCTAAGCGAGTGAAGATTGTCTATCAAGACTTG
GAGCCGCTGATACTAACAATTGAGGAAAGTATACAACACAACTCCTCCTTCAAGCCAGAA
AGGAAACTGGAATATGGAAATGTTGACGAAGCATTTAAAGTGGTTGATCAAATTCTTGAA
GGTGAAATACATATGGGAGGTCAAGAACATTTTTATATGGAAACCCAAAGCATGCTTGTC
GTTCCCAAGGGAGAGGATCAAGAAATGGATGTCTACGTGTCCACACAGTTTCCCAAATAT
ATACAGGACATTGTTGCCTCAACCTTGAAGCTCCCAGCTAACAAGGTCATGTGCCATGTA
AGGCGTGTTGGTGGAGCGTTTGGAGGGAAGGTGTTAAAAACCGGAATCATTGCAGCCGTC
ACTGCATTTGCCGCAAACAAACATGGCCGTGCAGTTCGCTGTGTTCTGGAACGAGGAGAA
GACATGTTAATAACTGGAGGCCGCCATCCTTACCTTGGAAAGTACAAAGCTGGATTCATG
AACGATGGCAGAATCTTGGCCCTGGACATGGAGCATTACAGCAATGCAGGCGCCTCCTTG
GATGAATCATTATTCGTGATAGAAATGGGACTTCTGAAAATGGACAATGCTTACAAGTTT
CCCAATCTCCGCTGCCGGGGTTGGGCATGCAGAACCAACCTTCCATCCAACACAGCTTTT
CGTGGGTTTGGCTTTCCTCAGGCAGCGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGGCTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA
Enzyme 3 GenBank Gene ID NM_001159.3 Link Image
Enzyme 3 GeneCard ID AOX1 Link Image
Enzyme 3 GenAtlas ID AOX1 Link Image
Enzyme 3 HGNC ID HGNC:553 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2q33
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10690-4. [PubMed Link Image]
  2. 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5378
Enzyme 4 Name Peroxisomal acyl-coenzyme A oxidase 1
Enzyme 4 Synonyms
  1. AOX
  2. Palmitoyl-CoA oxidase
  3. Straight-chain acyl-CoA oxidase
  4. SCOX
Enzyme 4 Gene Name ACOX1
Enzyme 4 Protein Sequence >Peroxisomal acyl-coenzyme A oxidase 1
MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRY
EVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQK
EKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGL
GKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYL
KMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIA
IRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIG
QGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF
EGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSP
ESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFS
EKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIR
SDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
Enzyme 4 Number of Residues 660
Enzyme 4 Molecular Weight 74423.0
Enzyme 4 Theoretical pI 8.29
Enzyme 4 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 4 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 4 Specific Function Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs
Enzyme 4 Pathways
Enzyme 4 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 14250616 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q15067 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ACOX1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1983 bp
ATGAACCCGGACCTGCGCAGGGAGCGGGATTCCGCCAGCTTCAACCCGGAGCTGCTTACA
CACATCCTGGACGGCAGCCCCGAGAAAACCCGGCGCCGCCGAGAGATCGAGAACATGATC
CTGAACGACCCAGACTTCCAGCATGAGGACTTGAACTTCCTCACTCGCAGCCAGCGTTAT
GAGGTGGCTGTCAGGAAAAGTGCCATCATGGTGAAGAAGATGAGGGAGTTTGGCATCGCT
GACCCTGATGAAATTATGTGGTTTAAAAATTTTGTGCACCGAGGGCGGCCTGAGCCTCTG
GATCTTCACTTGGGCATGTTCCTGCCCACCTTGCTTCACCAGGCAACTGCGGAGCAGCAG
GAGCGCTTCTTCATGCCCGCCTGGAACTTGGAGATCATTGGCACTTATGCCCAGACAGAG
ATGGGTCATGGAACTCACCTTCGAGGCTTGGAAACCACAGCCACGTATGACCCTGAAACC
CAGGAGTTCATTCTCAACAGTCCTACTGTGACCTCCATTAAATGGTGGCCTGGTGGGCTT
GGAAAGACTTCAAATCATGCAATAGTTCTTGCCCAGCTCATCACTAAGGGGAAATGCTAT
GGATTACATGCCTTTATCGTACCTATTCGTGAAATCGGGACCCATAAGCCTTTGCCAGGA
ATTACCGTTGGTGACATCGGCCCCAAATTTGGTTATGATGAGATAGACAATGGCTACCTC
AAAATGGACAACCATCGTATTCCCAGAGAAAACATGCTGATGAAGTATGCCCAGGTGAAG
CCTGATGGCACATACGTGAAACCGCTGAGTAACAAGCTGACTTACGGGACCATGGTGTTT
GTCAGGTCCTTCCTTGTGGGAGAAGCTGCTCGGGCTCTGTCTAAGGCGTGCACCATTGCC
ATCCGATACAGCGCTGTGAGGCACCAGTCTGAAATGAAGCCAGGTGAACCAGAACCACAG
ATTTTGGATTTTCAAACCCAGCAGTATAAACTCTTTCCACTCCTGGCCACTGCCTATGCC
TTCCAGTTTGTGGGCGCATACATGAAGGAGACCTATCACCGGATTAACGAAGGCATTGGT
CAAGGGGACCTGAGTGAACTGCCTGAGCTTCATGCCCTCACCGCTGGACTGAAGGCTTTC
ACCTCCTGGACTGCAAACACTGGCATTGAAGCATGTCGGATGGCTTGTGGTGGGCATGGC
TATTCTCATTGCAGTGGTCTTCCAAATATTTATGTCAATTTCACCCCAAGCTGTACCTTT
GAGGGAGAAAACACTGTCATGATGCTCCAGACGGCTAGGTTCCTGATGAAAAGTTATGAT
CAGGTGCACTCAGGAAAGTTGGTGTGTGGCATGGTGTCCTATTTGAACGACCTGCCCAGT
CAGCGCATCCAGCCACAGCAGGTAGCAGTCTGGCCAACCATGGTGGATATCAACAGCCCC
GAAAGCCTAACCGAAGCATATAAACTCCGTGCAGCCAGATTAGTAGAAATTGCTGCAAAA
AACCTTCAAAAAGAAGTGATTCACAGAAAAAGCAAGGAGGTAGCTTGGAACCTAACTTCT
GTTGACCTTGTTCGAGCAAGTGAGGCACATTGCCACTATGTGGTAGTTAAGCTCTTTTCA
GAAAAACTCCTCAAAATTCAAGATAAAGCCATTCAAGCTGTCTTAAGGAGTTTATGTCTG
CTGTATTCTCTGTATGGAATCAGTCAGAACGCGGGGGATTTCCTTCAGGGGAGCATCATG
ACAGAGCCTCAGATTACACAAGTAAACCAGCGTGTAAAGGAGTTACTCACTCTGATTCGC
TCAGATGCTGTTGCTTTGGTTGATGCATTTGATTTTCAGGATGTGACACTTGGCTCTGTG
CTTGGCCGCTATGATGGGAATGTGTATGAAAACTTGTTTGAGTGGGCTAAGAACTCCCCA
CTGAACAAAGCAGAGGTCCACGAATCTTACAAGCACCTGAAGTCACTGCAGTCCAAGCTC
TGA
Enzyme 4 GenBank Gene ID BC008767 Link Image
Enzyme 4 GeneCard ID ACOX1 Link Image
Enzyme 4 GenAtlas ID ACOX1 Link Image
Enzyme 4 HGNC ID HGNC:119 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 17q24-q25|17q25.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK: Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3107-11. [PubMed Link Image]
  2. Chu R, Varanasi U, Chu S, Lin Y, Usuda N, Rao MS, Reddy JK: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [PubMed Link Image]
  3. Fournier B, Saudubray JM, Benichou B, Lyonnet S, Munnich A, Clevers H, Poll-The BT: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest. 1994 Aug;94(2):526-31. [PubMed Link Image]
  4. Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T: Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8. [PubMed Link Image]
  5. 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]
  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. 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. 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. 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. Suzuki Y, Iai M, Kamei A, Tanabe Y, Chida S, Yamaguchi S, Zhang Z, Takemoto Y, Shimozawa N, Kondo N: Peroxisomal acyl CoA oxidase deficiency. J Pediatr. 2002 Jan;140(1):128-30. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5393
Enzyme 5 Name Amine oxidase [flavin-containing] B
Enzyme 5 Synonyms
  1. Monoamine oxidase type B
  2. MAO-B
Enzyme 5 Gene Name MAOB
Enzyme 5 Protein Sequence >Amine oxidase [flavin-containing] B
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
Enzyme 5 Number of Residues 520
Enzyme 5 Molecular Weight 58762.5
Enzyme 5 Theoretical pI 7.55
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 5 General Function Involved in oxidoreductase activity
Enzyme 5 Specific Function Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine
Enzyme 5 Pathways
Enzyme 5 Reactions
  • RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 490-516
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID P27338 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AOFB_HUMAN Link Image
Enzyme 5 PDB ID 2BK3 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1560 bp
ATGAGCAACAAATGCGACGTGGTCGTGGTGGGGGGCGGCATCTCAGGTATGGCAGCAGCC
AAACTTCTGCATGACTCTGGACTGAATGTGGTTGTTCTGGAAGCCCGGGACCGTGTGGGA
GGCAGGACTTACACTCTTAGGAACCAAAAGGTTAAATATGTGGACCTTGGAGGATCCTAT
GTTGGACCAACCCAGAATCGTATCTTGAGATTAGCCAAGGAGCTAGGATTGGAGACCTAC
AAAGTGAATGAGGTTGAGCGTCTGATCCACCATGTAAAGGGCAAATCATACCCCTTCAGG
GGGCCATTCCCACCTGTATGGAATCCAATTACCTACTTAGATCATAACAACTTTTGGAGG
ACAATGGATGACATGGGGCGAGAGATTCCGAGTGATGCCCCATGGAAGGCTCCCCTTGCA
GAAGAGTGGGACAACATGACAATGAAGGAGCTACTGGACAAGCTCTGCTGGACTGAATCT
GCAAAGCAGCTTGCCACTCTCTTTGTGAACCTGTGTGTCACTGCAGAGACCCATGAGGTC
TCTGCTCTCTGGTTCCTGTGGTATGTGAAGCAGTGTGGAGGCACAACAAGAATCATCTCG
ACAACAAATGGAGGACAGGAGAGGAAATTTGTGGGCGGATCTGGTCAAGTGAGTGAGCGG
ATAATGGACCTCCTTGGAGACCGAGTGAAGCTGGAGAGGCCTGTGATCTACATTGACCAG
ACAAGAGAAAATGTCCTTGTGGAGACCCTAAACCATGAGATGTATGAGGCTAAATATGTG
ATTAGTGCTATTCCTCCTACTCTGGGCATGAAGATTCACTTCAATCCCCCTCTGCCAATG
ATGAGAAACCAGATGATCACTCGTGTGCCTTTGGGTTCAGTCATCAAGTGTATAGTTTAT
TATAAAGAGCCTTTCTGGAGGAAAAAGGATTACTGTGGAACCATGATTATTGATGGAGAA
GAAGCTCCAGTTGCCTACACGTTGGATGATACCAAACCTGAAGGCAACTATGCTGCCATA
ATGGGATTTATCCTGGCCCACAAAGCCAGAAAACTGGCACGTCTTACCAAAGAGGAAAGG
TTGAAGAAACTTTGTGAACTCTATGCCAAGGTTCTGGGTTCCCTAGAAGCTCTGGAGCCA
GTGCATTATGAAGAAAAGAACTGGTGTGAGGAGCAGTACTCTGGGGGCTGCTACACAACT
TATTTCCCCCCTGGGATCCTGACTCAATATGGAAGGGTTCTACGCCAGCCAGTGGACAGG
ATTTACTTTGCAGGCACCGAGACTGCCACACACTGGAGCGGCTACATGGAGGGGGCTGTA
GAGGCCGGGGAGAGAGCAGCCCGAGAGATCCTGCATGCCATGGGGAAGATTCCAGAGGAT
GAAATCTGGCAGTCAGAACCAGAGTCTGTGGATGTCCCTGCACAGCCCATCACCACCACC
TTTTTGGAGAGACATTTGCCCTCCGTGCCAGGCCTGCTCAGGCTGATTGGATTGACCACC
ATCTTTTCAGCAACGGCTCTTGGCTTCCTGGCCCACAAAAGGGGGCTACTTGTGAGAGTC
Enzyme 5 GenBank Gene ID S62734 Link Image
Enzyme 5 GeneCard ID MAOB Link Image
Enzyme 5 GenAtlas ID MAOB Link Image
Enzyme 5 HGNC ID HGNC:6834 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [PubMed Link Image]
  2. Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed Link Image]
  3. Chen K, Wu HF, Shih JC: The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical. J Neurochem. 1993 Jul;61(1):187-90. [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. 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]
  6. Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed Link Image]
  7. Newton-Vinson P, Hubalek F, Edmondson DE: High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif. 2000 Nov;20(2):334-45. [PubMed Link Image]
  8. Cesura AM, Gottowik J, Lahm HW, Lang G, Imhof R, Malherbe P, Rothlisberger U, Da Prada M: Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis. Eur J Biochem. 1996 Mar 15;236(3):996-1002. [PubMed Link Image]
  9. Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed Link Image]
  10. Binda C, Newton-Vinson P, Hubalek F, Edmondson DE, Mattevi A: Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol. 2002 Jan;9(1):22-6. [PubMed Link Image]
  11. Binda C, Li M, Hubalek F, Restelli N, Edmondson DE, Mattevi A: Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9750-5. Epub 2003 Aug 11. [PubMed Link Image]
  12. Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J Med Chem. 2004 Mar 25;47(7):1767-74. [PubMed Link Image]
  13. Hubalek F, Binda C, Khalil A, Li M, Mattevi A, Castagnoli N, Edmondson DE: Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors. J Biol Chem. 2005 Apr 22;280(16):15761-6. Epub 2005 Feb 14. [PubMed Link Image]
  14. Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis. J Med Chem. 2005 Dec 29;48(26):8148-54. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5401
Enzyme 6 Name Amine oxidase [flavin-containing] A
Enzyme 6 Synonyms
  1. Monoamine oxidase type A
  2. MAO-A
Enzyme 6 Gene Name MAOA
Enzyme 6 Protein Sequence >Amine oxidase [flavin-containing] A
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
Enzyme 6 Number of Residues 527
Enzyme 6 Molecular Weight 59681.3
Enzyme 6 Theoretical pI 7.96
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 oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine
Enzyme 6 Pathways
Enzyme 6 Reactions
  • RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 498-518
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 187355 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P21397 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AOFA_HUMAN Link Image
Enzyme 6 PDB ID 1O5W Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1584 bp
ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGTCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCAGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGACATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
Enzyme 6 GenBank Gene ID M69226 Link Image
Enzyme 6 GeneCard ID MAOA Link Image
Enzyme 6 GenAtlas ID MAOA Link Image
Enzyme 6 HGNC ID HGNC:6833 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO: Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem. 1988 Oct;51(4):1321-4. [PubMed Link Image]
  2. Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed Link Image]
  3. Chen ZY, Hotamisligil GS, Huang JK, Wen L, Ezzeddine D, Aydin-Muderrisoglu N, Powell JF, Huang RH, Breakefield XO, Craig I, et al.: Structure of the human gene for monoamine oxidase type A. Nucleic Acids Res. 1991 Aug 25;19(16):4537-41. [PubMed Link Image]
  4. Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [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. Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed Link Image]
  7. Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed Link Image]
  8. Denney RM, Sharma A, Dave SK, Waguespack A: A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression. J Neurochem. 1994 Sep;63(3):843-56. [PubMed Link Image]
  9. Chen SA, Weyler W: Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B. Biochem Biophys Res Commun. 1988 Oct 14;156(1):445-50. [PubMed Link Image]
  10. Weyler W: Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Biochem J. 1989 Jun 15;260(3):725-9. [PubMed Link Image]
  11. Li M, Hubalek F, Newton-Vinson P, Edmondson DE: High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif. 2002 Feb;24(1):152-62. [PubMed Link Image]
  12. Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed Link Image]
  13. De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A: Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12684-9. Epub 2005 Aug 29. [PubMed Link Image]
  14. Brunner HG, Nelen M, Breakefield XO, Ropers HH, van Oost BA: Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A. Science. 1993 Oct 22;262(5133):578-80. [PubMed Link Image]
  15. Son SY, Ma J, Kondou Y, Yoshimura M, Yamashita E, Tsukihara T: Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5739-44. Epub 2008 Apr 7. [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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5413
Enzyme 7 Name Xanthine dehydrogenase/oxidase
Enzyme 7 Synonyms
  1. Xanthine dehydrogenase
  2. XD
  3. Xanthine oxidase
  4. XO
  5. Xanthine oxidoreductase
Enzyme 7 Gene Name XDH
Enzyme 7 Protein Sequence >Xanthine dehydrogenase/oxidase
MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDR
LQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI
VMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCC
MNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAS
TLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFG
AACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISD
LNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSA
FKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKE
ELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLD
PTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRY
ENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDK
VTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDL
KKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKM
LGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGR
HPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGR
LCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKL
EGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGA
LLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAA
SVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLG
YSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAF
VQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAV
GEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVT
GVPENCKPWSVRV
Enzyme 7 Number of Residues 1333
Enzyme 7 Molecular Weight 146423.0
Enzyme 7 Theoretical pI 7.70
Enzyme 7 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • molybdenum ion binding
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
  • oxidoreductase activity, acting on CH or CH2 groups, oxygen as acceptor
  • purine nucleoside binding
  • transition metal ion binding
  • xanthine dehydrogenase activity
  • xanthine oxidase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 7 General Function Involved in oxidoreductase activity
Enzyme 7 Specific Function Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • xanthine + H2O + O2 = urate + H2O2 [RN:R02107]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID P47989 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name XDH_HUMAN Link Image
Enzyme 7 PDB ID 1V97 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >4002 bp
ATGACAGCAGACAAATTGGTTTTCTTTGTGAATGGCAGAAAGGTGGTGGAGAAAAATGCA
GATCCAGAGACAACCCTTTTGGCCTACCTGAGAAGAAAGTTGGGGCTGAGTGGAACCAAG
CTCGGCTGTGGAGAGGGGGGCTGCGGGGCTTGCACAGTGATGCTCTCCAAGTATGATCGT
CTGCAGAACAAGATCGTCCACTTTTCTGCCAATGCCTGCCTGGCCCCCATCTGCTCCTTG
CACCATGTTGCAGTGACAACTGTGGAAGGAATAGGAAGCACCAAGACGAGGCTGCATCCT
GTGCAGGAGAGAATTGCCAAAAGCCACGGCTCCCAGTGCGGGTTCTGCACCCCTGGCATC
GTCATGAGTATGTACACACTGCTCCGGAATCAGCCCGAGCCCACCATGGAGGAGATTGAG
AATGCCTTCCAAGGAAATCTGTGCCGCTGCACAGGCTACAGACCCATCCTCCAGGGCTTC
CGGACCTTTGCCAGGGATGGTGGATGCTGTGGAGGAGATGGGAATAATCCAAATTGCTGC
ATGAACCAGAAGAAAGACCACTCAGTCAGCCTCTCGCCATCTTTATTCAAACCAGAGGAG
TTCACGCCCCTGGATCCAACCCAGGAGCCCATTTTTCCCCCAGAGTTGCTGAGGCTGAAA
GACACTCCTCGGAAGCAGCTGCGATTTGAAGGGGAGCGTGTGACGTGGATACAGGCCTCA
ACCCTCAAGGAGCTGCTGGACCTCAAGGCTCAGCACCCTGACGCCAAGCTGGTCGTGGGG
AACACGGAGATTGGCATTGAGATGAAGTTCAAGAATATGCTGTTTCCTATGATTGTCTGC
CCAGCCTGGATCCCTGAGCTGAATTCGGTAGAACATGGACCCGACGGTATCTCCTTTGGA
GCTGCTTGCCCCCTGAGCATTGTGGAAAAAACCCTGGTGGATGCTGTTGCTAAGCTTCCT
GCCCAAAAGACAGAGGTGTTCAGAGGGGTCCTGGAGCAGCTGCGCTGGTTTGCTGGGAAG
CAAGTCAAGTCTGTGGCGTCCGTTGGAGGGAACATCATCACTGCCAGCCCCATCTCCGAC
CTCAACCCCGTGTTCATGGCCAGTGGGGCCAAGCTGACACTTGTGTCCAGAGGCACCAGG
AGAACTGTCCAGATGGACCACACCTTCTTCCCTGGCTACAGAAAGACCCTGCTGAGCCCG
GAGGAGATACTGCTCTCCATAGAGATCCCCTACAGCAGGGAGGGGGAGTATTTCTCAGCA
TTCAAGCAGGCCTCCCGGAGAGAAGATGACATTGCCAAGGTAACCAGTGGCATGAGAGTT
TTATTCAAGCCAGGAACCACAGAGGTACAGGAGCTGGCCCTTTGCTATGGTGGAATGGCC
AACAGAACCATCTCAGCCCTCAAGACCACTCAGAGGCAGCTTTCCAAGCTCTGGAAGGAG
GAGCTGCTGCAGGACGTGTGTGCAGGACTGGCAGAGGAGCTGCATCTGCCTCCCGATGCC
CCTGGTGGCATGGTGGACTTCCGGTGCACCCTCACCCTCAGCTTCTTCTTCAAGTTCTAC
CTGACAGTCCTTCAGAAGCTGGGCCAAGAGAACCTGGAAGACAAGTGTGGTAAACTGGAC
CCCACTTTCGCCAGTGCAACTTTACTGTTTCAGAAAGACCCCCCAGCCGATGTCCAGCTC
TTCCAAGAGGTGCCCAAGGGTCAGTCTGAGGAGGACATGGTGGGCCGGCCCCTGCCCCAC
CTGGCAGCGGACATGCAGGCCTCTGGTGAGGCCGTGTACTGTGACGACATTCCTCGCTAC
GAGAATGAGCTGTCTCTCCGGCTGGTCACCAGCACCCGGGCCCACGCCAAGATCAAGTCC
ATAGATACATCAGAAGCTAAGAAGGTTCCAGGGTTTGTTTGTTTCATTTCCGCTGATGAT
GTTCCTGGGAGTAACATAACTGGAATTTGTAATGATGAGACAGTCTTTGCGAAGGATAAG
GTTACTTGTGTTGGGCATATCATTGGTGCTGTGGTTGCTGACACCCCGGAACACACACAG
AGAGCTGCCCAAGGGGTGAAAATCACCTATGAAGAACTACCAGCCATTATCACAATTGAG
GATGCTATAAAGAACAACTCCTTTTATGGACCTGAGCTGAAGATCGAGAAAGGGGACCTA
AAGAAGGGGTTTTCCGAAGCAGATAATGTTGTGTCAGGGGAGATATACATCGGTGGCCAA
GAGCACTTCTACCTGGAGACTCACTGCACCATTGCTGTTCCAAAAGGCGAGGCAGGGGAG
ATGGAGCTCTTTGTGTCTACACAGAACACCATGAAGACCCAGAGCTTTGTTGCAAAAATG
TTGGGGGTTCCAGCAAACCGGATTGTGGTTCGAGTGAAGAGAATGGGAGGAGGCTTTGGA
GGCAAGGAGACCCGGAGCACTGTGGTGTCCACGGCAGTGGCCCTGGCTGCATATAAGACC
GGCCGCCCTGTGCGATGCATGCTGGACCGTGATGAGGACATGCTGATAACTGGTGGCAGA
CATCCCTTCCTGGCCAGATACAAGGTTGGCTTCATGAAGACTGGGACAGTTGTGGCTCTT
GAGGTGGACCACTTCAGCAATGTGGGGAACACCCAGGATCTCTCTCAGAGTATTATGGAA
CGAGCTTTATTCCACATGGACAACTGCTATAAAATCCCCAACATCCGGGGCACTGGGCGG
CTGTGCAAAACCAACCTTCCCTCCAACACGGCCTTCCGGGGCTTTGGGGGGCCCCAGGGG
ATGCTCATTGCCGAGTGCTGGATGAGTGAAGTTGCAGTGACCTGTGGGATGCCTGCAGAG
GAGGTGCGGAGAAAAAACCTGTACAAAGAAGGGGACCTGACACACTTCAACCAGAAGCTT
GAGGGTTTCACCTTGCCCAGATGCTGGGAAGAATGCCTAGCAAGCTCTCAGTATCATGCT
CGGAAGAGTGAGGTTGACAAGTTCAACAAGGAGAATTGTTGGAAAAAGAGAGGATTGTGC
ATAATTCCCACCAAGTTTGGAATAAGCTTCACAGTTCCTTTTCTGAATCAGGCAGGAGCC
CTACTTCATGTGTACACAGATGGCTCTGTGCTGCTGACCCACGGGGGGACTGAGATGGGC
CAAGGCCTTCATACCAAAATGGTCCAGGTGGCCAGTAGAGCTCTGAAAATCCCCACCTCT
AAGATTTATATCAGCGAGACAAGCACTAACACTGTGCCCAACACCTCTCCCACGGCTGCC
TCTGTCAGCGCTGACCTCAATGGACAGGCCGTCTATGCGGCTTGTCAGACCATCTTGAAA
AGGCTGGAACCCTACAAGAAGAAGAATCCCAGTGGCTCCTGGGAAGACTGGGTCACAGCT
GCCTACATGGACACAGTGAGCTTGTCTGCCACTGGGTTTTATAGAACACCCAATCTGGGC
TACAGCTTTGAGACTAACTCAGGGAACCCCTTCCACTACTTCAGCTATGGGGTGGCTTGC
TCTGAAGTAGAAATCGACTGCCTAACAGGAGATCATAAGAACCTCCGCACAGATATTGTC
ATGGATGTTGGCTCCAGTCTAAACCCTGCCATTGATATTGGACAGGTGGAAGGGGCATTT
GTCCAGGGCCTTGGCCTCTTCACCCTAGAGGAGCTACACTATTCCCCCGAGGGGAGCCTG
CACACCCGTGGCCCTAGCACCTACAAGATCCCGGCATTTGGCAGCATCCCCATTGAGTTC
AGGGTGTCCCTGCTCCGCGACTGCCCCAACAAGAAGGCCATCTATGCATCGAAGGCTGTT
GGAGAGCCGCCCCTCTTCCTGGCTGCTTCTATCTTCTTTGCCATCAAAGATGCCATCCGT
GCAGCTCGAGCTCAGCACACAGGTAATAACGTGAAGGAACTCTTCCGGCTAGACAGCCCT
GCCACCCCGGAGAAGATCCGCAATGCCTGCGTGGACAAGTTCACCACCCTGTGTGTCACT
GGTGTCCCAGAAAACTGCAAACCCTGGTCTGTGAGGGTCTAA
Enzyme 7 GenBank Gene ID D11456 Link Image
Enzyme 7 GeneCard ID XDH Link Image
Enzyme 7 GenAtlas ID XDH Link Image
Enzyme 7 HGNC ID HGNC:12805 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 2p23.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T: Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene. 1993 Nov 15;133(2):279-84. [PubMed Link Image]
  2. Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1994 Mar 15;199(2):998-1004. [PubMed Link Image]
  3. Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1995 Oct 4;215(1):429. [PubMed Link Image]
  4. Saksela M, Raivio KO: Cloning and expression in vitro of human xanthine dehydrogenase/oxidase. Biochem J. 1996 Apr 1;315 ( Pt 1):235-9. [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]
  6. Ichida K, Amaya Y, Kamatani N, Nishino T, Hosoya T, Sakai O: Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria. J Clin Invest. 1997 May 15;99(10):2391-7. [PubMed Link Image]
  7. Levartovsky D, Lagziel A, Sperling O, Liberman U, Yaron M, Hosoya T, Ichida K, Peretz H: XDH gene mutation is the underlying cause of classical xanthinuria: a second report. Kidney Int. 2000 Jun;57(6):2215-20. [PubMed Link Image]
  8. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed Link Image]
  9. Yamaguchi Y, Matsumura T, Ichida K, Okamoto K, Nishino T: Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate. J Biochem. 2007 Apr;141(4):513-24. Epub 2007 Feb 14. [PubMed Link Image]
  10. Sakamoto N, Yamamoto T, Moriwaki Y, Teranishi T, Toyoda M, Onishi Y, Kuroda S, Sakaguchi K, Fujisawa T, Maeda M, Hada T: Identification of a new point mutation in the human xanthine dehydrogenase gene responsible for a case of classical type I xanthinuria. Hum Genet. 2001 Apr;108(4):279-83. [PubMed Link Image]
  11. Gok F, Ichida K, Topaloglu R: Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria. Nephrol Dial Transplant. 2003 Nov;18(11):2278-83. [PubMed Link Image]
  12. 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5416
Enzyme 8 Name Dihydroorotate dehydrogenase, mitochondrial
Enzyme 8 Synonyms
  1. DHOdehase
  2. Dihydroorotate oxidase
Enzyme 8 Gene Name DHODH
Enzyme 8 Protein Sequence >Dihydroorotate dehydrogenase, mitochondrial
MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVR
FTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSV
TPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVN
LGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQER
DGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSET
GGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTF
WGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR
Enzyme 8 Number of Residues 395
Enzyme 8 Molecular Weight 42866.9
Enzyme 8 Theoretical pI 10.23
Enzyme 8 GO Classification
Function
  • catalytic activity
  • dihydroorotate dehydrogenase activity
  • dihydroorotate oxidase activity
  • 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
  • membrane
Enzyme 8 General Function Involved in catalytic activity
Enzyme 8 Specific Function (S)-dihydroorotate + a quinone = orotate + a quinol
Enzyme 8 Pathways
Enzyme 8 Reactions
  • (S)-dihydroorotate + a quinone = orotate + a quinol [RN:R01868]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 12-32
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 158258018 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q02127 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PYRD_HUMAN Link Image
Enzyme 8 PDB ID 1D3H Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1188 bp
ATGGCGTGGAGACACCTGCAAAAGCGGGCCCAGGATGCTGTGATCATCCTGGGGGGAGGA
GGACTTCTCTTCGCCTCCTACCTGATGGCCACGGGAGATGAGCGTTTCTATGCTGAACAC
CTGATGCCGACTCTGCAGGGGCTGCTGGACCCGGAGTCAGCCCACAGACTGGCTGTTCGC
TTCACCTCCCTGGGGCTCCTTCCACGGGCCAGATTTCAAGACTCTGACATGCTGGAAGTG
AGAGTTCTGGGCCATAAATTCCGAAATCCAGTAGGAATTGCTGCAGGATTTGACAAGCAT
GGGGAAGCCGTGGACGGACTTTATAAGATGGGCTTTGGTTTTGTTGAGATAGGAAGTGTG
ACTCCAAAACCTCAGGAAGGAAACCCTAGACCCAGAGTCTTCCGCCTCCCTGAGGACCAA
GCTGTCATTAACAGGTATGGATTTAACAGTCACGGGCTTTCAGTGGTGGAACACAGGTTA
CGGGCCAGACAGCAGAAGCAGGCCAAGCTCACAGAAGATGGACTGCCTCTGGGGGTCAAC
TTGGGGAAGAACAAGACCTCAGTGGACGCCGCGGAGGACTACGCAGAAGGGGTGCGCGTA
CTGGGCCCCCTGGCCGACTACCTGGTGGTGAATGTGTCCAGCCCCAACACTGCCGGGCTG
CGGAGCCTTCAGGGAAAGGCCGAGCTGCGCCGCCTGCTGACCAAGGTGCTGCAGGAGAGG
GATGGCTTGCGGAGAGTGCACAGGCCGGCAGTCCTGGTGAAGATCGCTCCTGACCTCACC
AGCCAGGATAAGGAGGACATTGCCAGTGTGGTCAAAGAGTTGGGCATCGATGGGCTGATT
GTTACGAACACCACCGTGAGTCGCCCTGCGGGCCTCCAGGGTGCCCTGCGCTCTGAAACA
GGAGGGCTGAGTGGGAAGCCCCTCCGGGATTTATCAACTCAAACCATTCGGGAGATGTAT
GCACTCACCCAAGGCCGAGTTCCCATAATTGGGGTTGGTGGTGTGAGCAGCGGGCAGGAC
GCGCTGGAGAAGATCCGGGCAGGGGCCTCCCTGGTGCAGCTGTACACGGCCCTCACCTTC
TGGGGGCCACCCGTTGTGGGCAAAGTCAAGCGGGAACTGGAGGCCCTTCTGAAAGAGCAG
GGCTTTGGCGGAGTCACAGATGCCATTGGAGCAGATCATCGGAGGTGA
Enzyme 8 GenBank Gene ID AK292293 Link Image
Enzyme 8 GeneCard ID DHODH Link Image
Enzyme 8 GenAtlas ID DHODH Link Image
Enzyme 8 HGNC ID HGNC:2867 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 16q22
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Minet M, Dufour ME, Lacroute F: Cloning and sequencing of a human cDNA coding for dihydroorotate dehydrogenase by complementation of the corresponding yeast mutant. Gene. 1992 Nov 16;121(2):393-6. [PubMed Link Image]
  2. Copeland RA, Davis JP, Dowling RL, Lombardo D, Murphy KB, Patterson TA: Recombinant human dihydroorotate dehydrogenase: expression, purification, and characterization of a catalytically functional truncated enzyme. Arch Biochem Biophys. 1995 Oct 20;323(1):79-86. [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. Knecht W, Bergjohann U, Gonski S, Kirschbaum B, Loffler M: Functional expression of a fragment of human dihydroorotate dehydrogenase by means of the baculovirus expression vector system, and kinetic investigation of the purified recombinant enzyme. Eur J Biochem. 1996 Aug 15;240(1):292-301. [PubMed Link Image]
  6. Liu S, Neidhardt EA, Grossman TH, Ocain T, Clardy J: Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents. Structure. 2000 Jan 15;8(1):25-33. [PubMed Link Image]
  7. Ng SB, Buckingham KJ, Lee C, Bigham AW, Tabor HK, Dent KM, Huff CD, Shannon PT, Jabs EW, Nickerson DA, Shendure J, Bamshad MJ: Exome sequencing identifies the cause of a mendelian disorder. Nat Genet. 2010 Jan;42(1):30-5. Epub 2009 Nov 13. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5424
Enzyme 9 Name Peroxisomal acyl-coenzyme A oxidase 3
Enzyme 9 Synonyms
  1. Branched-chain acyl-CoA oxidase
  2. BRCACox
  3. Pristanoyl-CoA oxidase
Enzyme 9 Gene Name ACOX3
Enzyme 9 Protein Sequence >Peroxisomal acyl-coenzyme A oxidase 3
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPL
FARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAK
YLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPAT
EEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMP
GVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS
LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL
AAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQ
ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFR
SPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSG
SSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSL
SRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADG
ELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL
Enzyme 9 Number of Residues 700
Enzyme 9 Molecular Weight 77628.3
Enzyme 9 Theoretical pI 7.27
Enzyme 9 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 9 General Function Involved in oxidoreductase activity, acting on the CH-CH group of donors
Enzyme 9 Specific Function Oxidizes the CoA-esters of 2-methyl-branched fatty acids
Enzyme 9 Pathways
Enzyme 9 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 2326549 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O15254 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ACOX3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2103 bp
ATGGCATCCACTGTGGAAGGAGGCGACACAGCTCTGCTCCCAGAATTCCCCAGGGGGCCC
CTCGATGCCTACCGAGCAAGAGCGTCCTTCAGCTGGAAGGACGTGGCGCTGTTCACGGAA
GGGGAGGGCAATGTCCGCTTTAAGAAAACCATCTTCTCAGCTCTTGAGAATGACCCTCTT
TTCGCTCGTTCCCCTGGAGCCGACCTGTCCTTGGAGAAGTATCGCGAGCTGAACTTCCTT
CGATGCAAGCGGATCTTCGAGTATGACTTCCTCAGTGTCGAAGCAATGTTCAAGAGCCCT
CTGAAGGTCCCCGCCTTGATTCAGTGCCTGGGCATGTATGACTCTTCTCTGGCTGCCAAG
TACCTCCTCCATAGCTTGGTTTTTGGATCAGCAGTTTACAGTTCTGGTTCTGAAAGACAT
CTCACATATATTCAAAAGATCTTCAGGATGGAGATTTTTGGATGTTTTGCTCTGACCGAA
TTAAGCCACGGCAGTAATACCAAGGCCATTCGCACAACTGCCCACTACGATCCTGCCACT
GAGGAATTCATCATACATTCCCCTGATTTCGAAGCTGCCAAGTTTTGGGTTGGCAACATG
GGCAAGACAGCCACTCACGCGGTGGTGTTTGCTAAGCTGTGTGTGCCAGGGGACCAGTGC
CATGGGCTGCATCCCTTTATCGTGCAGATCCGGGACCCGAAGACCCTTCTTCCCATGCCT
GGAGTGATGGTTGGCGACATAGGAAAAAAACTCGGGCAGAACGGTCTAGATAATGGTTTC
GCCATGTTCCACAAGGTCAGAGTTCCTCGCCAGAGCCTTCTGAACCGGATGGGAGACGTC
ACCCCCGAGGGCACCTATGTCAGCCCCTTTAAGGACGTCAGGCAGCGCTTTGGAGCGTCC
CTGGGGAGCCTGTCCTCGGGCCGGGTCTCCATCGTGAGCCTGGCCATCCTTAACCTAAAG
CTGGCCGTGGCCATCGCTCTTCGCTTCTCAGCCACTCGGCGTCAGTTTGGACCCACAGAG
GAGGAGGAAATACCAGTGCTTGAGTATCCAATGCAGCAATGGCGCTTGCTTCCATATCTG
GCAGCTGTCTACGGCTTAGACCATTTCTCCAAGTCGCTCTTCCTGGACCTGGTGGAGCTC
CAGCGAGGACTTGCATCGGGAGACCGCAGCGCCAGACAGGCAGAGCTTGGACGTGAGATC
CACGCCCTGGCATCGGCCAGCAAGCCCCTGGCCTCGTGGACCACCCAGCAAGGAATTCAG
GAATGCCGGGAGGCGTGTGGAGGACACGGCTATCTGGCCATGAACCGGTTGGGTGTCCTT
AGAGATGACAACGATCCCAACTGCACATACGAAGGTGACAACAACATCCTGCTGCAGCAG
ACAAGCAACTATTTGCTGGGTCTCCTGGCACACCAGGTCCACGATGGAGCTTGCTTCCGC
AGTCCGCTGAAGTCAGTGGACTTTCTGGACGCCTATCCCGGCATCCTTGACCAGAAGTTT
GAGGTCTCCAGTGTTGCCGACTGCTTGGACTCTGCAGTCGCCCTGGCAGCATACAAGTGG
CTGGTTTGCTACCTGCTCCGAGAGACTTATCAAAAATTAAACCAAGAGAAAAGATCAGGA
AGCAGTGACTTTGAAGCAAGGAACAAATGCCAGGTGTCCCACGGCCGTCCGTTGGCGCTG
GCCTTCGTGGAGCTCACGGTGGTCCAGAGGTTCCACGAGCACGTGCACCAGCCTTCCGTG
CCGCCCTCGCTGCGGGCCGTGCTGGGGCGGCTCAGTGCTCTGTACGCCCTGTGGTCCCTG
AAGCGCCACGCGGCCCTGCTCTACCGAGGAGGATACTTCTCCGGTGAGCAGGCGGGAGAA
GTGTTGGAGAGCGCCGTCCTGGCTTTGTGTTCCCAGCTGAAAGACGATGCAGTTGCCCTG
GTAGACGTGATCGCTCCTCCTGACTTTGTTCTGGACTCACCGATTGGCAGAGCCGACGGC
GAGCTCTACAAAAACCTCTGGGGCGCTGTCCTGCAGGAAAGCAAGGTGTTGGAGCGGGCA
TCCTGGTGGCCAGAGTTTTCTGTGAACAAACCTGTCATAGGAAGTCTGAAATCGAAGCTC
TAG
Enzyme 9 GenBank Gene ID Y11411 Link Image
Enzyme 9 GeneCard ID ACOX3 Link Image
Enzyme 9 GenAtlas ID ACOX3 Link Image
Enzyme 9 HGNC ID HGNC:121 Link Image
Enzyme 9 Chromosome Location 4
Enzyme 9 Locus 4p15.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP: Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem J. 1997 Aug 1;325 ( Pt 3):593-9. [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. 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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5438
Enzyme 10 Name D-amino-acid oxidase
Enzyme 10 Synonyms
  1. DAAO
  2. DAMOX
  3. DAO
Enzyme 10 Gene Name DAO
Enzyme 10 Protein Sequence >D-amino-acid oxidase
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
Enzyme 10 Number of Residues 347
Enzyme 10 Molecular Weight 39473.7
Enzyme 10 Theoretical pI 6.84
Enzyme 10 GO Classification
Function
  • D-amino-acid oxidase activity
  • binding
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 10 General Function Involved in D-amino-acid oxidase activity
Enzyme 10 Specific Function Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids
Enzyme 10 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • D-Arginine and D-ornithine Metabolism (map00472 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 10 Reactions
  • a D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2 [RN:R01340]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 30446 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P14920 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name OXDA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1044 bp
ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT
GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC
CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC
AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT
TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA
GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA
GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG
GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC
CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC
TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG
CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG
AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC
ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG
GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT
GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT
TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG
GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC
AGAATGCCACCATCCCACCTCTGA
Enzyme 10 GenBank Gene ID X13227 Link Image
Enzyme 10 GeneCard ID DAO Link Image
Enzyme 10 GenAtlas ID DAO Link Image
Enzyme 10 HGNC ID HGNC:2671 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 12q24
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Momoi K, Fukui K, Watanabe F, Miyake Y: Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 1988 Sep 26;238(1):180-4. [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. 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. Fukui K, Miyake Y: Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase. J Biol Chem. 1992 Sep 15;267(26):18631-8. [PubMed Link Image]
  5. Kawazoe T, Tsuge H, Pilone MS, Fukui K: Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 2006 Dec;15(12):2708-17. Epub 2006 Nov 6. [PubMed Link Image]
  6. Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K: Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis. Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. [PubMed Link Image]
  7. Sparey T, Abeywickrema P, Almond S, Brandon N, Byrne N, Campbell A, Hutson PH, Jacobson M, Jones B, Munshi S, Pascarella D, Pike A, Prasad GS, Sachs N, Sakatis M, Sardana V, Venkatraman S, Young MB: The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors. Bioorg Med Chem Lett. 2008 Jun 1;18(11):3386-91. Epub 2008 Apr 13. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5508
Enzyme 11 Name Thyroid peroxidase
Enzyme 11 Synonyms
  1. TPO
Enzyme 11 Gene Name TPO
Enzyme 11 Protein Sequence >Thyroid peroxidase
MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQR
NLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALS
EDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPV
YEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHD
IAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGD
QGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSG
RAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAA
LKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPT
VSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIR
GLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGL
PRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQ
MKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFES
CDSITGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQL
TCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVD
SGRLPRVTWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQ
AVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL
Enzyme 11 Number of Residues 933
Enzyme 11 Molecular Weight 102961.6
Enzyme 11 Theoretical pI 6.75
Enzyme 11 GO Classification
Function
  • antioxidant activity
  • binding
  • calcium ion binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 11 General Function Involved in calcium ion binding
Enzyme 11 Specific Function Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4)
Enzyme 11 Pathways
Enzyme 11 Reactions
  • 2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O [RN:R02810]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-14
Enzyme 11 Transmembrane Regions
  • 847-871
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 339867 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P07202 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PERT_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2802 bp
ATGAGAGCGCTCGCTGTGCTGTCTGTCACGCTGGTTATGGCCTGCACAGAAGCCTTCTTC
CCCTTCATCTCGAGAGGGAAAGAACTCCTTTGGGGAAAGCCTGAGGAGTCTCGTGTCTCT
AGCGTCTTGGAGGAAAGCAAGCGCCTGGTGGACACCGCCATGTACGCCACGATGCAGAGA
AACCTCAAGAAAAGAGGAATCCTTTCTCCAGCTCAGCTTCTGTCTTTTTCCAAACTTCCT
GAGCCAACAAGCGGAGTGATTGCCCGAGCAGCAGAGATAATGGAAACATCAATACAAGCG
ATGAAAAGAAAAGTCAACCTGAAAACTCAACAATCACAGCATCCAACGGATGCTTTATCA
GAAGATCTGCTGAGCATCATTGCAAACATGTCTGGATGTCTCCCTTACATGCTGCCCCCA
AAATGCCCAAACACTTGCCTGGCGAACAAATACAGGCCCATCACAGGAGCTTGCAACAAC
AGAGACCACCCCAGATGGGGCGCCTCCAACACGGCCCTGGCACGATGGCTCCCTCCAGTC
TATGAGGACGGCTTCAGTCAGCCCCGAGGCTGGAACCCCGGCTTCTTGTACAACGGGTTC
CCACTGCCCCCGGTCCGGGAGGTGACAAGACATGTCATTCAAGTTTCAAATGAGGTTGTC
ACAGATGATGACCGCTATTCTGACCTCCTGATGGCATGGGGACAATACATCGACCACGAC
ATCGCGTTCACACCACAGAGCACCAGCAAAGCTGCCTTCGGGGGAGGGGCTGACTGCCAG
ATGACTTGTGAGAACCAAAACCCATGTTTTCCCATACAACTCCCGGAGGAGGCCCGGCCG
GCCGCGGGCACCGCCTGTCTGCCCTTCTACCGCTCTTCGGCCGCCTGCGGCACCGGGGAC
CAAGGCGCGCTCTTTGGGAACCTGTCCACGGCCAACCCGCGGCAGCAGATGAACGGGTTG
ACCTCGTTCCTGGACGCGTCCACCGTGTATGGCAGCTCCCCGGCCCTAGAGAGGCAGCTG
CGGAACTGGACCAGTGCCGAAGGGCTGCTCCGCGTCCACGCGCGCCTCCGGGACTCCGGC
CGCGCCTACCTGCCCTTCGTGCCGCCACGGCGGCCTGCGGCCTGTGCGCCCGAGCCCGGC
ATCCCCGGAGAGACCCGCGGGCCCTGCTTCCTGGCCGGAGACGGCCGCGCCAGCGAGGTC
CCCTCCCTGACGGCACTGCACACGCTGTGGCTGCGCGAGCACAACCGCCTGGCCGCGGCG
CTCAAGGCCCTCAATGCGCACTGGAGCGCGGACGCCGTGTACCAGGAGGCGCGCAAGGTC
GTGGGCGCTCTGCACCAGATCATCACCCTGAGGGATTACATCCCCAGGATCCTGGGACCC
GAGGCCTTCCAGCAGTACGTGGGTCCCTATGAAGGCTATGACTCCACCGCCAACCCCACT
GTGTCCAACGTGTTCTCCACAGCCGCCTTCCGCTTCGGCCATGCCACGATCCACCCGCTG
GTGAGGAGGCTGGACGCCAGCTTCCAGGAGCACCCCGACCTGCCCGGGCTGTGGCTGCAC
CAGGCTTTCTTCAGCCCATGGACATTACTCCGTGGAGGTGGTTTGGACCCACTAATACGA
GGCCTTCTTGCAAGACCAGCCAAACTGCAGGTGCAGGATCAGCTGATGAACGAGGAGCTG
ACGGAAAGGCTCTTTGTGCTGTCCAATTCCAGCACCTTGGATCTGGCGTCCATCAACCTG
CAGAGGGGCCGGGACCACGGGCTGCCAGGTTACAATGAGTGGAGGGAGTTCTGCGGCCTG
CCTCGCCTGGAGACCCCCGCTGACCTGAGCACAGCCATCGCCAGCAGGAGCGTGGCCGAC
AAGATCCTGGACTTGTACAAGCATCCTGACAACATCGATGTCTGGCTGGGAGGCTTAGCT
GAAAACTTCCTCCCCAGGGCTCGGACAGGGCCCCTGTTTGCCTGTCTCATTGGGAAGCAG
ATGAAGGCTCTGCGGGATGGTGACTGGTTTTGGTGGGAGAACAGCCACGTCTTCACGGAT
GCACAGAGGCGTGAGCTGGAGAAGCACTCCCTGTCTCGGGTCATCTGTGACAACACTGGC
CTCACCAGGGTGCCCATGGATGCCTTCCAAGTCGGCAAATTCCCTGAAGACTTTGAGTCT
TGTGACAGCATCCCTGGCATGAACCTGGAGGCCTGGAGGGAAACCTTTCCTCAAGACGAC
AAGTGTGGCTTCCCAGAGAGCGTGGAGAATGGGGACTTTGTGCACTGTGAGGAGTCTGGG
AGGCGCGTGCTGGTGTATTCCTGCCGGCACGGGTATGAGCTCCAAGGCCGGGAGCAGCTC
ACTTGCACCCAGGAAGGATGGGATTTCCAGCCTCCCCTCTGCAAAGATGTGAACGAGTGT
GCAGACGGTGCCCACCCCCCCTGCCACGCCTCTGCGAGGTGCAGAAACACCAAAGGCGGC
TTCCAGTGTCTCTGCGCGGACCCCTACGAGTTAGGAGACGATGGGAGAACCTGCGTAGAC
TCCGGGAGGCTCCCTCGGGCGACTTGGATCTCCATGTCGCTGGCTGCTCTGCTGATCGGA
GGCTTCGCAGGTCTCACCTCGACGGTGATTTGCAGGTGGACACGCACTGGCACTAAATCC
ACACTGCCCATCTCGGAGACAGGCGGAGGAACTCCCGAGCTGAGATGCGGAAAGCACCAG
GCCGTAGGGACCTCACCGCAGCGGGCCGCAGCTCAGGACTCGGAGCAGGAGAGTGCTGGG
ATGGAAGGCCGGGATACTCACAGGCTGCCGAGAGCCCTCTGA
Enzyme 11 GenBank Gene ID J02969 Link Image
Enzyme 11 GeneCard ID TPO Link Image
Enzyme 11 GenAtlas ID TPO Link Image
Enzyme 11 HGNC ID HGNC:12015 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 2p25
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Kimura S, Kotani T, McBride OW, Umeki K, Hirai K, Nakayama T, Ohtaki S: Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5555-9. [PubMed Link Image]
  2. Libert F, Ruel J, Ludgate M, Swillens S, Alexander N, Vassart G, Dinsart C: Complete nucleotide sequence of the human thyroperoxidase-microsomal antigen cDNA. Nucleic Acids Res. 1987 Aug 25;15(16):6735. [PubMed Link Image]
  3. Kimura S, Hong YS, Kotani T, Ohtaki S, Kikkawa F: Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene. Biochemistry. 1989 May 16;28(10):4481-9. [PubMed Link Image]
  4. Barnett PS, Banga JP, Watkins J, Huang GC, Gluckman DR, Page MJ, McGregor AM: Nucleotide sequence of the alternatively spliced human thyroid peroxidase cDNA, TPO-2. Nucleic Acids Res. 1990 Feb 11;18(3):670. [PubMed Link Image]
  5. Ferrand M, Le Fourn V, Franc JL: Increasing diversity of human thyroperoxidase generated by alternative splicing. Characterized by molecular cloning of new transcripts with single- and multispliced mRNAs. J Biol Chem. 2003 Feb 7;278(6):3793-800. Epub 2002 Nov 25. [PubMed Link Image]
  6. Seto P, Hirayu H, Magnusson RP, Gestautas J, Portmann L, DeGroot LJ, Rapoport B: Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. J Clin Invest. 1987 Oct;80(4):1205-8. [PubMed Link Image]
  7. Zanelli E, Henry M, Charvet B, Malthiery Y: Evidence for an alternate splicing in the thyroperoxidase messenger from patients with Graves' disease. Biochem Biophys Res Commun. 1990 Jul 31;170(2):735-41. [PubMed Link Image]
  8. 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]
  9. Bikker H, Vulsma T, Baas F, de Vijlder JJ: Identification of five novel inactivating mutations in the human thyroid peroxidase gene by denaturing gradient gel electrophoresis. Hum Mutat. 1995;6(1):9-16. [PubMed Link Image]
  10. Bikker H, Baas F, De Vijlder JJ: Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects. J Clin Endocrinol Metab. 1997 Feb;82(2):649-53. [PubMed Link Image]
  11. Santos CL, Bikker H, Rego KG, Nascimento AC, Tambascia M, De Vijlder JJ, Medeiros-Neto G: A novel mutation in the TPO gene in goitrous hypothyroid patients with iodide organification defect. Clin Endocrinol (Oxf). 1999 Aug;51(2):165-72. [PubMed Link Image]
  12. Pannain S, Weiss RE, Jackson CE, Dian D, Beck JC, Sheffield VC, Cox N, Refetoff S: Two different mutations in the thyroid peroxidase gene of a large inbred Amish kindred: power and limits of homozygosity mapping. J Clin Endocrinol Metab. 1999 Mar;84(3):1061-71. [PubMed Link Image]
  13. Kotani T, Umeki K, Yamamoto I, Maesaka H, Tachibana K, Ohtaki S: A novel mutation in the human thyroid peroxidase gene resulting in a total iodide organification defect. J Endocrinol. 1999 Feb;160(2):267-73. [PubMed Link Image]
  14. Bakker B, Bikker H, Vulsma T, de Randamie JS, Wiedijk BM, De Vijlder JJ: Two decades of screening for congenital hypothyroidism in The Netherlands: TPO gene mutations in total iodide organification defects (an update). J Clin Endocrinol Metab. 2000 Oct;85(10):3708-12. [PubMed Link Image]
  15. Ambrugger P, Stoeva I, Biebermann H, Torresani T, Leitner C, Gruters A: Novel mutations of the thyroid peroxidase gene in patients with permanent congenital hypothyroidism. Eur J Endocrinol. 2001 Jul;145(1):19-24. [PubMed Link Image]
  16. Umeki K, Kotani T, Kawano J, Suganuma T, Yamamoto I, Aratake Y, Furujo M, Ichiba Y: Two novel missense mutations in the thyroid peroxidase gene, R665W and G771R, result in a localization defect and cause congenital hypothyroidism. Eur J Endocrinol. 2002 Apr;146(4):491-8. [PubMed Link Image]
  17. Niu DM, Hwang B, Chu YK, Liao CJ, Wang PL, Lin CY: High prevalence of a novel mutation (2268 insT) of the thyroid peroxidase gene in Taiwanese patients with total iodide organification defect, and evidence for a founder effect. J Clin Endocrinol Metab. 2002 Sep;87(9):4208-12. [PubMed Link Image]
  18. Wu JY, Shu SG, Yang CF, Lee CC, Tsai FJ: Mutation analysis of thyroid peroxidase gene in Chinese patients with total iodide organification defect: identification of five novel mutations. J Endocrinol. 2002 Mar;172(3):627-35. [PubMed Link Image]
  19. Calaciura F, Miscio G, Coco A, Leonardi D, Cisternino C, Regalbuto C, Bozzali M, Maiorana R, Ranieri A, Carta A, Buscema M, Trischitta V, Sava L, Tassi V: Genetics of specific phenotypes of congenital hypothyroidism: a population-based approach. Thyroid. 2002 Nov;12(11):945-51. [PubMed Link Image]
  20. Kotani T, Umeki K, Kawano J, Suganuma T, Hishinuma A, Ieiri T, Harada S: Partial iodide organification defect caused by a novel mutation of the thyroid peroxidase gene in three siblings. Clin Endocrinol (Oxf). 2003 Aug;59(2):198-206. [PubMed Link Image]
  21. Rivolta CM, Esperante SA, Gruneiro-Papendieck L, Chiesa A, Moya CM, Domene S, Varela V, Targovnik HM: Five novel inactivating mutations in the thyroid peroxidase gene responsible for congenital goiter and iodide organification defect. Hum Mutat. 2003 Sep;22(3):259. [PubMed Link Image]
  22. Fugazzola L, Cerutti N, Mannavola D, Vannucchi G, Fallini C, Persani L, Beck-Peccoz P: Monoallelic expression of mutant thyroid peroxidase allele causing total iodide organification defect. J Clin Endocrinol Metab. 2003 Jul;88(7):3264-71. [PubMed Link Image]
  23. Tajima T, Tsubaki J, Fujieda K: Two novel mutations in the thyroid peroxidase gene with goitrous hypothyroidism. Endocr J. 2005 Oct;52(5):643-5. [PubMed Link Image]
  24. Pfarr N, Borck G, Turk A, Napiontek U, Keilmann A, Muller-Forell W, Kopp P, Pohlenz J: Goitrous congenital hypothyroidism and hearing impairment associated with mutations in the TPO and SLC26A4/PDS genes. J Clin Endocrinol Metab. 2006 Jul;91(7):2678-81. Epub 2006 May 9. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5511
Enzyme 12 Name Lactoperoxidase
Enzyme 12 Synonyms
  1. LPO
  2. Salivary peroxidase
  3. SPO
Enzyme 12 Gene Name LPO
Enzyme 12 Protein Sequence >Lactoperoxidase
MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAM
SSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLE
VGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTP
GKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSE
YSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINAL
TSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTT
ARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAF
VQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDE
NYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQ
PTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGL
YGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDS
LQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN
Enzyme 12 Number of Residues 712
Enzyme 12 Molecular Weight 80287.1
Enzyme 12 Theoretical pI 8.76
Enzyme 12 GO Classification
Function
  • antioxidant activity
  • binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 12 General Function Involved in peroxidase activity
Enzyme 12 Specific Function May contribute to airway host defense against infection
Enzyme 12 Pathways
Enzyme 12 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-26
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID P22079 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PERL_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >2139 bp
ATGAGGGTCCTTCTCCATCTCCCAGCCCTCCTGGCTTCCCTCATCTTGCTTCAGGCTGCA
GCATCTACCACAAGAGCGCAGACTACCAGAACCTCTGCCATCTCCGATACTGTGAGTCAG
GCCAAGGTCCAAGTCAACAAGGCCTTCCTGGACTCCCGAACCAGGCTGAAGACCGCCATG
AGCTCTGAGACTCCCACCAGCCGACAGCTCTCAGAATACCTCAAGCATGCCAAAGGCCGG
ACGCGCACAGCCATCCGCAATGGACAGGTGTGGGAGGAGTCTTTAAAGAGACTGAGGCAG
AAGGCATCCTTGACCAATGTCACAGATCCCAGCCTGGACTTGACTTCACTGTCTCTGGAG
GTGGGCTGTGGTGCTCCTGCTCCCGTGGTGAGATGCGACCCGTGCAGCCCTTACCGCACC
ATTACGGGAGACTGCAATAACAGGAGGAAGCCTGCGCTGGGCGCCGCCAACAGGGCTCTG
GCGCGCTGGCTGCCCGCGGAGTACGAGGACGGGCTCTCCCTGCCCTTCGGCTGGACGCCG
GGGAAGACGCGCAACGGCTTCCCTCTCCCGCTGGCCCGGGAGGTATCTAACAAGATTGTT
GGCTATCTGAATGAGGAGGGTGTTCTGGACCAAAACAGGTCCCTGCTCTTCATGCAGTGG
GGTCAGATTGTGGATCATGACCTGGACTTTGCCCCTGACACCGAGCTGGGGAGTAGCGAG
TACTCCAAAGCCCAGTGTGATGAGTACTGTATCCAGGGAGACAACTGCTTCCCCATCATG
TTCCCACCCAATGACCCCAAGGCGGGGACTCAAGGGAAATGCATGCCTTTCTTCCGAGCT
GGGTTCGTCTGCCCCACTCCACCCTACAAGTCCCTGGCCCGAGAGCAGATCAACGCTCTG
ACCTCCTTCCTGGATGCCAGCTTTGTGTACAGCTCCGAGCCAAGCCTGGCCAGCCGCCTC
CGCAACCTCAGCAGCCCCCTGGGCCTCATGGCTGTCAACCAGGAGGTCTCAGACCATGGA
CTACCCTACCTGCCCTATGACAGCAAGAAGCCAAGCCCCTGTGAGTTCATCAACACCACT
GCCCGTGTGCCCTGCTTCCTGGCAGGAGATTCTCGAGCCTCAGAGCATATTCTGCTGGCC
ACATCCCACACCCTCTTTCTCCGCGAGCATAACCGGCTGGCCAGAGAACTAAAGAGACTC
AACCCTCAGTGGGATGGAGAGAAGCTCTACCAGGAAGCCCGGAAAATCCTGGGAGCCTTC
GTGCAGATTATCACCTTTAGGGACTACCTACCCATTTTGCTAGGTGACCACATGCAGAAG
TGGATACCCCCATATCAAGGCTACAGTGAATCTGTGGATCCCAGAATTTCCAATGTCTTC
ACCTTCGCCTTCCGCTTTGGCCACTTGGAGGTCCCCTCTAGTATGTTCCGCCTGGATGAG
AATTATCAGCCATGGGGGCCAGAACCAGAACTCCCCCTCCACACCCTCTTCTTCAACACT
TGGAGGATGGTCAAAGATGGTGGAATTGATCCTCTGGTGCGGGGCCTGCTGGCCAAGAAA
TCCAAGCTGATGAAACAGAATAAAATGATGACTGGAGAGCTGCGCAACAAGCTTTTCCAG
CCAACTCACAGGATCCATGGCTTTGACCTGGCTGCCATCAACACACAGCGTTGCCGGGAC
CATGGGCAACCTGGGTACAATTCCTGGAGAGCCTTCTGTGACCTCTCACAGCCGCAGACA
CTAGAGGAGTTGAACACAGTGCTGAAGAGCAAGATGCTGGCCAAGAAGTTACTGGGTCTC
TACGGGACCCCTGACAACATCGACATCTGGATAGGGGCCATTGCTGAGCCGCTGGTGGAA
AGGGGTCGGGTGGGGCCTCTCCTGGCCTGCCTCTTGGGCAAGCAGTTCCAGCAGATCCGT
GATGGAGACAGGTTCTGGTGGGAAAACCCTGGGGTCTTCACGAACGAGCAGAAGGACTCT
CTACAGAAAATGTCCTTCTCACGCCTTGTCTGTGACAACACCCGCATCACCAAGGTCCCA
CGGGACCCATTCTGGGCCAACAGCTACCCCTATGACTTCGTGGATTGCTCAGCCATCGAC
AAGCTGGACCTGTCACCCTGGGCCTCAGTGAAGAATTAG
Enzyme 12 GenBank Gene ID U39573 Link Image
Enzyme 12 GeneCard ID LPO Link Image
Enzyme 12 GenAtlas ID LPO Link Image
Enzyme 12 HGNC ID HGNC:6678 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 17q23.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Kiser C, Caterina CK, Engler JA, Rahemtulla B, Rahemtulla F: Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA. Gene. 1996 Sep 16;173(2):261-4. [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. Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ: Molecular cloning of cDNAs encoding bovine and human lactoperoxidase. DNA Cell Biol. 1990 Sep;9(7):499-509. [PubMed Link Image]
  4. Wijkstrom-Frei C, El-Chemaly S, Ali-Rachedi R, Gerson C, Cobas MA, Forteza R, Salathe M, Conner GE: Lactoperoxidase and human airway host defense. Am J Respir Cell Mol Biol. 2003 Aug;29(2):206-12. Epub 2003 Mar 6. [PubMed Link Image]
  5. Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed Link Image]
  6. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5514
Enzyme 13 Name Myeloperoxidase
Enzyme 13 Synonyms
  1. MPO
  2. 89 kDa myeloperoxidase
  3. 84 kDa myeloperoxidase
  4. Myeloperoxidase light chain
  5. Myeloperoxidase heavy chain
Enzyme 13 Gene Name MPO
Enzyme 13 Protein Sequence >Myeloperoxidase
MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTS
LVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLH
VALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMC
NNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTD
QLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPND
PRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQL
GLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLL
REHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYR
SYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLE
GGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYN
AWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPL
LACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMS
NSYPRDFVNCSTLPALNLASWREAS
Enzyme 13 Number of Residues 745
Enzyme 13 Molecular Weight 83867.7
Enzyme 13 Theoretical pI 9.14
Enzyme 13 GO Classification
Function
  • antioxidant activity
  • binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 13 General Function Involved in peroxidase activity
Enzyme 13 Specific Function Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity
Enzyme 13 Pathways
Enzyme 13 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-48
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 189040 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P05164 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PERM_HUMAN Link Image
Enzyme 13 PDB ID 1MYP Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >2238 bp
ATGGGGGTTCCCTTCTTCTCTTCTCTCAGATGCATGGTGGACTTAGGACCTTGCTGGGCT
GGGGGTCTCACTGCAGAGATGAAGCTGCTTCTGGCCCTAGCAGGGCTCCTGGCCATTCTG
GCCACGCCCCAGCCCTCTGAAGGTGCTGCTCCAGCTGTCCTGGGGGAGGTGGACACCTCG
TTGGTGCTGAGCTCCATGGAGGAGGCCAAGCAGCTGGTGGACAAGGCCTACAAGGAGCGG
CGGGAAAGCATCAAGCAGCGGCTTCGCAGCGGCTCAGCCAGCCCCATGGAACTCCTATCC
TACTTCAAGCAGCCGGTGGCAGCCACCAGGACGGCGGTGAGGGCCGCTGACTACCTGCAC
GTGGCTCTAGACCTGCTGGAGAGGAAGCTGCGGTCCCTGTGGCGAAGGCCATTCAATGTC
ACTGATGTGCTGACGCCCGCCCAGCTGAATGTGTTGTCCAAGTCAAGCGGCTGCGCCTAC
CAGGACGTGGGGGTGACTTGCCCGGAGCAGGACAAATACCGCACCATCACCGGGATGTGC
AACAACAGACGCAGCCCCACGCTGGGGGCCTCCAACCGTGCCTTTGTGCGCTGGCTGCCG
GCGGAGTATGAGGACGGCTTCTCTCTTCCCTACGGCTGGACGCCCGGGGTCAAGCGCAAC
GGCTTCCCGGTGGCTCTGGCTCGCGCGGTCTCCAACGAGATCGTGCGCTTCCCCACTGAT
CAGCTGACTCCGGACCAGGAGCGCTCACTCATGTTCATGCAATGGGGCCAGCTGTTGGAC
CACGACCTCGACTTCACCCCTGAGCCGGCCGCCCGGGCCTCCTTCGTCACTGGCGTCAAC
TGCGAGACCAGCTGCGTTCAGCAGCCGCCCTGCTTCCCGCTCAAGATCCCGCCCAATGAC
CCCCGCATCAAGAACCAAGCCGACTGCATCCCGTTCTTCCGCTCCTGCCCGGCTTGCCCC
GGGAGCAACATCACCATCCGCAACCAGATCAACGCGCTCACTTCCTTCGTGGACGCCAGC
ATGGTGTACGGCAGCGAGGAGCCCCTGGCCAGGAACCTGCGCAACATGTCCAACCAGCTG
GGGCTGCTGGCCGTCAACCAGCGCTTCCAAGACAACGGCCGGGCCCTGCTGCCCTTTGAC
AACCTGCACGATGACCCCTGTCTCCTCACCAACCGCTCAGCGCGCATCCCCTGCTTCCTG
GCAGGGGACACCCGTTCCAGTGAGATGCCCGAGCTCACCTCCATGCACACCCTCTTACTT
CGGGAGCACAACCGGCTGGCCACAGAGCTCAAGAGCCTGAACCCTAGGTGGGATGGGGAG
AGGCTCTACCAGGAAGCCCGGAAGATCGTGGGGGCCATGGTCCAGATCATCACTTACCGG
GACTACCTGCCCCTGGTGCTGGGGCCAACGGCCATGAGGAAGTACCTGCCCACGTACCGT
TCCTACAATGACTCAGTGGACCCACGCATCGCCAACGTCTTCACCAATGCCTTCCGCTAC
GGCCACACCCTCATCCAACCCTTCATGTTCCGCCTGGACAATCGGTACCAGCCCATGGAA
CCCAACCCCCGTGTCCCCCTCAGCAGGGTCTTTTTTGCCTCCTGGAGGGTCGTGCTGGAA
GGTGGCATTGACCCCATCCTCCGGGGCCTCATGGCCACCCCTGCCAAGCTGAATCGTCAG
AACCAAATTGCAGTGGATGAGATCCGGGAGCGATTGTTTGAGCAGGTCATGAGGATTGGG
CTGGACCTGCCTGCTCTGAACATGCAGCGCAGCAGGGACCACGGCCTCCCAGGATACAAT
GCCTGGAGGCGCTTCTGTGGGCTCCCGCAGCCTGAAACTGTGGGCCAGCTGGGCACGGTG
CTGAGGAACCTGAAATTGGCGAGGAAACTGATGGAGCAGTATGGCACGCCCAACAACATC
GACATCTGGATGGGCGGCGTGTCCGAGCCTCTGAAGCGCAAAGGCCGCGTGGGCCCACTC
CTCGCCTGCATCATCGGTACCCAGTTCAGGAAGCTCCGGGATGGTGATCGGTTTTGGTGG
GAGAACGAGGGTGTGTTCAGCATGCAGCAGCGACAGGCCCTGGCCCAGATCTCATTGCCC
CGGATCATCTGCGACAACACAGGCATCACCACCGTGTCTAAGAACAACATCTTCATGTCC
AACTCATATCCCCGGGACTTTGTCAACTGCAGTACACTTCCTGCATTGAACCTGGCTTCC
TGGAGGGAAGCCTCCTAG
Enzyme 13 GenBank Gene ID J02694 Link Image
Enzyme 13 GeneCard ID MPO Link Image
Enzyme 13 GenAtlas ID MPO Link Image
Enzyme 13 HGNC ID HGNC:7218 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 17q23.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Morishita K, Kubota N, Asano S, Kaziro Y, Nagata S: Molecular cloning and characterization of cDNA for human myeloperoxidase. J Biol Chem. 1987 Mar 15;262(8):3844-51. [PubMed Link Image]
  2. Morishita K, Tsuchiya M, Asano S, Kaziro Y, Nagata S: Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor. J Biol Chem. 1987 Nov 5;262(31):15208-13. [PubMed Link Image]
  3. Seto P, Hirayu H, Magnusson RP, Gestautas J, Portmann L, DeGroot LJ, Rapoport B: Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. J Clin Invest. 1987 Oct;80(4):1205-8. [PubMed Link Image]
  4. Johnson KR, Nauseef WM, Care A, Wheelock MJ, Shane S, Hudson S, Koeffler HP, Selsted M, Miller C, Rovera G: Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species. Nucleic Acids Res. 1987 Mar 11;15(5):2013-28. [PubMed Link Image]
  5. Hashinaka K, Nishio C, Hur SJ, Sakiyama F, Tsunasawa S, Yamada M: Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation. Biochemistry. 1988 Aug 9;27(16):5906-14. [PubMed Link Image]
  6. Johnson K, Gemperlein I, Hudson S, Shane S, Rovera G: Complete nucleotide sequence of the human myeloperoxidase gene. Nucleic Acids Res. 1989 Oct 11;17(19):7985-6. [PubMed Link Image]
  7. Hosokawa Y, Kawaguchi R, Hikiji K, Yamada M, Suzuki K, Nakagawa T, Yoshihara T, Yamaguchi K: Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1. Leukemia. 1993 Mar;7(3):441-5. [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. Yamada M, Hur SJ, Toda H: Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures. Biochem Biophys Res Commun. 1990 Jan 30;166(2):852-9. [PubMed Link Image]
  10. Taylor KL, Pohl J, Kinkade JM Jr: Unique autolytic cleavage of human myeloperoxidase. Implications for the involvement of active site MET409. J Biol Chem. 1992 Dec 15;267(35):25282-8. [PubMed Link Image]
  11. Yamada M, Yoshida M, Hashinaka K: Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene. J Biol Chem. 1993 Jun 25;268(18):13479-85. [PubMed Link Image]
  12. Yamada M, Hur SJ, Hashinaka K, Tsuneoka K, Saeki T, Nishio C, Sakiyama F, Tsunasawa S: Isolation and characterization of a cDNA coding for human myeloperoxidase. Arch Biochem Biophys. 1987 May 15;255(1):147-55. [PubMed Link Image]
  13. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  14. Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed Link Image]
  15. 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]
  16. Fiedler TJ, Davey CA, Fenna RE: X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem. 2000 Apr 21;275(16):11964-71. [PubMed Link Image]
  17. Fenna R, Zeng J, Davey C: Structure of the green heme in myeloperoxidase. Arch Biochem Biophys. 1995 Jan 10;316(1):653-6. [PubMed Link Image]
  18. Blair-Johnson M, Fiedler T, Fenna R: Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution. Biochemistry. 2001 Nov 20;40(46):13990-7. [PubMed Link Image]
  19. Kizaki M, Miller CW, Selsted ME, Koeffler HP: Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency. Blood. 1994 Apr 1;83(7):1935-40. [PubMed Link Image]
  20. Nauseef WM, Brigham S, Cogley M: Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan. J Biol Chem. 1994 Jan 14;269(2):1212-6. [PubMed Link Image]
  21. Nauseef WM, Cogley M, McCormick S: Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase. J Biol Chem. 1996 Apr 19;271(16):9546-9. [PubMed Link Image]
  22. DeLeo FR, Goedken M, McCormick SJ, Nauseef WM: A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J Clin Invest. 1998 Jun 15;101(12):2900-9. [PubMed Link Image]
  23. Romano M, Dri P, Dadalt L, Patriarca P, Baralle FE: Biochemical and molecular characterization of hereditary myeloperoxidase deficiency. Blood. 1997 Nov 15;90(10):4126-34. [PubMed Link Image]
  24. 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5517
Enzyme 14 Name Eosinophil peroxidase
Enzyme 14 Synonyms
  1. EPO
  2. Eosinophil peroxidase light chain
  3. Eosinophil peroxidase heavy chain
Enzyme 14 Gene Name EPX
Enzyme 14 Protein Sequence >Eosinophil peroxidase
MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQ
RLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTE
PQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLS
LPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPE
SPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRN
QINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCL
LTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARK
IMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPF
MFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDEL
RDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLAR
KFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTK
RQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT
Enzyme 14 Number of Residues 715
Enzyme 14 Molecular Weight 81039.5
Enzyme 14 Theoretical pI 10.81
Enzyme 14 GO Classification
Function
  • antioxidant activity
  • binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 14 General Function Involved in peroxidase activity
Enzyme 14 Specific Function Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis
Enzyme 14 Pathways
Enzyme 14 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-17
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 66268791 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P11678 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PERE_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2148 bp
ATGCATCTGCTCCCAGCCCTGGCAGGGGTCCTGGCCACACTCGTCCTCGCCCAGCCCTGT
GAGGGCACTGACCCAGCCTCCCCTGGGGCAGTGGAGACCTCGGTCCTGCGAGACTGCATA
GCAGAGGCCAAGTTGCTGGTGGATGCTGCCTACAATTGGACCCAGAAGAGCATCAAGCAG
CGGCTTCGCAGCGGTTCAGCCAGCCCCATGGACCTCCTGTCCTACTTCAAACAACCGGTA
GCAGCCACCAGGACAGTTGTTCGGGCCGCAGATTATATGCATGTGGCTTTGGGGCTGCTT
GAAGAGAAGTTACAACCCCAGCGGTCCGGACCCTTCAATGTCACTGATGTGCTAACAGAA
CCACAGCTGCGGCTGCTGTCCCAGGCCAGTGGCTGTGCTCTCCGGGACCAGGCCGAGCGC
TGCAGCGACAAGTACCGCACCATCACTGGACGGTGCAACAACAAGAGGAGACCCTTGCTA
GGGGCCTCCAACCAGGCTCTGGCTCGCTGGCTGCCCGCCGAGTATGAGGATGGGCTGTCG
CTCCCCTTCGGCTGGACCCCCAGCAGGAGGCGCAATGGCTTCCTTCTCCCTCTTGTCCGG
GCTGTCTCCAACCAGATTGTGCGCTTCCCCAATGAGAGACTGACCTCCGACCGTGGCCGA
GCCCTCATGTTCATGCAGTGGGGCCAGTTCATTGACCATGACCTGGACTTCTCCCCGGAG
TCCCCGGCCAGAGTGGCCTTCACTGCAGGCGTTGACTGTGAGAGGACCTGCGCCCAGCTG
CCCCCCTGCTTTCCCATCAAGATCCCACCCAATGACCCCCGCATCAAGAACCAGCGTGAC
TGCATCCCTTTCTTCCGCTCGGCACCCTCATGCCCCCAAAACAAGAACAGAGTCCGCAAC
CAGATCAACGCGCTCACCTCCTTTGTGGACGCCAGCATGGTGTATGGCAGTGAGGTCTCC
CTCTCGCTGCGGCTCCGCAACCGGACCAACTACCTGGGGCTGCTGGCCATCAACCAGCGC
TTTCAAGACAACGGCCGGGCCCTGCTGCCCTTCGACAACCTGCACGATGACCCCTGTCTC
CTCACCAACCGCTCGGCGCGCATCCCCTGCTTCCTGGCAGGTGACACCCGATCAACGGAA
ACCCCCAAACTGGCAGCCATGCACACCCTCTTTATGCGAGAGCACAACCGGCTGGCCACC
GAGCTGAGACGCCTGAATCCCCGGTGGAATGGAGACAAACTGTACAATGAGGCTCGGAAG
ATCATGGGGGCCATGGTCCAGATCATCACCTACCGAGACTTTCTGCCCCTGGTTCTGGGC
AAGGCCCGGGCCAGGAGAACCCTGGGGCACTACAGGGGGTACTGCTCCAATGTGGACCCA
CGGGTGGCCAATGTCTTCACCCTGGCCTTCCGCTTTGGCCACACAATGCTCCAGCCCTTC
ATGTTCCGCTTGGACAGTCAGTACCGGGCCTCCGCACCCAACTCGCATGTCCCACTTAGC
TCTGCCTTCTTTGCCAGCTGGCGGATCGTGTATGAAGGGGGCATCGACCCCATCCTCCGG
GGCCTCATGGCCACCCCTGCCAAGCTGAACCGTCAGGATGCCATGTTAGTGGATGAGCTC
CGGGACCGGCTGTTTCGGCAAGTGAGGAGGATTGGGCTGGACCTGGCAGCTCTCAACATG
CAACGAAGCCGGGACCACGGCCTTCCAGGGTACAATGCTTGGAGGCGCTTCTGTGGGCTC
TCCCAGCCCCGGAATTTGGCACAGCTTAGCCGGGTGCTGAAAAACCAGGACTTGGCAAGG
AAGTTCCTGAATTTGTATGGAACACCTGACAACATTGACATCTGGATTGGGGCCATCGCT
GAGCCTCTTTTGCCGGGGGCTCGAGTGGGGCCTCTTCTGGCTTGTCTGTTCGAGAACCAG
TTCAGAAGAGCCCGAGACGGAGACAGGTTCTGGTGGCAGAAACGAGGTGTTTTCACCAAA
AGACAGCGCAAGGCCCTGAGCAGAATTTCCTTGTCTCGAATTATATGTGACAATACCGGT
ATCACCACGGTTTCAAGGGACATCTTCAGAGCCAACATCTACCCTCGGGGCTTTGTGAAC
TGCAGCCGTATCCCCAGGTTGAACCTATCAGCCTGGCGAGGGACATGA
Enzyme 14 GenBank Gene ID DQ054598 Link Image
Enzyme 14 GeneCard ID EPX Link Image
Enzyme 14 GenAtlas ID EPX Link Image
Enzyme 14 HGNC ID HGNC:3423 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 17q23.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Sakamaki K, Tomonaga M, Tsukui K, Nagata S: Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J Biol Chem. 1989 Oct 5;264(28):16828-36. [PubMed Link Image]
  2. Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ: Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family. J Exp Med. 1989 May 1;169(5):1757-69. [PubMed Link Image]
  3. Oxvig C, Thomsen AR, Overgaard MT, Sorensen ES, Hojrup P, Bjerrum MJ, Gleich GJ, Sottrup-Jensen L: Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo. J Biol Chem. 1999 Jun 11;274(24):16953-8. [PubMed Link Image]
  4. Borelli V, Vita F, Shankar S, Soranzo MR, Banfi E, Scialino G, Brochetta C, Zabucchi G: Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis. Infect Immun. 2003 Feb;71(2):605-13. [PubMed Link Image]
  5. Ulrich M, Petre A, Youhnovski N, Promm F, Schirle M, Schumm M, Pero RS, Doyle A, Checkel J, Kita H, Thiyagarajan N, Acharya KR, Schmid-Grendelmeier P, Simon HU, Schwarz H, Tsutsui M, Shimokawa H, Bellon G, Lee JJ, Przybylski M, Doring G: Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase. J Biol Chem. 2008 Oct 17;283(42):28629-40. Epub 2008 Aug 11. [PubMed Link Image]
  6. Romano M, Patriarca P, Melo C, Baralle FE, Dri P: Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12496-500. [PubMed Link Image]
  7. Nakamura H, Miyagawa K, Ogino K, Endo T, Imai T, Ozasa K, Motohashi Y, Matsuzaki I, Sasahara S, Hatta K, Eboshida A: High contribution contrast between the genes of eosinophil peroxidase and IL-4 receptor alpha-chain in Japanese cedar pollinosis. J Allergy Clin Immunol. 2003 Dec;112(6):1127-31. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5627
Enzyme 15 Name Amiloride-sensitive amine oxidase [copper-containing]
Enzyme 15 Synonyms
  1. DAO
  2. Diamine oxidase
  3. Amiloride-binding protein
  4. ABP
  5. Histaminase
  6. Kidney amine oxidase
  7. KAO
Enzyme 15 Gene Name ABP1
Enzyme 15 Protein Sequence >Amiloride-sensitive amine oxidase [copper-containing]
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
Enzyme 15 Number of Residues 751
Enzyme 15 Molecular Weight 85377.1
Enzyme 15 Theoretical pI 7.10
Enzyme 15 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
Enzyme 15 General Function Involved in copper ion binding
Enzyme 15 Specific Function Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function
Enzyme 15 Pathways
Enzyme 15 Reactions
  • histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2 [RN:R02150]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-19
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 73486661 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P19801 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name ABP1_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >2256 bp
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCTCGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGCCC
CTCTTCTCCTCCCACAAGCCCCGCGGGGACTTCCCCAGCCCCATCCATGTGAGCGGCCCC
CGCTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGC
GGCTGGAGCTTTGCCTTCCGGCTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCAC
TTCGGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGA
GGACACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGC
GTCACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACT
TTCCACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAA
ATGCCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAAC
TTCTATGCGGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAAT
TATGATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCAT
GCCACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGGCTGCGCCACGGCACTCGC
CTGCACACCCACCTGATTGGCAACATACACACTCACTTGGTGCACTACCGCGTAGACCTG
GATGTGGCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACC
AACCCCTGGAGCCCAAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCC
TGGGAGCGCCAGGCGGCCTTCCGCTTCAAAAGGAAGCTGCCTAAGTACCTGCTCTTTACC
AGCCCCCAGGAGAACCCCTGGGGCCACAAGCGCACGTACCGCCTGCAGATCCACTCCATG
GCCGACCAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTAC
CCCCTGGCAGTGACCAAGTACCGGGAGTCGGAGCTGTGCAGCAGCAGCATCTACCACCAG
AACGACCCCTGGCACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATT
GAAAATGAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAG
GACATTCCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAAC
TTCTTCCCAGAGGACCCCTCCCTGGCATCCAGAGACACTGTGATCGTGTGGCCTCGGGAC
AACGGCCCCAACTACGTCCAGCGCTGGATCCCTGAGGACAGGGACTGCTCGATGCCTCCC
CCTTTTAGCTACAATGGGACCTATAGACCTGTGTGA
Enzyme 15 GenBank Gene ID NM_001091.2 Link Image
Enzyme 15 GeneCard ID ABP1 Link Image
Enzyme 15 GenAtlas ID ABP1 Link Image
Enzyme 15 HGNC ID HGNC:80 Link Image
Enzyme 15 Chromosome Location 7
Enzyme 15 Locus 7q34-q36
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Barbry P, Champe M, Chassande O, Munemitsu S, Champigny G, Lingueglia E, Maes P, Frelin C, Tartar A, Ullrich A, et al.: Human kidney amiloride-binding protein: cDNA structure and functional expression. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7347-51. [PubMed Link Image]
  2. Chassande O, Renard S, Barbry P, Lazdunski M: The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J Biol Chem. 1994 May 20;269(20):14484-9. [PubMed Link Image]
  3. Zhang X, Kim J, McIntire WS: cDNA sequences of variant forms of human placenta diamine oxidase. Biochem Genet. 1995 Aug;33(7-8):261-8. [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. Novotny WF, Chassande O, Baker M, Lazdunski M, Barbry P: Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues. J Biol Chem. 1994 Apr 1;269(13):9921-5. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5630
Enzyme 16 Name Membrane primary amine oxidase
Enzyme 16 Synonyms
  1. Copper amine oxidase
  2. HPAO
  3. Semicarbazide-sensitive amine oxidase
  4. SSAO
  5. Vascular adhesion protein 1
  6. VAP-1
Enzyme 16 Gene Name AOC3
Enzyme 16 Protein Sequence >Membrane primary amine oxidase
MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
Enzyme 16 Number of Residues 763
Enzyme 16 Molecular Weight 84621.3
Enzyme 16 Theoretical pI 6.51
Enzyme 16 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
Enzyme 16 General Function Involved in copper ion binding
Enzyme 16 Specific Function Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin- independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis
Enzyme 16 Pathways
Enzyme 16 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 6-26
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID Q16853 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name AOC3_HUMAN Link Image
Enzyme 16 PDB ID 1PU4 Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2292 bp
ATGAACCAGAAGACAATCCTCGTGCTCCTCATTCTGGCCGTCATCACCATCTTTGCCTTG
GTTTGTGTCCTGCTGGTGGGCAGGGGTGGAGATGGGGGTGAACCCAGCCAGCTTCCCCAT
TGCCCCTCTGTATCTCCCAGTGCCCAGCCTTGGACACACCCTGGCCAGAGCCAGCTGTTT
GCAGACCTGAGCCGAGAGGAGCTGACGGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGG
CCAGGGCTGGTGGATGCAGCCCAGGCCCGGCCCTCGGACAACTGTGTCTTCTCAGTGGAG
TTGCAGCTGCCTCCCAAGGCTGCAGCCCTGGCTCACTTGGACAGGGGGAGCCCCCCACCT
GCCCGGGAGGCACTGGCCATCGTCTTCTTTGGCAGGCAACCCCAGCCCAACGTGAGTGAG
CTGGTGGTGGGGCCACTGCCTCACCCCTCCTACATGCGGGACGTGACTGTGGAGCGTCAT
GGAGGCCCCCTGCCCTATCACCGACGCCCCGTGCTGTTCCAAGAGTACCTGGACATAGAC
CAGATGATCTTCAACAGAGAGCTGCCCCAGGCTTCTGGGCTTCTCCACCACTGTTGCTTC
TACAAGCACCGGGGACGGAACCTGGTGACAATGACCACGGCTCCCCGTGGTCTGCAATCA
GGGGACCGGGCCACCTGGTTTGGCCTCTACTACAACATCTCGGGCGCTGGGTTCTTCCTG
CACCACGTGGGCTTGGAGCTGCTAGTGAACCACAAGGCCCTTGACCCTGCCCGCTGGACT
ATCCAGAAGGTGTTCTATCAAGGCCGCTACTACGACAGCCTGGCCCAGCTGGAGGCCCAG
TTTGAGGCCGGCCTGGTGAATGTGGTGCTGATCCCAGACAATGGCACAGGTGGGTCCTGG
TCCCTGAAGTCCCCTGTGCCCCCGGGTCCAGCTCCCCCTCTACAGTTCTATCCCCAAGGC
CCCCGCTTCAGTGTCCAGGGAAGTCGAGTGGCCTCCTCACTGTGGACTTTCTCCTTTGGC
CTCGGAGCATTCAGTGGCCCAAGGATCTTTGACGTTCGCTTCCAAGGAGAAAGACTAGTT
TATGAGATAAGCCTCCAAGAGGCCTTGGCCATCTATGGTGGAAATTCCCCAGCAGCAATG
ACGACCCGCTATGTGGATGGAGGCTTTGGCATGGGCAAGTACACCACGCCCCTGACCCGT
GGGGTGGACTGCCCCTACTTGGCCACCTACGTGGACTGGCACTTCCTTTTGGAGTCCCAG
GCCCCCAAGACAATACGTGATGCCTTTTGTGTGTTTGAACAGAACCAGGGCCTCCCCCTG
CGGCGACACCACTCAGATCTCTACTCGCACTACTTTGGGGGTCTTGCGGAAACGGTGCTG
GTCGTCAGATCTATGTCCACCTTGCTCAACTATGACTATGTGTGGGATACGGTCTTCCAC
CCCAGTGGGGCCATAGAAATACGATTCTATGCCACGGGCTACATCAGCTCGGCATTCCTC
TTTGGTGCTACTGGGAAGTACGGGAACCAAGTGTCAGAGCACACCCTGGGCACGGTCCAC
ACCCACAGCGCCCACTTCAAGGTGGATCTGGATGTAGCAGGACTGGAGAACTGGGTCTGG
GCCGAGGATATGGTCTTTGTCCCCATGGCTGTGCCCTGGAGCCCTGAGCACCAGCTGCAG
AGGCTGCAGGTGACCCGGAAGCTGCTGGAGATGGAGGAGCAGGCCGCCTTCCTCGTGGGA
AGCGCCACCCCTCGCTACCTGTACCTGGCCAGCAACCACAGCAACAAGTGGGGTCACCCC
CGGGGCTACCGCATCCAGATGCTCAGCTTTGCTGGAGAGCCGCTGCCCCAAAACAGCTCC
ATGGCGAGAGGCTTCAGCTGGGAGAGGTACCAGCTGGCTGTGACCCAGCGGAAGGAGGAG
GAGCCCAGTAGCAGCAGCGTTTTCAATCAGAATGACCCTTGGGCCCCCACTGTGGATTTC
AGTGACTTCATCAACAATGAGACCATTGCTGGAAAGGATTTGGTGGCCTGGGTGACAGCT
GGTTTTCTGCATATCCCACATGCAGAGGACATTCCTAACACAGTGACTGTGGGGAACGGC
GTGGGCTTCTTCCTCCGACCCTATAACTTCTTTGACGAAGACCCCTCCTTCTACTCTGCC
GACTCCATCTACTTCCGAGGGGACCAGGATGCTGGGGCCTGCGAGGTCAACCCCCTAGCT
TGCCTGCCCCAGGCTGCTGCCTGTGCCCCCGACCTCCCTGCCTTCTCCCACGGGGGCTTC
TCTCACAACTAG
Enzyme 16 GenBank Gene ID U39447 Link Image
Enzyme 16 GeneCard ID AOC3 Link Image
Enzyme 16 GenAtlas ID AOC3 Link Image
Enzyme 16 HGNC ID HGNC:550 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 17q21
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Zhang X, McIntire WS: Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta. Gene. 1996 Nov 14;179(2):279-86. [PubMed Link Image]
  2. Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S: Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. [PubMed Link Image]
  3. Zhang Q, Mashima Y, Noda S, Imamura Y, Kudoh J, Shimizu N, Nishiyama T, Umeda S, Oguchi Y, Tanaka Y, Iwata T: Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina. Gene. 2003 Oct 30;318:45-53. [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. 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]
  7. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  8. Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed Link Image]
  9. Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed Link Image]
  10. 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]
  11. Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA: Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications. Protein Sci. 2005 Aug;14(8):1964-74. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5631
Enzyme 17 Name Retina-specific copper amine oxidase
Enzyme 17 Synonyms
  1. RAO
  2. Amine oxidase [copper-containing]
  3. Semicarbazide-sensitive amine oxidase
  4. SSAO
Enzyme 17 Gene Name AOC2
Enzyme 17 Protein Sequence >Retina-specific copper amine oxidase
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
Enzyme 17 Number of Residues 756
Enzyme 17 Molecular Weight 83672.7
Enzyme 17 Theoretical pI 7.03
Enzyme 17 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
Enzyme 17 General Function Involved in copper ion binding
Enzyme 17 Specific Function Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina
Enzyme 17 Pathways
Enzyme 17 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-32
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 3510335 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O75106 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name AOC2_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2271 bp
ATGCATCTCAAGATAGTCCTGGCGTTCCTGGCACTGTCCCTCATTACCATCTTTGCCCTG
GCCTATGTTTTGCTGACCAGCCCAGGTGGTTCCAGCCAGCCTCCCCACTGCCCCTCTGTA
TCCCATAGGGCCCAGCCCTGGCCACACCCTGGCCAGAGCCAGCTGTTTGCAGACCTGAGC
CGAGAGGAGTTGACAGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGGCCAGGGCTGGTG
GACGCAGCCCAGGCTCAGCCCTCGGACAACTGCATCTTCTCAGTGGAGCTGCAGCTGCCC
CCCAAGGCTGCAGCCCTGGCCCACCTGGACAGGGGGAGCCCCCCACCTGCCCGGGAGGCA
CTGGCCATCGTCCTCTTTGGTGGACAACCCCAACCCAATGTGAGTGAGCTGGTGGTGGGG
CCGCTGCCTCACCCCTCGTACATGCGGGATGTGACTGTGGAGCGTCACGGCGGGCCCCTG
CCCTATCACCGTCGCCCGGTGCTGAGAGCTGAGTTTACACAGATGTGGAGGCATCTGAAA
GATGTGGAGCTACCCAAGGCACCCATCTTCCTGTCGTCCACCTTCAACTACAATGGCTCT
ACCCTGGCAGCTGTGCATGCCACCCCTCGGGGCTTGCGCTCAAGGGAACGAACTACCTGG
ATGGCCCTCTACCATAACATCTCAGGGGTTGGTCTTTTCCTTCACCCCGTGGGGCTGGAG
CTACTACTGGACCACAGGGCCCTGGACCCTGCCCACTGGACTGTCCAGCAGGTCTTCTAC
CTTGGGCACTACTATGCAGACTTGGGCCAGTTGGAACGGGAGTTTAAGTCTGGCCGGTTG
GAAGTGGTTAGAGTCCCTCTACCTCCACCAAATGGAGCTTCATCCCTGAGGTCTCGGAAC
TCTCCAGGTCCTCTTCCCCCTCTTCAGTTCTCGCCCCAGGGTTCCCAGTACAGTGTGCAA
GGAAACCTGGTGGTATCCTCCCTCTGGTCATTTACCTTTGGCCATGGGGTGTTCAGCGGC
CTGAGGATTTTTGATGTTCGGTTCCAGGGTGAGCGAATAGCCTATGAAGTCAGTGTCCAG
GAGTGTGTATCTATCTATGGTGCCGATTCACCCAAGACGATGCTGACTCGCTATTTGGAT
AGCAGCTTTGGACTCGGCCGTAACAGCCGAGGCTTGGTGCGGGGAGTGGACTGCCCCTAT
CAAGCCACGATGGTGGACATCCATATATTAGTGGGCAAAGGGGCAGTCCAGCTGCTTCCA
GGGGCTGTGTGTGTATTTGAGGAAGCCCAGGGACTGCCCCTTCGAAGGCACCACAATTAC
CTTCAAAATCATTTCTATGGTGGTTTGGCCAGCTCAGCCCTTGTGGTCAGGTCTGTGTCA
TCTGTGGGCAACTATGACTACATTTGGGACTTTGTGTTGTACCCAAATGGGGCACTTGAA
GGGCGGGTCCATGCCACGGGTTATATCAACACAGCTTTCCTGAAAGGGGGAGAGGAGGGC
CTCCTCTTTGGGAACCGTGTGGGGGAAAGAGTGCTGGGAACGGTGCACACACATGCCTTC
CACTTCAAGCTGGACCTGGATGTGGCAGGGCTGAAAAACTGGGTGGTAGCTGAAGACGTG
GTGTTTAAACCTGTGGCTGCCCCCTGGAACCCGGAGCACTGGCTACAGCGCCCACAGCTG
ACTCGGCAGGTCCTGGGAAAGGAGGACCTGACAGCTTTTTCCTTGGGAAGCCCCCTACCC
CGCTACCTCTACCTGGCTAGCAACCAGACTAATGCGTGGGGTCACCAGCGCGGGTACCGA
ATCCAGATCCACAGCCCCCTTGGCATACAAATACCCCTGGAGAGTGACATGGAGAGGGCC
CTCAGCTGGGGGAGATACCAGCTTGTGGTGACCCAGAGAAAGGAGGAGGAGTCACAGAGC
AGTAGCATCTATCACCAGAATGACATCTGGACACCCACAGTTACCTTTGCTGACTTCATC
AACAATGAAACCCTCTTAGGAGAGGATCTGGTGGCTTGGGTCACAGCCAGCTTCCTGCAC
ATTCCCCATGCCGAGGACATCCCAAACACAGTGACTCTGGGGAACAGAGTTGGCTTCTTG
CTCCGACCCTATAACTTCTTTGATGAGGACCCCTCCATCTTCTCCCCTGGCAGTGTGTAC
TTTGAGAAGGGCCAGGATGCTGGGCTCTGCAGCATCAATCCTGTGGCCTGCCTCCCCGAC
CTGGCAGCCTGTGTCCCGGACTTACCCCCTTTCTCTTACCACGGCTTCTAG
Enzyme 17 GenBank Gene ID AB012943 Link Image
Enzyme 17 GeneCard ID AOC2 Link Image
Enzyme 17 GenAtlas ID AOC2 Link Image
Enzyme 17 HGNC ID HGNC:549 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 17q21
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Imamura Y, Kubota R, Wang Y, Asakawa S, Kudoh J, Mashima Y, Oguchi Y, Shimizu N: Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 1997 Mar 1;40(2):277-83. [PubMed Link Image]
  2. Imamura Y, Noda S, Mashima Y, Kudoh J, Oguchi Y, Shimizu N: Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina. Genomics. 1998 Jul 15;51(2):293-8. [PubMed Link Image]
  3. 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]
  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. Heniquez A, Meissonnier G, Visentin V, Prevot D, Carpene C: High expression of semicarbazide-sensitive amine oxidase genes AOC2 and AOC3, but not the diamine oxidase gene AOC1 in human adipocytes. Inflamm Res. 2003 Apr;52 Suppl 1:S74-5. [PubMed Link Image]
  6. Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed Link Image]
  7. Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5947
Enzyme 18 Name Pyridoxine-5'-phosphate oxidase
Enzyme 18 Synonyms
  1. Pyridoxamine-phosphate oxidase
Enzyme 18 Gene Name PNPO
Enzyme 18 Protein Sequence >Pyridoxine-5'-phosphate oxidase
MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVK
QFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKE
LDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPD
REYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGD
SPLGPMTHRGEEDWLYERLAP
Enzyme 18 Number of Residues 261
Enzyme 18 Molecular Weight 29987.8
Enzyme 18 Theoretical pI 7.09
Enzyme 18 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • pyridoxamine-phosphate oxidase activity
Process
  • metabolic process
  • oxidation reduction
  • pyridoxine biosynthetic process
  • pyridoxine metabolic process
  • small molecule metabolic process
  • vitamin B6 metabolic process
  • vitamin metabolic process
  • water-soluble vitamin metabolic process
Component
Enzyme 18 General Function Involved in pyridoxamine-phosphate oxidase activity
Enzyme 18 Specific Function Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)
Enzyme 18 Pathways
Enzyme 18 Reactions
  • (1) pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2 [RN:R00277]
  • (2) pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2 [RN:R00278]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID Q9NVS9 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PNPO_HUMAN Link Image
Enzyme 18 PDB ID 1NRG Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >786 bp
ATGACGTGCTGGCTGCGGGGCGTCACGGCGACGTTCGGGCGACCTGCCGAGTGGCCAGGC
TACCTCAGTCACCTGTGTGGTCGCAGTGCTGCCATGGACCTGGGACCCATGCGCAAGAGT
TACCGCGGGGACCGAGAGGCATTTGAGGAGACTCATCTGACCTCCCTTGACCCAGTGAAA
CAGTTTGCTGCCTGGTTTGAGGAGGCTGTTCAGTGTCCTGACATAGGGGAAGCCAATGCC
ATGTGTCTGGCTACCTGCACCAGAGATGGAAAACCCTCTGCTCGCATGTTGCTGCTGAAG
GGCTTCGGGAAAGATGGCTTCCGCTTCTTCACTAACTTCGAGAGTCGAAAAGGAAAAGAG
CTGGACTCTAATCCCTTTGCTTCCCTTGTCTTCTACTGGGAGCCACTTAACCGTCAGGTG
CGTGTGGAAGGCCCTGTGAAGAAACTGCCTGAGGAGGAGGCTGAGTGCTACTTCCACTCC
CGCCCCAAGAGCAGCCAGATTGGGGCTGTGGTCAGCCACCAGAGTTCTGTGATCCCTGAT
CGGGAGTATCTGAGAAAGAAAAATGAGGAACTGGAACAGCTCTACCAGGATCAAGAGGTG
CCCAAGCCAAAATCCTGGGGTGGCTATGTCCTGTACCCTCAGGTGATGGAGTTCTGGCAA
GGTCAAACCAACCGCCTGCATGACCGGATAGTCTTTCGGCGGGGCCTACCCACAGGAGAT
TCCCCTTTGGGGCCCATGACCCACCGCGGGGAGGAAGACTGGCTCTATGAGAGACTTGCA
CCTTAA
Enzyme 18 GenBank Gene ID AF468030 Link Image
Enzyme 18 GeneCard ID PNPO Link Image
Enzyme 18 GenAtlas ID PNPO Link Image
Enzyme 18 HGNC ID HGNC:30260 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 17q21.32
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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. 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]
  4. Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK: Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. Protein Sci. 2003 Jul;12(7):1455-63. [PubMed Link Image]
  5. Mills PB, Surtees RA, Champion MP, Beesley CE, Dalton N, Scambler PJ, Heales SJ, Briddon A, Scheimberg I, Hoffmann GF, Zschocke J, Clayton PT: Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase. Hum Mol Genet. 2005 Apr 15;14(8):1077-86. Epub 2005 Mar 16. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5969
Enzyme 19 Name Protein-lysine 6-oxidase
Enzyme 19 Synonyms
  1. Lysyl oxidase
Enzyme 19 Gene Name LOX
Enzyme 19 Protein Sequence >Protein-lysine 6-oxidase
MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSL
GSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPT
ARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDD
NPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAA
EENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDE
FSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADID
CQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY
Enzyme 19 Number of Residues 417
Enzyme 19 Molecular Weight 46943.7
Enzyme 19 Theoretical pI 8.14
Enzyme 19 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 19 General Function Involved in copper ion binding
Enzyme 19 Specific Function Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of extracellular matrix proteins, may have a direct role in tumor suppression
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2 [RN:R04239]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-21
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 4104739 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P28300 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name LYOX_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1254 bp
ATGCGCTTCGCCTGGACCGTGCTCCTGCTCGGGCCTTTGCAGCTCTGCGCGCTAGTGCAC
TGCGCCCCTCCCGCCGCCGGCCAACAGCAGCCCCCGCGCGAGCCGCCGGCGGCTCCGGGC
GCCTGGCGCCAGCAGATCCAATGGGAGAACAACGGGCAGGTGTTCAGCTTGCTGAGCCTG
GGCTCACAGTACCAGCCTCAGCGCCGCCGGGACCCGGGCGCCGCCGTCCCTGGTGCAGCC
AACGCCTCCGCCCAGCAGCCCCGCACTCCGATCCTGCTGATCCGCGACAACCGCACCGCC
GCGGCGCGAACGCGGACGGCCGGCTCATCTGGAGTCACCGCTGGCCGCCCCAGGCCCACC
GCCCGTCACTGGTTCCAAGCTGGCTACTCGACATCTAGAGCCCGCGAAGCTGGCGCCTCG
CGCGCGGAGAACCAGACAGCGCCGGGAGAAGTTCCTGCGCTCAGTAACCTGCGGCCGCCC
AGCCGCGTGGACGGCATGGTGGGCGACGACCCTTACAACCCCTACAAGTACTCTGACGAC
AACCCTTATTACAACTACTACGATACTTATGAAAGGCCCAGACCTGGGGGCAGGTACCGG
CCCGGATACGGCACTGGCTACTTCCAGTACGGTCTCCCAGACCTGGTGGCCGACCCCTAC
TACATCCAGGCGTCCACGTACGTGCAGAAGATGTCCATGTACAACCTGAGATGCGCGGCG
GAGGAAAACTGTCTGGCCAGTACAGCATACAGGGCAGATGTCAGAGATTATGATCACAGG
GTGCTGCTCAGATTTCCCCAAAGAGTGAAAAACCAAGGGACATCAGATTTCTTACCCAGC
CGACCAAGATATTCCTGGGAATGGCACAGTTGTCATCAACATTACCACAGTATGGATGAG
TTTAGCCACTATGACCTGCTTGATGCCAACACCCAGAGGAGAGTGGCTGAAGGCCACAAA
GCAAGTTTCTGTCTTGAAGACACATCCTGTGACTATGGCTACCACAGGCGATTTGCATGT
ACTGCACACACACAGGGATTGAGTCCTGGCTGTTATGATACCTATGGTGCAGACATAGAC
TGCCAGTGGATTGATATTACAGATGTAAAACCTGGAAACTATATCCTAAAGGTCAGTGTA
AACCCCAGCTACCTGGTTCCTGAATCTGACTATACCAACAATGTTGTGCGCTGTGACATT
CGCTACACAGGACATCATGCGTATGCCTCAGGCTGCACAATTTCACCGTATTAG
Enzyme 19 GenBank Gene ID AF039291 Link Image
Enzyme 19 GeneCard ID LOX Link Image
Enzyme 19 GenAtlas ID LOX Link Image
Enzyme 19 HGNC ID HGNC:6664 Link Image
Enzyme 19 Chromosome Location 5
Enzyme 19 Locus 5q23.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Hamalainen ER, Jones TA, Sheer D, Taskinen K, Pihlajaniemi T, Kivirikko KI: Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2. Genomics. 1991 Nov;11(3):508-16. [PubMed Link Image]
  2. Mariani TJ, Trackman PC, Kagan HM, Eddy RL, Shows TB, Boyd CD, Deak SB: The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene). Matrix. 1992 Jun;12(3):242-8. [PubMed Link Image]
  3. Kim Y, Boyd CD, Csiszar K: A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase. J Biol Chem. 1995 Mar 31;270(13):7176-82. [PubMed Link Image]
  4. Contente S, Kenyon K, Sriraman P, Subramanyan S, Friedman RM: Epigenetic inhibition of lysyl oxidase transcription after transformation by ras oncogene. Mol Cell Biochem. 1999 Apr;194(1-2):79-91. [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. 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. Hamalainen ER, Kemppainen R, Pihlajaniemi T, Kivirikko KI: Structure of the human lysyl oxidase gene. Genomics. 1993 Sep;17(3):544-8. [PubMed Link Image]
  8. Svinarich DM, Twomey TA, Macauley SP, Krebs CJ, Yang TP, Krawetz SA: Characterization of the human lysyl oxidase gene locus. J Biol Chem. 1992 Jul 15;267(20):14382-7. [PubMed Link Image]
  9. Khakoo A, Thomas R, Trompeter R, Duffy P, Price R, Pope FM: Congenital cutis laxa and lysyl oxidase deficiency. Clin Genet. 1997 Feb;51(2):109-14. [PubMed Link Image]
  10. Csiszar K, Mariani TJ, Gosin JS, Deak SB, Boyd CD: A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene. Genomics. 1993 May;16(2):401-6. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6068
Enzyme 20 Name Hydroxyacid oxidase 2
Enzyme 20 Synonyms
  1. HAOX2
  2. (S)-2-hydroxy-acid oxidase, peroxisomal
  3. Cell growth-inhibiting gene 16 protein
  4. Long chain alpha-hydroxy acid oxidase
  5. Long-chain L-2-hydroxy acid oxidase
Enzyme 20 Gene Name HAO2
Enzyme 20 Protein Sequence >Hydroxyacid oxidase 2
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDT
RTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAA
PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLT
DLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQG
IIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG
RPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
Enzyme 20 Number of Residues 351
Enzyme 20 Molecular Weight 38838.4
Enzyme 20 Theoretical pI 7.69
Enzyme 20 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 20 General Function Involved in FMN binding
Enzyme 20 Specific Function Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids
Enzyme 20 Pathways
  • Glyoxylate and Dicarboxylate Metabolism (map00630 Link Image)
Enzyme 20 Reactions
  • an (S)-2-hydroxy acid + O2 = a 2-oxo acid + H2O2 [RN:R01341]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 6478782 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9NYQ3 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name HAOX2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1056 bp
ATGTCCTTGGTGTGTCTGACAGACTTTCAGGCCCATGCGCGAGAGCAGCTGTCTAAGTCA
ACTCGGGATTTTATTGAAGGTGGAGCAGATGACAGCATCACGCGGGATGACAACATTGCA
GCATTTAAAAGAATTCGCCTCCGTCCGCGGTACCTGAGAGATGTGTCTGAGGTGGACACC
AGAACCACAATCCAAGGGGAGGAGATCAGTGCCCTTATTTGTATCGCACCCACAGGGTAC
CACTGCCTCGTCTGGCCTGATGGGGAAATGAGCACAGCAAGAGCTGCCCAAGCGGCTGGT
ATCTGCTACATCACCAGCACATTTGCCAGCTGTAGCCTTGAAGACATTGTCATTGCAGCT
CCCGAAGGCCTCCGATGGTTCCAACTCTATGTGCATCCAGACCTGCAGCTGAACAAACAG
TTGATCCAGAGGGTAGAATCCCTAGGTTTCAAAGCTTTGGTAATAACTTTGGATACACCT
GTATGTGGCAACAGGCGACATGACATTCGAAACCAGTTGAGGAGGAACTTAACACTAACA
GATCTTCAATCACCTAAAAAGGGAAATGCAATACCTTATTTCCAGATGACTCCTATCAGC
ACTTCTCTCTGCTGGAATGATCTCTCCTGGTTTCAGAGCATAACTCGATTGCCCATCATC
CTGAAAGGGATTTTGACAAAAGAGGATGCAGAGTTAGCTGTGAAGCACAATGTCCAGGGT
ATCATTGTTTCCAACCATGGTGGGAGGCAGCTTGATGAGGTTCTTGCTTCAATTGATGCT
TTGACAGAAGTGGTGGCTGCTGTAAAGGGGAAAATTGAAGTCTACCTGGATGGCGGGGTC
CGAACTGGCAATGATGTGCTGAAGGCTCTGGCCCATGAAGATAAGTGCATTTTTCTTGGG
AGACCAATCCTATGGGGCCTTGCCTGCAAGGGTGAACATGGTGTTAAGGAAGTTTTGAAC
ATTTTAACAAATGAGTTCCACACTTCCATGGCCCTTACAGGCTGCCGGTCGGTCGCTGAG
ATCAATCGAAACTTGGTCCAGTTTTCCAGGCTGTAA
Enzyme 20 GenBank Gene ID AF203975 Link Image
Enzyme 20 GeneCard ID HAO2 Link Image
Enzyme 20 GenAtlas ID HAO2 Link Image
Enzyme 20 HGNC ID HGNC:4810 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 1p13.3-p13.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Jones JM, Morrell JC, Gould SJ: Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J Biol Chem. 2000 Apr 28;275(17):12590-7. [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]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6089
Enzyme 21 Name Glutathione peroxidase 7
Enzyme 21 Synonyms
  1. GPx-7
  2. GSHPx-7
  3. CL683
Enzyme 21 Gene Name GPX7
Enzyme 21 Protein Sequence >Glutathione peroxidase 7
MVAATVAAAWLLLWAAACAQQEQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFT
DQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFARRTYSVSFPMFSKIAV
TGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALVRKLI
LLKREDL
Enzyme 21 Number of Residues 187
Enzyme 21 Molecular Weight 20995.9
Enzyme 21 Theoretical pI 8.46
Enzyme 21 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 21 General Function Involved in glutathione peroxidase activity
Enzyme 21 Specific Function 2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Enzyme 21 Pathways
Enzyme 21 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [RN:R00274]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-19
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID Q96SL4 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name GPX7_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >564 bp
ATGGTGGCGGCGACGGTGGCAGCGGCGTGGCTGCTCCTGTGGGCTGCGGCCTGCGCGCAG
CAGGAGCAGGACTTCTACGACTTCAAGGCGGTCAACATCCGGGGCAAACTGGTGTCGCTG
GAGAAGTACCGCGGATCGGTGTCCCTGGTGGTGAATGTGGCCAGCGAGTGCGGCTTCACA
GACCAGCACTACCGAGCCCTGCAGCAGCTGCAGCGAGACCTGGGCCCCCACCACTTTAAC
GTGCTCGCCTTCCCCTGCAACCAGTTTGGCCAACAGGAGCCTGACAGCAACAAGGAGATT
GAGAGCTTTGCCCGCCGCACCTACAGTGTCTCATTCCCCATGTTTAGCAAGATTGCAGTC
ACCGGTACTGGTGCCCATCCTGCCTTCAAGTACCTGGCCCAGACTTCTGGGAAGGAGCCC
ACCTGGAACTTCTGGAAGTACCTAGTAGCCCCAGATGGAAAGGTGGTAGGGGCTTGGGAC
CCAACTGTGTCAGTGGAGGAGGTCAGACCCCAGATCACAGCGCTCGTGAGGAAGCTCATC
CTACTGAAGCGAGAAGACTTATAA
Enzyme 21 GenBank Gene ID AF320068 Link Image
Enzyme 21 GeneCard ID GPX7 Link Image
Enzyme 21 GenAtlas ID GPX7 Link Image
Enzyme 21 HGNC ID HGNC:4559 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 1p32
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. 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]
  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]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6090
Enzyme 22 Name Epididymal secretory glutathione peroxidase
Enzyme 22 Synonyms
  1. Epididymis-specific glutathione peroxidase-like protein
  2. EGLP
  3. Glutathione peroxidase 5
  4. GPx-5
  5. GSHPx-5
Enzyme 22 Gene Name GPX5
Enzyme 22 Protein Sequence >Epididymal secretory glutathione peroxidase
MTTQLRVVHLLPLLLACFVQTSPKQEKMKMDCHKDEKGTIYDYEAIALNKNEYVSFKQYV
GKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPGLK
YVRPGGGFVPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSEILGTFKSISWDPVKVHDIR
WNFEKFLVGPDGIPVMRWSHRATVSSVKTDILAYLKQFKTK
Enzyme 22 Number of Residues 221
Enzyme 22 Molecular Weight 25202.1
Enzyme 22 Theoretical pI 8.89
Enzyme 22 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 22 General Function Involved in glutathione peroxidase activity
Enzyme 22 Specific Function Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids
Enzyme 22 Pathways
Enzyme 22 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [RN:R00274]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-21
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 3288455 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID O75715 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name GPX5_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >666 bp
ATGACTACACAGTTAAGGGTCGTCCATCTGCTTCCCCTTCTCCTAGCCTGCTTTGTGCAA
ACAAGTCCCAAGCAGGAGAAGATGAAGATGGATTGCCACAAAGACGAGAAAGGCACCATC
TATGACTATGAGGCCATCGCACTTAATAAGAATGAATATGTTTCCTTCAAGCAGTATGTG
GGCAAGCACATCCTCTTCGTCAACGTGGCCACCTACTGTGGTCTGACAGCGCAATATCCT
GAACTAAATGCACTCCAGGAGGAGCTGAAGCCCTATGGTCTAGTTGTGTTGGGCTTTCCC
TGCAACCAATTTGGAAAGCAAGAACCAGGAGATAACAAAGAGATTCTTCCTGGGCTCAAG
TATGTCCGTCCAGGGGGAGGATTTGTACCTAGTTTCCAGCTTTTTGAGAAAGGGGATGTG
AATGGTGAAAAAGAACAGAAAGTCTTCAGTTTCTTGAAGCACTCCTGTCCTCATCCCTCT
GAGATTTTGGGCACATTCAAATCTATATCCTGGGACCCTGTAAAGGTCCATGACATCCGT
TGGAACTTTGAAAAGTTCCTGGTGGGGCCTGATGGAATCCCTGTCATGCGCTGGTCCCAC
CGGGCTACGGTCAGCTCAGTCAAGACAGACATCCTGGCGTACTTGAAGCAATTCAAAACC
AAATAG
Enzyme 22 GenBank Gene ID AJ005277 Link Image
Enzyme 22 GeneCard ID GPX5 Link Image
Enzyme 22 GenAtlas ID GPX5 Link Image
Enzyme 22 HGNC ID HGNC:4557 Link Image
Enzyme 22 Chromosome Location 6
Enzyme 22 Locus 6p22.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Hall L, Williams K, Perry AC, Frayne J, Jury JA: The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract. Biochem J. 1998 Jul 1;333 ( Pt 1):5-9. [PubMed Link Image]
  2. 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]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6106
Enzyme 23 Name Glutathione peroxidase 6
Enzyme 23 Synonyms
  1. GPx-6
  2. GSHPx-6
Enzyme 23 Gene Name GPX6
Enzyme 23 Protein Sequence >Glutathione peroxidase 6
MFQQFQASCLVLFFLVGFAQQTLKPQNRKVDCNKGVTGTIYEYGALTLNGEEYIQFKQFA
GKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLGLK
YVCPGSGFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDLLGSSSQLFWEPMKVHDIR
WNFEKFLVGPDGVPVMHWFHQAPVSTVKSDILEYLKQFNTH
Enzyme 23 Number of Residues 221
Enzyme 23 Molecular Weight 24970.5
Enzyme 23 Theoretical pI 6.66
Enzyme 23 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 23 General Function Involved in glutathione peroxidase activity
Enzyme 23 Specific Function 2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Enzyme 23 Pathways
Enzyme 23 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [RN:R00274]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-19
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID P59796 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name GPX6_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >666 bp
ATGTTCCAGCAGTTCCAGGCCTCCTGTCTTGTCCTGTTTTTCCTGGTTGGCTTTGCTCAG
CAGACCCTAAAGCCTCAAAATAGGAAGGTGGATTGCAACAAAGGGGTAACAGGCACCATC
TATGAGTATGGAGCCCTCACCCTCAACGGCGAGGAGTACATCCAATTCAAGCAGTTTGCA
GGCAAGCACGTCCTGTTTGTCAATGTGGCCGCCTATTGAGGCTTGGCAGCTCAGTATCCT
GAACTGAATGCACTACAGGAGGAGCTGAAGAATTTTGGTGTCATTGTGTTGGCCTTTCCC
TGCAACCAGTTTGGAAAACAAGAACCAGGAACAAACTCAGAAATACTTCTTGGTCTCAAG
TATGTGTGTCCAGGTAGTGGCTTTGTCCCCAGTTTCCAGCTCTTTGAGAAAGGGGATGTG
AATGGAGAAAAAGAACAGAAGGTCTTTACTTTCCTGAAGAACTCCTGCCCTCCGACCTCT
GATCTTTTGGGCTCATCAAGCCAACTCTTCTGGGAGCCCATGAAGGTCCATGATATCCGC
TGGAACTTTGAGAAATTTCTGGTGGGGCCCGATGGAGTCCCTGTCATGCATTGGTTCCAC
CAGGCTCCAGTCAGCACAGTCAAGTCAGACATCCTGGAGTACCTAAAGCAGTTCAATACC
CACTAG
Enzyme 23 GenBank Gene ID AY324826 Link Image
Enzyme 23 GeneCard ID GPX6 Link Image
Enzyme 23 GenAtlas ID GPX6 Link Image
Enzyme 23 HGNC ID HGNC:4558 Link Image
Enzyme 23 Chromosome Location 6
Enzyme 23 Locus 6p22.1
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed Link Image]
  2. 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]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6109
Enzyme 24 Name Glutathione peroxidase 1
Enzyme 24 Synonyms
  1. GPx-1
  2. GSHPx-1
  3. Cellular glutathione peroxidase
Enzyme 24 Gene Name GPX1
Enzyme 24 Protein Sequence >Glutathione peroxidase 1
MCAARLAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNEL
QRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGA
HPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRR
FQTIDIEPDIEALLSQGPSCA
Enzyme 24 Number of Residues 201
Enzyme 24 Molecular Weight 21945.8
Enzyme 24 Theoretical pI 6.51
Enzyme 24 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 24 General Function Involved in glutathione peroxidase activity
Enzyme 24 Specific Function Protects the hemoglobin in erythrocytes from oxidative breakdown
Enzyme 24 Pathways
Enzyme 24 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [RN:R00274]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 577777 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P07203 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name GPX1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >606 bp
ATGTGTGCTGCTCGGCTAGCGGCGGCGGCGGCCCAGTCGGTGTATGCCTTCTCGGCGCGC
CCGTTGGCCGGCGGGGAGCCTGTGAGCCTGGGCTCCCTGCGGGGCAAGGTACTACTTATC
GAGAATGTGGCGTCCCTCTGAGGCACCACGGTCCGGGACTACACCCAGATGAACGAGCTG
CAGCGGCGCCTCGGACCCCGGGGCCTGGTGGTGCTCGGCTTCCCGTGCAACCAGTTTGGG
CATCAGGAGAACGCCAAGAACGAAGAGATTCTGAATTCCCTCAAGTACGTCCGGCCTGGT
GGTGGGTTCGAGCCCAACTTCATGCTCTTCGAGAAGTGCGAGGTGAACGGTGCGGGGGCG
CACCCTCTCTTCGCCTTCCTGCGGGAGGCCCTGCCAGCTCCCAGCGACGACGCCACCGCG
CTTATGACCGACCCCAAGCTCATCACCTGGTCTCCGGTGTGTCGCAACGATGTTGCCTGG
AACTTTGAGAAGTTCCTGGTGGGCCCTGACGGTGTGCCCCTACGCAGGTACAGCCGCCGC
TTCCAGACCATTGACATCGAGCCTGACATCGAAGCCCTGCTGTCTCAAGGGCCCAGCTGT
GCCTAG
Enzyme 24 GenBank Gene ID Y00433 Link Image
Enzyme 24 GeneCard ID GPX1 Link Image
Enzyme 24 GenAtlas ID GPX1 Link Image
Enzyme 24 HGNC ID HGNC:4553 Link Image
Enzyme 24 Chromosome Location 3
Enzyme 24 Locus 3p21.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Sukenaga Y, Ishida K, Takeda T, Takagi K: cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res. 1987 Sep 11;15(17):7178. [PubMed Link Image]
  2. Ishida K, Morino T, Takagi K, Sukenaga Y: Nucleotide sequence of a human gene for glutathione peroxidase. Nucleic Acids Res. 1987 Dec 10;15(23):10051. [PubMed Link Image]
  3. Mullenbach GT, Tabrizi A, Irvine BD, Bell GI, Hallewell RA: Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine. Nucleic Acids Res. 1987 Jul 10;15(13):5484. [PubMed Link Image]
  4. Chada S, Le Beau MM, Casey L, Newburger PE: Isolation and chromosomal localization of the human glutathione peroxidase gene. Genomics. 1990 Feb;6(2):268-71. [PubMed Link Image]
  5. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed Link Image]
  6. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [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. Forsberg L, de Faire U, Morgenstern R: Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1. Hum Mutat. 1999;13(4):294-300. [PubMed Link Image]
  9. Kote-Jarai Z, Durocher F, Edwards SM, Hamoudi R, Jackson RA, Ardern-Jones A, Murkin A, Dearnaley DP, Kirby R, Houlston R, Easton DF, Eeles R: Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer. Prostate Cancer Prostatic Dis. 2002;5(3):189-92. [PubMed Link Image]
  10. Hamanishi T, Furuta H, Kato H, Doi A, Tamai M, Shimomura H, Sakagashira S, Nishi M, Sasaki H, Sanke T, Nanjo K: Functional variants in the glutathione peroxidase-1 (GPx-1) gene are associated with increased intima-media thickness of carotid arteries and risk of macrovascular diseases in japanese type 2 diabetic patients. Diabetes. 2004 Sep;53(9):2455-60. [PubMed Link Image]
  11. Ichimura Y, Habuchi T, Tsuchiya N, Wang L, Oyama C, Sato K, Nishiyama H, Ogawa O, Kato T: Increased risk of bladder cancer associated with a glutathione peroxidase 1 codon 198 variant. J Urol. 2004 Aug;172(2):728-32. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6110
Enzyme 25 Name Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
Enzyme 25 Synonyms
  1. PHGPx
  2. Glutathione peroxidase 4
  3. GPx-4
  4. GSHPx-4
Enzyme 25 Gene Name GPX4
Enzyme 25 Protein Sequence >Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYR
GFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA
AGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRY
GPMEEPLVIEKDLPHYF
Enzyme 25 Number of Residues 197
Enzyme 25 Molecular Weight 22174.5
Enzyme 25 Theoretical pI 8.48
Enzyme 25 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 25 General Function Involved in glutathione peroxidase activity
Enzyme 25 Specific Function Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage
Enzyme 25 Pathways
Enzyme 25 Reactions
  • 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O [RN:R03167]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 825667 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P36969 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name GPX4_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >594 bp
ATGAGCCTCGGCCGCCTTTGCCGCCTACTGAAGCCGGCGCTGCTCTGTGGGGCTCTGGCC
GCGCCTGGCCTGGCCGGGACCATGTGCGCGTCCCGGGACGACTGGCGCTGTGCGCGCTCC
ATGCACGAGTTTTCCGCCAAGGACATCGACGGGCACATGGTTAACCTGGACAAGTACCGG
GGCTTCGTGTGCATCGTCACCAACGTGGCCTCCCAGTGAGGCAAGACCGAAGTAAACTAC
ACTCAGCTCGTCGACCTGCACGCCCGATACGCTGAGTGTGGTTTGCGGATCCTGGCCTTC
CCGTGTAACCAGTTCGGGAAGCAGGAGCCAGGGAGTAACGAAGAGATCAAAGAGTTCGCC
GCGGGCTACAACGTCAAATTCGATATGTTCAGCAAGATCTGCGTGAACGGGGACGACGCC
CACCCGCTGTGGAAGTGGATGAAGATCCAACCCAAGGGCAAGGGCATCCTGGGAAATGCC
ATCAAGTGGAACTTCACCAAGTTCCTCATCGACAAGAACGGCTGCGTGGTGAAGCGCTAC
GGACCCATGGAGGAGCCCCTGGTGATAGAGAAGGACCTGCCCCACTATTTCTAG
Enzyme 25 GenBank Gene ID X71973 Link Image
Enzyme 25 GeneCard ID GPX4 Link Image
Enzyme 25 GenAtlas ID GPX4 Link Image
Enzyme 25 HGNC ID HGNC:4556 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 19p13.3
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Esworthy RS, Doan K, Doroshow JH, Chu FF: Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase. Gene. 1994 Jul 8;144(2):317-8. [PubMed Link Image]
  2. Kelner MJ, Montoya MA: Structural organization of the human selenium-dependent phospholipid hydroperoxide glutathione peroxidase gene (GPX4): chromosomal localization to 19p13.3. Biochem Biophys Res Commun. 1998 Aug 10;249(1):53-5. [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. 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. Scheerer P, Borchert A, Krauss N, Wessner H, Gerth C, Hohne W, Kuhn H: Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4). Biochemistry. 2007 Aug 7;46(31):9041-9. Epub 2007 Jul 13. [PubMed Link Image]
  7. Maiorino M, Bosello V, Ursini F, Foresta C, Garolla A, Scapin M, Sztajer H, Flohe L: Genetic variations of gpx-4 and male infertility in humans. Biol Reprod. 2003 Apr;68(4):1134-41. Epub 2002 Nov 27. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6111
Enzyme 26 Name Glutathione peroxidase 3
Enzyme 26 Synonyms
  1. GPx-3
  2. GSHPx-3
  3. Extracellular glutathione peroxidase
  4. Plasma glutathione peroxidase
  5. GPx-P
  6. GSHPx-P
Enzyme 26 Gene Name GPX3
Enzyme 26 Protein Sequence >Glutathione peroxidase 3
MARLLQASCLLSLLLAGFVSQSRGQEKSKMDCHGGISGTIYEYGALTIDGEEYIPFKQYA
GKYVLFVNVASYUGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPTLK
YVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIR
WNFEKFLVGPDGIPIMRWHHRTTVSNVKMDILSYMRRQAALGVKRK
Enzyme 26 Number of Residues 226
Enzyme 26 Molecular Weight 25552.2
Enzyme 26 Theoretical pI 8.29
Enzyme 26 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 26 General Function Involved in glutathione peroxidase activity
Enzyme 26 Specific Function Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione
Enzyme 26 Pathways
Enzyme 26 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [RN:R00274]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-20
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 6006001 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P22352 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name GPX3_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >681 bp
ATGGCCCGGCTGCTGCAGGCGTCCTGCCTGCTTTCCCTGCTCCTGGCCGGCTTCGTCTCG
CAGAGCCGGGGACAAGAGAAGTCGAAGATGGACTGCCATGGTGGCATAAGTGGCACCATT
TACGAGTACGGAGCCCTCACCATTGATGGGGAGGAGTACATCCCCTTCAAGCAGTATGCT
GGCAAATACGTCCTCTTTGTCAACGTGGCCAGCTACTGAGGCCTGACGGGCCAGTACATT
GAACTGAATGCACTACAGGAAGAGCTTGCACCATTCGGTCTGGTCATTCTGGGCTTTCCC
TGCAACCAATTTGGAAAACAGGAACCAGGAGAGAACTCAGAGATCCTTCCTACCCTCAAG
TATGTCCGACCAGGTGGAGGCTTTGTCCCTAATTTCCAGCTCTTTGAGAAAGGGGATGTC
AATGGAGAGAAAGAGCAGAAATTCTACACTTTCCTAAAGAACTCCTGTCCTCCCACCTCG
GAGCTCCTGGGTACATCTGACCGCCTCTTCTGGGAACCCATGAAGGTTCACGACATCCGC
TGGAACTTTGAGAAGTTCCTGGTGGGGCCAGATGGTATACCCATCATGCGCTGGCACCAC
CGGACCACGGTCAGCAACGTCAAGATGGACATCCTGTCCTACATGAGGCGGCAGGCAGCC
CTGGGGGTCAAGAGGAAGTAA
Enzyme 26 GenBank Gene ID NM_002084.3 Link Image
Enzyme 26 GeneCard ID GPX3 Link Image
Enzyme 26 GenAtlas ID GPX3 Link Image
Enzyme 26 HGNC ID HGNC:4555 Link Image
Enzyme 26 Chromosome Location 5
Enzyme 26 Locus 5q23
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Takahashi K, Akasaka M, Yamamoto Y, Kobayashi C, Mizoguchi J, Koyama J: Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J Biochem (Tokyo). 1990 Aug;108(2):145-8. [PubMed Link Image]
  2. Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF: Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 1992 Jun 15;79(12):3233-8. [PubMed Link Image]
  3. Yoshimura S, Suemizu H, Taniguchi Y, Arimori K, Kawabe N, Moriuchi T: The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32. Gene. 1994 Aug 5;145(2):293-7. [PubMed Link Image]
  4. Comhair SA, Thomassen MJ, Erzurum SC: Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke. Am J Respir Cell Mol Biol. 2000 Sep;23(3):350-4. [PubMed Link Image]
  5. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [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. Esworthy RS, Chu FF, Paxton RJ, Akman S, Doroshow JH: Characterization and partial amino acid sequence of human plasma glutathione peroxidase. Arch Biochem Biophys. 1991 May 1;286(2):330-6. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6114
Enzyme 27 Name Glutathione peroxidase 2
Enzyme 27 Synonyms
  1. GPx-2
  2. GSHPx-2
  3. Gastrointestinal glutathione peroxidase
  4. Glutathione peroxidase-gastrointestinal
  5. GPx-GI
  6. GSHPx-GI
  7. Glutathione peroxidase-related protein 2
  8. GPRP-2
Enzyme 27 Gene Name GPX2
Enzyme 27 Protein Sequence >Glutathione peroxidase 2
MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRFPRR
LVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLK
DKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEP
DIKRLLKVAI
Enzyme 27 Number of Residues 190
Enzyme 27 Molecular Weight 21953.8
Enzyme 27 Theoretical pI 7.93
Enzyme 27 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 27 General Function Involved in glutathione peroxidase activity
Enzyme 27 Specific Function Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors
Enzyme 27 Pathways
Enzyme 27 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [RN:R00274]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 4902773 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P18283 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name GPX2_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >573 bp
ATGGCTTTCATTGCCAAGTCCTTCTATGACCTCAGTGCCATCAGCCTGGATGGGGAGAAG
GTAGATTTCAATACGTTCCGGGGCAGGGCCGTGCTGATTGAGAATGTGCGTTCGCTCTGA
GGCACAACCACCCGGGACTTCACCCAGCTCAACGAGCTGCAATGCCGCTTTCCCAGGCGC
CTGGTGGTCCTTGGCTTCCCTTGCAACCAATTTGGACATCAGGAGAACAGTCAGAATGAG
GAGATCCTGAACAGTCTCAAGTATGTCCGTCCTGGGGGTGGATACCAGCCCACCTTCACC
CTTGTCCAAAAATGTGAGGTGAATGGGCAGAACGAGCATCCTGTCTTCGCCTACCTGAAG
GACAAGCTCCCCTACCCTTATGATGACCCATTTTCCCTCATGACCGATCCCAAGCTCATC
ATTTGGAGCCCTGTGCGCCGCTCAGATGTGGCCTGGAACTTTGAGAAGTTCCTCATAGGG
CCGGAGGGAGAGCCCTTCCGACGCTACAGCCGCACCTTCCCAACCATCAACATTGAGCCT
GACATCAAGCGCCTCCTTAAAGTTGCCATATAG
Enzyme 27 GenBank Gene ID X53463 Link Image
Enzyme 27 GeneCard ID GPX2 Link Image
Enzyme 27 GenAtlas ID GPX2 Link Image
Enzyme 27 HGNC ID HGNC:4554 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 14q24.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Akasaka M, Mizoguchi J, Takahashi K: A human cDNA sequence of a novel glutathione peroxidase-related protein. Nucleic Acids Res. 1990 Aug 11;18(15):4619. [PubMed Link Image]
  2. Chu FF, Doroshow JH, Esworthy RS: Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J Biol Chem. 1993 Feb 5;268(4):2571-6. [PubMed Link Image]
  3. Kelner MJ, Bagnell RD, Montoya MA, Lanham KA: Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Gene. 2000 May 2;248(1-2):109-16. [PubMed Link Image]
  4. 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]
  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 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6346
Enzyme 28 Name Sulfite oxidase, mitochondrial
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name SUOX
Enzyme 28 Protein Sequence >Sulfite oxidase, mitochondrial
MLLLHRAVVLRLQQACRLKSIPSRICIQACSTNDSFQPQRPSLTFSGDNSSTQGWRVMGT
LLGLGAVLAYQDHRCRAAQESTHIYTKEEVSSHTSPETGIWVTLGSEVFDVTEFVDLHPG
GPSKLMLAAGGPLEPFWALYAVHNQSHVRELLAQYKIGELNPEDKVAPTVETSDPYADDP
VRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGG
QSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCD
VLAQAGHQLCETEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRD
HGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSI
QELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQ
RPRKAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVH
VYVSP
Enzyme 28 Number of Residues 545
Enzyme 28 Molecular Weight 60282.6
Enzyme 28 Theoretical pI 6.03
Enzyme 28 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • molybdenum ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 28 General Function Involved in heme binding
Enzyme 28 Specific Function Sulfite + O(2) + H(2)O = sulfate + H(2)O(2)
Enzyme 28 Pathways
Enzyme 28 Reactions
  • sulfite + O2 + H2O = sulfate + H2O2 [RN:R00533]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 74099694 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P51687 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name SUOX_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1638 bp
ATGCTGCTGCTGCACAGAGCTGTGGTCCTCAGGCTCCAACAGGCCTGCAGACTCAAGTCA
ATCCCCTCAAGGATCTGCATTCAGGCCTGCTCCACAAATGATTCATTTCAGCCCCAGCGC
CCCAGCCTCACCTTCTCTGGTGATAACTCCAGCACCCAGGGATGGAGAGTCATGGGGACC
CTATTAGGTCTCGGTGCAGTGTTGGCCTATCAGGACCATCGGTGTAGGGCTGCTCAGGAG
TCAACACACATATACACTAAGGAGGAAGTGAGTTCCCACACCAGCCCTGAGACTGGGATC
TGGGTGACTCTGGGCTCTGAGGTCTTTGATGTCACAGAATTTGTGGACCTACATCCAGGG
GGGCCTTCAAAGCTGATGCTAGCAGCTGGGGGTCCCCTAGAGCCCTTCTGGGCCCTCTAT
GCTGTTCACAACCAGTCCCATGTGCGTGAGTTACTGGCTCAGTACAAGATTGGGGAGCTG
AATCCTGAAGACAAGGTAGCCCCCACCGTGGAGACCTCTGACCCTTATGCTGATGATCCT
GTACGTCACCCAGCCCTGAAGGTCAACAGCCAGCGGCCCTTTAATGCAGAGCCTCCCCCT
GAGCTGCTGACAGAAAACTACATCACACCCAACCCTATCTTCTTCACCCGGAACCATCTG
CCTGTACCTAACCTGGATCCAGACACCTATCGCTTACACGTAGTAGGAGCACCTGGGGGT
CAGTCACTGTCTCTTTCCCTGGATGACTTGCACAACTTTCCCAGGTACGAGATCACAGTC
ACTCTGCAGTGTGCCGGCAACCGACGCTCTGAGATGACTCAGGTCAAAGAAGTAAAAGGT
CTGGAGTGGAGAACAGGAGCCATCAGCACTGCACGCTGGGCTGGGGCACGGCTCTGTGAT
GTGTTAGCCCAGGCTGGCCACCAACTCTGTGAAACTGAGGCCCACGTCTGCTTTGAGGGA
CTGGACTCAGACCCTACTGGGACTGCCTATGGAGCATCCATCCCTCTGGCTCGGGCCATG
GACCCTGAAGCTGAGGTCCTGCTGGCATATGAGATGAATGGGCAGCCTCTGCCACGTGAC
CACGGCTTCCCTGTGCGTGTGGTGGTTCCTGGAGTGGTGGGTGCCCGCCATGTCAAATGG
CTGGGCAGAGTGAGTGTGCAGCCAGAGGAAAGTTACAGCCACTGGCAACGGCGGGATTAC
AAAGGCTTCTCTCCATCTGTGGACTGGGAGACTGTAGATTTTGACTCTGCTCCATCCATT
CAGGAACTTCCTGTCCAGTCGGCCATCACAGAGCCCCGGGATGGAGAGACTGTAGAATCA
GGGGAGGTGACCATCAAGGGCTATGCATGGAGTGGTGGTGGCAGGGCTGTGATCCGGGTG
GATGTGTCTCTGGATGGGGGCCTAACCTGGCAGGTGGCTAAGCTGGATGGAGAGGAACAG
CGCCCCAGGAAGGCCTGGGCATGGCGTCTGTGGCAGTTGAAAGCCCCTGTGCCAGCTGGA
CAAAAGGAACTGAACATTGTTTGTAAGGCTGTGGATGATGGTTACAATGTGCAGCCAGAC
ACCGTGGCCCCAATCTGGAACCTGCGAGGTGTTCTCAGCAATGCCTGGCATCGTGTCCAT
GTCTATGTCTCCCCATGA
Enzyme 28 GenBank Gene ID NM_000456.2 Link Image
Enzyme 28 GeneCard ID SUOX Link Image
Enzyme 28 GenAtlas ID SUOX Link Image
Enzyme 28 HGNC ID HGNC:11460 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 12q13.2
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Garrett RM, Bellissimo DB, Rajagopalan KV: Molecular cloning of human liver sulfite oxidase. Biochim Biophys Acta. 1995 Jun 9;1262(2-3):147-9. [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. Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C: The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1183-91. Epub 2003 Jun 27. [PubMed Link Image]
  4. Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC: Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell. 1997 Dec 26;91(7):973-83. [PubMed Link Image]
  5. Garrett RM, Johnson JL, Graf TN, Feigenbaum A, Rajagopalan KV: Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme. Proc Natl Acad Sci U S A. 1998 May 26;95(11):6394-8. [PubMed Link Image]
  6. Edwards MC, Johnson JL, Marriage B, Graf TN, Coyne KE, Rajagopalan KV, MacDonald IM: Isolated sulfite oxidase deficiency: review of two cases in one family. Ophthalmology. 1999 Oct;106(10):1957-61. [PubMed Link Image]
  7. Johnson JL, Coyne KE, Garrett RM, Zabot MT, Dorche C, Kisker C, Rajagopalan KV: Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients. Hum Mutat. 2002 Jul;20(1):74. [PubMed Link Image]
  8. Lee HF, Mak BS, Chi CS, Tsai CR, Chen CH, Shu SG: A novel mutation in neonatal isolated sulphite oxidase deficiency. Neuropediatrics. 2002 Aug;33(4):174-9. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6878
Enzyme 29 Name Catalase
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name CAT
Enzyme 29 Protein Sequence >Catalase
MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDE
MAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGES
GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPD
MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ
GIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLT
KVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPD
THRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALE
HSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVK
NFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
Enzyme 29 Number of Residues 527
Enzyme 29 Molecular Weight 59755.8
Enzyme 29 Theoretical pI 7.41
Enzyme 29 GO Classification
Function
  • antioxidant activity
  • binding
  • catalase activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
Enzyme 29 General Function Involved in catalase activity
Enzyme 29 Specific Function Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells
Enzyme 29 Pathways
Enzyme 29 Reactions
  • 2 H2O2 = O2 + 2 H2O [RN:R00009]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 29721 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P04040 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name CATA_HUMAN Link Image
Enzyme 29 PDB ID 1F4J Link Image
Enzyme 29 PDB File Show
Enzyme 29 3D Structure
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1584 bp
ATGGCTGACAGCCGGGATCCCGCCAGCGACCAGATGCAGCACTGGAAGGAGCAGCGGGCC
GCGCAGAAAGCTGATGTCCTGACCACTGGAGCTGGTAACCCAGTAGGAGACAAACTTAAT
GTTATTACAGTAGGGCCCCGTGGGCCCCTTCTTGTTCAGGATGTGGTTTTCACTGATGAA
ATGGCTCATTTTGACCGAGAGAGAATTCCTGAGAGAGTTGTGCATGCTAAAGGAGCAGGG
GCCTTTGGCTACTTTGAGGTCACACATGACATTACCAAATACTCCAAGGCAAAGGTATTT
GAGCATATTGGAAAGAAGACTCCCATCGCAGTTCGGTTCTCCACTGTTGCTGGAGAATCG
GGTTCAGCTGACACAGTTCGGGACCCTCGTGGGTTTGCAGTGAAATTTTACACAGAAGAT
GGTAACTGGGATCTCGTTGGAAATAACACCCCCATTTTCTTCATCAGGGATCCCATATTG
TTTCCATCTTTTATCCACAGCCAAAAGAGAAATCCTCAGACACATCTGAAGGATCCGGAC
ATGGTCTGGGACTTCTGGAGCCTACGTCCTGAGTCTCTGCATCAGGTTTCTTTCTTGTTC
AGTGATCGGGGGATTCCAGATGGACATCGCCACATGAATGGATATGGATCACATACTTTC
AAGCTGGTTAATGCAAATGGGGAGGCAGTTTATTGCAAATTCCATTATAAGACTGACCAG
GGCATCAAAAACCTTTCTGTTGAAGATGCGGCGAGACTTTCCCAGGAAGATCCTGACTAT
GGCATCCGGGATCTTTTTAACGCCATTGCCACAGGAAAGTACCCCTCCTGGACTTTTTAC
ATCCAGGTCATGACATTTAATCAGGCAGAAACTTTTCCATTTAATCCATTCGATCTCACC
AAGGTTTGGCCTCACAAGGACTACCCTCTCATCCCAGTTGGTAAACTGGTCTTAAACCGG
AATCCAGTTAATTACTTTGCTGAGGTTGAACAGATAGCCTTCGACCCAAGCAACATGCCA
CCTGGCATTGAGGCCAGTCCTGACAAAATGCTTCAGGGCCGCCTTTTTGCCTATCCTGAC
ACTCACCGCCATCGCCTGGGACCCAATTATCTTCATATACCTGTGAACTGTCCCTACCGT
GCTCGAGTGGCCAACTACCAGCGTGATGGCCCGATGTGCATGCAGGACAATCAGGGTGGT
GCTCCAAATTACTACCCCAACAGCTTTGGTGCTCCGGAACAACAGCCTTCTGCCCTGGAG
CACAGCATCCAATATTCTGGAGAAGTGCGGAGATTCAACACTGCCAATGATGATAACGTT
ACTCAGGTGCGGGCATTCTATGTGAACGTGCTGAATGAGGAACAGAGGAAACGTCTGTGT
GAGAACATTGCCGGCCACCTGAAGGATGCACAAATTTTCATCCAGAAGAAAGCGGTCAAG
AACTTCACTGAGGTCCACCCTGACTACGGGAGCCACATCCAGGCTCTTCTGGACAAGTAC
AATGCTGAGAAGCCTAAGAATGCGATTCACACCTTTGTGCAGTCCGGATCTCACTTGGCG
GCAAGGGAGAAGGCAAATCTGTGA
Enzyme 29 GenBank Gene ID X04076 Link Image
Enzyme 29 GeneCard ID CAT Link Image
Enzyme 29 GenAtlas ID CAT Link Image
Enzyme 29 HGNC ID HGNC:1516 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 11p13
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Quan F, Korneluk RG, Tropak MB, Gravel RA: Isolation and characterization of the human catalase gene. Nucleic Acids Res. 1986 Jul 11;14(13):5321-35. [PubMed Link Image]
  2. Bell GI, Najarian RC, Mullenbach GT, Hallewell RA: cDNA sequence coding for human kidney catalase. Nucleic Acids Res. 1986 Jul 11;14(13):5561-2. [PubMed Link Image]
  3. Jin LH, Bahn JH, Eum WS, Kwon HY, Jang SH, Han KH, Kang TC, Won MH, Kang JH, Cho SW, Park J, Choi SY: Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells. Free Radic Biol Med. 2001 Dec 1;31(11):1509-19. [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. 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]
  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. Yoo JH, Erzurum SC, Hay JG, Lemarchand P, Crystal RG: Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress. J Clin Invest. 1994 Jan;93(1):297-302. [PubMed Link Image]
  8. 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]
  9. Takeuchi A, Miyamoto T, Yamaji K, Masuho Y, Hayashi M, Hayashi H, Onozaki K: A human erythrocyte-derived growth-promoting factor with a wide target cell spectrum: identification as catalase. Cancer Res. 1995 Apr 1;55(7):1586-9. [PubMed Link Image]
  10. Korneluk RG, Quan F, Lewis WH, Guise KS, Willard HF, Holmes MT, Gravel RA: Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. J Biol Chem. 1984 Nov 25;259(22):13819-23. [PubMed Link Image]
  11. 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]
  12. Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ: Structure of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. [PubMed Link Image]
  13. Putnam CD, Arvai AS, Bourne Y, Tainer JA: Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol. 2000 Feb 11;296(1):295-309. [PubMed Link Image]
  14. Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP: Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 7375
Enzyme 30 Name Superoxide dismutase [Mn], mitochondrial
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name SOD2
Enzyme 30 Protein Sequence >Superoxide dismutase [Mn], mitochondrial
MLSRAVCGTSRQLAPALGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVN
NLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEA
IKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLL
GIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
Enzyme 30 Number of Residues 222
Enzyme 30 Molecular Weight 24722.0
Enzyme 30 Theoretical pI 8.45
Enzyme 30 GO Classification
Function
  • antioxidant activity
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • superoxide dismutase activity
Process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
  • oxygen and reactive oxygen species metabolic process
  • superoxide metabolic process
Component
Enzyme 30 General Function Involved in superoxide dismutase activity
Enzyme 30 Specific Function Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions
  • 2 O2.- + 2 H+ = O2 + H2O2 [RN:R00275]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 34709 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P04179 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name SODM_HUMAN Link Image
Enzyme 30 PDB ID 1LUV Link Image
Enzyme 30 PDB File Show
Enzyme 30 3D Structure
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >669 bp
ATGTTGAGCCGGGCAGTGTGCGGCACCAGCAGGCAGCTGGCTCCGGCTTTGGGGTATCTG
GGCTCCAGGCAGAAGCACAGCCTCCCCGACCTGCCCTACGACTACGGCGCCCTGGAACCT
CACATCAACGCGCAGATCATGCAGCTGCACCACAGCAAGCACCACGCGGCCTACGTGAAC
AACCTGAACGTCAACGAGGAGAAGTACCAGGAGGCGTTGGCCAAGGGAGATGTTACAGCC
CAGATAGCTCTTCAGCCTGCACTGAAGTTCAATGGTGGTGGTCATATCAATCATAGCATT
TTCTGGACAAACCTCAGCCCTAACGGTGGTGGAGAACCCAAAGGGGAGTTGCTGGAAGCC
ATCAAACGTGACTTTGGTTCCTTTGACAAGTTTAAGGAGAAGCTGACGGCTGCATCTGTT
GGTGTCCAAGGCTCAGGTTGGGGTTGGCTTGGTTTCAATAAGGAACGGGGACACTTACAA
ATTGCTGCTTGTCCAAATCAGGATCCACTGCAAGGAACAACAGGCCTTATTCCACTGCTG
GGGATTGATGTGTGGGAGCACGCTTACTACCTTCAGTATAAAAATGTCAGGCCTGATTAT
CTAAAAGCTATTTGGAATGTAATCAACTGGGAGAATGTAACTGAAAGATACATGGCTTGC
AAAAAGTAA
Enzyme 30 GenBank Gene ID X59445 Link Image
Enzyme 30 GeneCard ID SOD2 Link Image
Enzyme 30 GenAtlas ID SOD2 Link Image
Enzyme 30 HGNC ID HGNC:11180 Link Image
Enzyme 30 Chromosome Location 6
Enzyme 30 Locus 6q25.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Wispe JR, Clark JC, Burhans MS, Kropp KE, Korfhagen TR, Whitsett JA: Synthesis and processing of the precursor for human mangano-superoxide dismutase. Biochim Biophys Acta. 1989 Jan 19;994(1):30-6. [PubMed Link Image]
  2. Beck Y, Oren R, Amit B, Levanon A, Gorecki M, Hartman JR: Human Mn superoxide dismutase cDNA sequence. Nucleic Acids Res. 1987 Nov 11;15(21):9076. [PubMed Link Image]
  3. Heckl K: Isolation of cDNAs encoding human manganese superoxide dismutase. Nucleic Acids Res. 1988 Jul 11;16(13):6224. [PubMed Link Image]
  4. Ho YS, Crapo JD: Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase. FEBS Lett. 1988 Mar 14;229(2):256-60. [PubMed Link Image]
  5. Church SL: Manganese superoxide dismutase: nucleotide and deduced amino acid sequence of a cDNA encoding a new human transcript. Biochim Biophys Acta. 1990 Oct 23;1087(2):250-2. [PubMed Link Image]
  6. St Clair DK, Holland JC: Complementary DNA encoding human colon cancer manganese superoxide dismutase and the expression of its gene in human cells. Cancer Res. 1991 Feb 1;51(3):939-43. [PubMed Link Image]
  7. Wan XS, Devalaraja MN, St Clair DK: Molecular structure and organization of the human manganese superoxide dismutase gene. DNA Cell Biol. 1994 Nov;13(11):1127-36. [PubMed Link Image]
  8. 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]
  9. 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]
  10. 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]
  11. Barra D, Schinina ME, Simmaco M, Bannister JV, Bannister WH, Rotilio G, Bossa F: The primary structure of human liver manganese superoxide dismutase. J Biol Chem. 1984 Oct 25;259(20):12595-601. [PubMed Link Image]
  12. Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65. [PubMed Link Image]
  13. 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]
  14. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed Link Image]
  15. MacMillan-Crow LA, Thompson JA: Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite. Arch Biochem Biophys. 1999 Jun 1;366(1):82-8. [PubMed Link Image]
  16. Xu S, Ying J, Jiang B, Guo W, Adachi T, Sharov V, Lazar H, Menzoian J, Knyushko TV, Bigelow D, Schoneich C, Cohen RA: Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging. Am J Physiol Heart Circ Physiol. 2006 Jun;290(6):H2220-7. Epub 2006 Jan 6. [PubMed Link Image]
  17. 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]
  18. Borgstahl GE, Parge HE, Hickey MJ, Beyer WF Jr, Hallewell RA, Tainer JA: The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell. 1992 Oct 2;71(1):107-18. [PubMed Link Image]
  19. Borgstahl GE, Parge HE, Hickey MJ, Johnson MJ, Boissinot M, Hallewell RA, Lepock JR, Cabelli DE, Tainer JA: Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface. Biochemistry. 1996 Apr 9;35(14):4287-97. [PubMed Link Image]
  20. Hsieh Y, Guan Y, Tu C, Bratt PJ, Angerhofer A, Lepock JR, Hickey MJ, Tainer JA, Nick HS, Silverman DN: Probing the active site of human manganese superoxide dismutase: the role of glutamine 143. Biochemistry. 1998 Apr 7;37(14):4731-9. [PubMed Link Image]
  21. Guan Y, Hickey MJ, Borgstahl GE, Hallewell RA, Lepock JR, O'Connor D, Hsieh Y, Nick HS, Silverman DN, Tainer JA: Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Biochemistry. 1998 Apr 7;37(14):4722-30. [PubMed Link Image]
  22. Leveque VJ, Stroupe ME, Lepock JR, Cabelli DE, Tainer JA, Nick HS, Silverman DN: Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis. Biochemistry. 2000 Jun 20;39(24):7131-7. [PubMed Link Image]
  23. Hearn AS, Stroupe ME, Cabelli DE, Lepock JR, Tainer JA, Nick HS, Silverman DN: Kinetic analysis of product inhibition in human manganese superoxide dismutase. Biochemistry. 2001 Oct 9;40(40):12051-8. [PubMed Link Image]
  24. Perry JJ, Hearn AS, Cabelli DE, Nick HS, Tainer JA, Silverman DN: Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis. Biochemistry. 2009 Apr 21;48(15):3417-24. [PubMed Link Image]
  25. Nomiyama T, Tanaka Y, Piao L, Nagasaka K, Sakai K, Ogihara T, Nakajima K, Watada H, Kawamori R: The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients. J Hum Genet. 2003;48(3):138-41. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 7429
Enzyme 31 Name Amyloid beta A4 protein
Enzyme 31 Synonyms
  1. ABPP
  2. APPI
  3. APP
  4. Alzheimer disease amyloid protein
  5. Cerebral vascular amyloid peptide
  6. CVAP
  7. PreA4
  8. Protease nexin-II
  9. PN-II
  10. N-APP
  11. Soluble APP-alpha
  12. S-APP-alpha
  13. Soluble APP-beta
  14. S-APP-beta
  15. C99
  16. Beta-amyloid protein 42
  17. Beta-APP42
  18. Beta-amyloid protein 40
  19. Beta-APP40
  20. C83
  21. P3(42)
  22. P3(40)
  23. C80
  24. Gamma-secretase C-terminal fragment 59
  25. Amyloid intracellular domain 59
  26. AICD-59
  27. AID(59)
  28. Gamma-CTF(59)
  29. Gamma-secretase C-terminal fragment 57
  30. Amyloid intracellular domain 57
  31. AICD-57
  32. AID(57)
  33. Gamma-CTF(57)
  34. Gamma-secretase C-terminal fragment 50
  35. Amyloid intracellular domain 50
  36. AICD-50
  37. AID(50)
  38. Gamma-CTF(50)
  39. C31
Enzyme 31 Gene Name APP
Enzyme 31 Protein Sequence >Amyloid beta A4 protein
MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTK
TCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVG
EFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFR
GVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEE
EADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPC
RAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARD
PVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQA
KNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITAL
QAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYER
MNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTET
KTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTN
IKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITL
VMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN
Enzyme 31 Number of Residues 770
Enzyme 31 Molecular Weight 86942.7
Enzyme 31 Theoretical pI 4.45
Enzyme 31 GO Classification
Function
  • binding
  • endopeptidase inhibitor activity
  • enzyme inhibitor activity
  • enzyme regulator activity
  • peptidase inhibitor activity
  • serine-type endopeptidase inhibitor activity
Process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 31 General Function Involved in binding
Enzyme 31 Specific Function N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6)
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-17
Enzyme 31 Transmembrane Regions
  • 700-723
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 4502167 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID P05067 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name A4_HUMAN Link Image
Enzyme 31 PDB ID 1RW6 Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >2313 bp
ATGCTGCCCGGTTTGGCACTGCTCCTGCTGGCCGCCTGGACGGCTCGGGCGCTGGAGGTA
CCCACTGATGGTAATGCTGGCCTGCTGGCTGAACCCCAGATTGCCATGTTCTGTGGCAGA
CTGAACATGCACATGAATGTCCAGAATGGGAAGTGGGATTCAGATCCATCAGGGACCAAA
ACCTGCATTGATACCAAGGAAGGCATCCTGCAGTATTGCCAAGAAGTCTACCCTGAACTG
CAGATCACCAATGTGGTAGAAGCCAACCAACCAGTGACCATCCAGAACTGGTGCAAGCGG
GGCCGCAAGCAGTGCAAGACCCATCCCCACTTTGTGATTCCCTACCGCTGCTTAGTTGGT
GAGTTTGTAAGTGATGCCCTTCTCGTTCCTGACAAGTGCAAATTCTTACACCAGGAGAGG
ATGGATGTTTGCGAAACTCATCTTCACTGGCACACCGTCGCCAAAGAGACATGCAGTGAG
AAGAGTACCAACTTGCATGACTACGGCATGTTGCTGCCCTGCGGAATTGACAAGTTCCGA
GGGGTAGAGTTTGTGTGTTGCCCACTGGCTGAAGAAAGTGACAATGTGGATTCTGCTGAT
GCGGAGGAGGATGACTCGGATGTCTGGTGGGGCGGAGCAGACACAGACTATGCAGATGGG
AGTGAAGACAAAGTAGTAGAAGTAGCAGAGGAGGAAGAAGTGGCTGAGGTGGAAGAAGAA
GAAGCCGATGATGACGAGGACGATGAGGATGGTGATGAGGTAGAGGAAGAGGCTGAGGAA
CCCTACGAAGAAGCCACAGAGAGAACCACCAGCATTGCCACCACCACCACCACCACCACA
GAGTCTGTGGAAGAGGTGGTTCGAGAGGTGTGCTCTGAACAAGCCGAGACGGGGCCGTGC
CGAGCAATGATCTCCCGCTGGTACTTTGATGTGACTGAAGGGAAGTGTGCCCCATTCTTT
TACGGCGGATGTGGCGGCAACCGGAACAACTTTGACACAGAAGAGTACTGCATGGCCGTG
TGTGGCAGCGCCATGTCCCAAAGTTTACTCAAGACTACCCAGGAACCTCTTGCCCGAGAT
CCTGTTAAACTTCCTACAACAGCAGCCAGTACCCCTGATGCCGTTGACAAGTATCTCGAG
ACACCTGGGGATGAGAATGAACATGCCCATTTCCAGAAAGCCAAAGAGAGGCTTGAGGCC
AAGCACCGAGAGAGAATGTCCCAGGTCATGAGAGAATGGGAAGAGGCAGAACGTCAAGCA
AAGAACTTGCCTAAAGCTGATAAGAAGGCAGTTATCCAGCATTTCCAGGAGAAAGTGGAA
TCTTTGGAACAGGAAGCAGCCAACGAGAGACAGCAGCTGGTGGAGACACACATGGCCAGA
GTGGAAGCCATGCTCAATGACCGCCGCCGCCTGGCCCTGGAGAACTACATCACCGCTCTG
CAGGCTGTTCCTCCTCGGCCTCGTCACGTGTTCAATATGCTAAAGAAGTATGTCCGCGCA
GAACAGAAGGACAGACAGCACACCCTAAAGCATTTCGAGCATGTGCGCATGGTGGATCCC
AAGAAAGCCGCTCAGATCCGGTCCCAGGTTATGACACACCTCCGTGTGATTTATGAGCGC
ATGAATCAGTCTCTCTCCCTGCTCTACAACGTGCCTGCAGTGGCCGAGGAGATTCAGGAT
GAAGTTGATGAGCTGCTTCAGAAAGAGCAAAACTATTCAGATGACGTCTTGGCCAACATG
ATTAGTGAACCAAGGATCAGTTACGGAAACGATGCTCTCATGCCATCTTTGACCGAAACG
AAAACCACCGTGGAGCTCCTTCCCGTGAATGGAGAGTTCAGCCTGGACGATCTCCAGCCG
TGGCATTCTTTTGGGGCTGACTCTGTGCCAGCCAACACAGAAAACGAAGTTGAGCCTGTT
GATGCCCGCCCTGCTGCCGACCGAGGACTGACCACTCGACCAGGTTCTGGGTTGACAAAT
ATCAAGACGGAGGAGATCTCTGAAGTGAAGATGGATGCAGAATTCCGACATGACTCAGGA
TATGAAGTTCATCATCAAAAATTGGTGTTCTTTGCAGAAGATGTGGGTTCAAACAAAGGT
GCAATCATTGGACTCATGGTGGGCGGTGTTGTCATAGCGACAGTGATCGTCATCACCTTG
GTGATGCTGAAGAAGAAACAGTACACATCCATTCATCATGGTGTGGTGGAGGTTGACGCC
GCTGTCACCCCAGAGGAGCGCCACCTGTCCAAGATGCAGCAGAACGGCTACGAAAATCCA
ACCTACAAGTTCTTTGAGCAGATGCAGAACTAG
Enzyme 31 GenBank Gene ID NM_000484.3 Link Image
Enzyme 31 GeneCard ID APP Link Image
Enzyme 31 GenAtlas ID APP Link Image
Enzyme 31 HGNC ID HGNC:620 Link Image
Enzyme 31 Chromosome Location 2
Enzyme 31 Locus 21q21.2|21q21.3
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
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Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 7532
Enzyme 32 Name Superoxide dismutase [Cu-Zn]
Enzyme 32 Synonyms Not Available
Enzyme 32 Gene Name SOD1
Enzyme 32 Protein Sequence >Superoxide dismutase [Cu-Zn]
MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTS
AGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVV
HEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Enzyme 32 Number of Residues 154
Enzyme 32 Molecular Weight 15935.7
Enzyme 32 Theoretical pI 6.07
Enzyme 32 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
  • oxygen and reactive oxygen species metabolic process
  • superoxide metabolic process
Component
Enzyme 32 General Function Involved in metal ion binding
Enzyme 32 Specific Function Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions
  • 2 O2.- + 2 H+ = O2 + H2O2 [RN:R00275]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 36542 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P00441 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name SODC_HUMAN Link Image
Enzyme 32 PDB ID 1PU0 Link Image
Enzyme 32 PDB File Show
Enzyme 32 3D Structure
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >465 bp
ATGGCGACGAAGGCCGTGTGCGTGCTGAAGGGCGACGGCCCAGTGCAGGGCATCATCAAT
TTCGAGCAGAAGGAAAGTAATGGACCAGTGAAGGTGTGGGGAAGCATTAAAGGACTGACT
GAAGGCCTGCATGGATTCCATGTTCATGAGTTTGGAGATAATACAGCAGGCTGTACCAGT
GCAGGTCCTCACTTTAATCCTCTATCCAGAAAACACGGTGGGCCAAAGGATGAAGAGAGG
CATGTTGGAGACTTGGGCAATGTGACTGCTGACAAAGATGGTGTGGCCGATGTGTCTATT
GAAGATTCTGTGATCTCACTCTCAGGAGACCATTGCATCATTGGCCGCACACTGGTGGTC
CATGAAAAAGCAGATGACTTGGGCAAAGGTGGAAATGAAGAAAGTACAAAGACAGGAAAC
GCTGGAAGTCGTTTGGCTTGTGGTGTAATTGGGATCGCCCAATAA
Enzyme 32 GenBank Gene ID X02317 Link Image
Enzyme 32 GeneCard ID SOD1 Link Image
Enzyme 32 GenAtlas ID SOD1 Link Image
Enzyme 32 HGNC ID HGNC:11179 Link Image
Enzyme 32 Chromosome Location 2
Enzyme 32 Locus 21q22.1|21q22.11
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
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  2. Levanon D, Lieman-Hurwitz J, Dafni N, Wigderson M, Sherman L, Bernstein Y, Laver-Rudich Z, Danciger E, Stein O, Groner Y: Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. EMBO J. 1985 Jan;4(1):77-84. [PubMed Link Image]
  3. Hallewell RA, Masiarz FR, Najarian RC, Puma JP, Quiroga MR, Randolph A, Sanchez-Pescador R, Scandella CJ, Smith B, Steimer KS, et al.: Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library. Nucleic Acids Res. 1985 Mar 25;13(6):2017-34. [PubMed Link Image]
  4. Kajihara J, Enomoto M, Nishijima K, Yabuuchi M, Katoh K: Comparison of properties between human recombinant and placental copper-zinc SOD. J Biochem (Tokyo). 1988 Nov;104(5):851-4. [PubMed Link Image]
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  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]
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  24. Strange RW, Antonyuk SV, Hough MA, Doucette PA, Valentine JS, Hasnain SS: Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. J Mol Biol. 2006 Mar 10;356(5):1152-62. Epub 2005 Dec 12. [PubMed Link Image]
  25. Hornberg A, Logan DT, Marklund SL, Oliveberg M: The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase. J Mol Biol. 2007 Jan 12;365(2):333-42. Epub 2006 Sep 23. [PubMed Link Image]
  26. Roberts BR, Tainer JA, Getzoff ED, Malencik DA, Anderson SR, Bomben VC, Meyers KR, Karplus PA, Beckman JS: Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS. J Mol Biol. 2007 Nov 2;373(4):877-90. Epub 2007 Aug 2. [PubMed Link Image]
  27. Strange RW, Yong CW, Smith W, Hasnain SS: Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase. Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10040-4. Epub 2007 Jun 4. [PubMed Link Image]
  28. Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ: Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. J Biol Chem. 2008 Jun 6;283(23):16169-77. Epub 2008 Mar 31. [PubMed Link Image]
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  35. Jones CT, Swingler RJ, Brock DJ: Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others. Hum Mol Genet. 1994 Apr;3(4):649-50. [PubMed Link Image]
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  42. Ikeda M, Abe K, Aoki M, Ogasawara M, Kameya T, Watanabe M, Shoji M, Hirai S, Itoyama Y: A novel point mutation in the Cu/Zn superoxide dismutase gene in a patient with familial amyotrophic lateral sclerosis. Hum Mol Genet. 1995 Mar;4(3):491-2. [PubMed Link Image]
  43. Yulug IG, Katsanis N, de Belleroche J, Collinge J, Fisher EM: An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4. Hum Mol Genet. 1995 Jun;4(6):1101-4. [PubMed Link Image]
  44. Sjalander A, Beckman G, Deng HX, Iqbal Z, Tainer JA, Siddique T: The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase that is prevalent in northern Sweden and Finland. Hum Mol Genet. 1995 Jun;4(6):1105-8. [PubMed Link Image]
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  48. Ikeda M, Abe K, Aoki M, Sahara M, Watanabe M, Shoji M, St George-Hyslop PH, Hirai S, Itoyama Y: Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene. Neurology. 1995 Nov;45(11):2038-42. [PubMed Link Image]
  49. Sapp PC, Rosen DR, Hosler BA, Esteban J, McKenna-Yasek D, O'Regan JP, Horvitz HR, Brown RH Jr: Identification of three novel mutations in the gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis. Neuromuscul Disord. 1995 Sep;5(5):353-7. [PubMed Link Image]
  50. Hosler BA, Nicholson GA, Sapp PC, Chin W, Orrell RW, de Belleroche JS, Esteban J, Hayward LJ, Mckenna-Yasek D, Yeung L, Cherryson AK, Dench JE, Wilton SD, Laing NG, Horvitz RH, Brown RH Jr: Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis. Neuromuscul Disord. 1996 Oct;6(5):361-6. [PubMed Link Image]
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  53. Kawamata J, Shimohama S, Takano S, Harada K, Ueda K, Kimura J: Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with apparently sporadic young-onset amyotrophic lateral sclerosis. Hum Mutat. 1997;9(4):356-8. [PubMed Link Image]
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Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 7995
Enzyme 33 Name Peroxiredoxin-5, mitochondrial
Enzyme 33 Synonyms
  1. Alu corepressor 1
  2. Antioxidant enzyme B166
  3. AOEB166
  4. Liver tissue 2D-page spot 71B
  5. PLP
  6. Peroxiredoxin V
  7. Prx-V
  8. Peroxisomal antioxidant enzyme
  9. TPx type VI
  10. Thioredoxin peroxidase PMP20
  11. Thioredoxin reductase
Enzyme 33 Gene Name PRDX5
Enzyme 33 Protein Sequence >Peroxiredoxin-5, mitochondrial
MGLAGVCALRRSAGYILVGGAGGQSAAAAARRCSEGEWASGGVRSFSRAAAAMAPIKVGD
AIPAVEVFEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGV
QVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLVSIFGNRRLKR
FSMVVQDGIVKALNVEPDGTGLTCSLAPNIISQL
Enzyme 33 Number of Residues 214
Enzyme 33 Molecular Weight 22026.2
Enzyme 33 Theoretical pI 8.77
Enzyme 33 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
Component
Enzyme 33 General Function Involved in oxidoreductase activity
Enzyme 33 Specific Function Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions
  • 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH [RN:R07180]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 6103724 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P30044 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PRDX5_HUMAN Link Image
Enzyme 33 PDB ID 1OC3 Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >645 bp
ATGGGACTAGCTGGCGTGTGCGCCCTGAGACGCTCAGCGGGCTATATACTCGTCGGTGGG
GCCGGCGGTCAGTCTGCGGCAGCGGCAGCAAGACGGTGCAGTGAAGGAGAGTGGGCGTCT
GGCGGGGTCCGCAGTTTCAGCAGAGCCGCTGCAGCCATGGCCCCAATCAAGGTGGGAGAT
GCCATCCCAGCAGTGGAGGTGTTTGAAGGGGAGCCAGGGAACAAGGTGAACCTGGCAGAG
CTGTTCAAGGGCAAGAAGGGTGTGCTGTTTGGAGTTCCTGGGGCCTTCACCCCTGGATGT
TCCAAGACACACCTGCCAGGGTTTGTGGAGCAGGCTGAGGCTCTGAAGGCCAAGGGAGTC
CAGGTGGTGGCCTGTCTGAGTGTTAATGATGCCTTTGTGACTGGCGAGTGGGGCCGAGCC
CACAAGGCGGAAGGCAAGGTTCGGCTCCTGGCTGATCCCACTGGGGCCTTTGGGAAGGAG
ACAGACTTATTACTAGATGATTCGCTGGTGTCCATCTTTGGGAATCGACGTCTCAAGAGG
TTCTCCATGGTGGTACAGGATGGCATAGTGAAGGCCCTGAATGTGGAACCAGATGGCACA
GGCCTCACCTGCAGCCTGGCACCCAATATCATCTCACAGCTCTGA
Enzyme 33 GenBank Gene ID AF110731 Link Image
Enzyme 33 GeneCard ID PRDX5 Link Image
Enzyme 33 GenAtlas ID PRDX5 Link Image
Enzyme 33 HGNC ID HGNC:9355 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 11q13
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Kropotov A, Sedova V, Ivanov V, Sazeeva N, Tomilin A, Krutilina R, Oei SL, Griesenbeck J, Buchlow G, Tomilin N: A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro. Eur J Biochem. 1999 Mar;260(2):336-46. [PubMed Link Image]
  2. Yamashita H, Avraham S, Jiang S, London R, Van Veldhoven PP, Subramani S, Rogers RA, Avraham H: Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro. J Biol Chem. 1999 Oct 15;274(42):29897-904. [PubMed Link Image]
  3. Knoops B, Clippe A, Bogard C, Arsalane K, Wattiez R, Hermans C, Duconseille E, Falmagne P, Bernard A: Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. J Biol Chem. 1999 Oct 22;274(43):30451-8. [PubMed Link Image]
  4. Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY: Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis. Biochem Biophys Res Commun. 2000 Feb 24;268(3):921-7. [PubMed Link Image]
  5. Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG: Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J Biol Chem. 2000 Jul 7;275(27):20346-54. [PubMed Link Image]
  6. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  7. 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]
  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. 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. 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]
  11. Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B: Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. J Mol Biol. 2001 Aug 24;311(4):751-9. [PubMed Link Image]
  12. 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 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 8628
Enzyme 34 Name Dual oxidase 2
Enzyme 34 Synonyms
  1. Large NOX 2
  2. Long NOX 2
  3. NADH/NADPH thyroid oxidase p138-tox
  4. NADPH oxidase/peroxidase DUOX2
  5. NADPH thyroid oxidase 2
  6. Thyroid oxidase 2
  7. p138 thyroid oxidase
Enzyme 34 Gene Name DUOX2
Enzyme 34 Protein Sequence >Dual oxidase 2
MLRARPEALMLLGALLTGSLGPSGNQDALSLPWEVQRYDGWFNNLRHHERGAVGCRLQRR
VPANYADGVYQALEEPQLPNPRRLSNAATRGIAGLPSLHNRTVLGVFFGYHVLSDVVSVE
TPGCPAEFLNIRIPPGDPVFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDLANQVTGWLD
GSAIYGSSHSWSDALRSFSGGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAF
GAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYE
WLPSFLQKTLPEYTGYRPFLDPSISPEFVVASEQFFSTMVPPGVYMRNASCHFRKVLNKG
FQSSQALRVCNNYWIRENPNLNSTQEVNELLLGMASQISELEDNIVVEDLRDYWPGPGKF
SRTDYVASSIQRGRDMGLPSYSQALLAFGLDIPRNWSDLNPNVDPQVLEATAALYNQDLS
QLELLLGGLLESHGDPGPLFSAIVLDQFVRLRDGDRYWFENTRNGLFSKKEIEDIRNTTL
RDVLVAVINIDPSALQPNVFVWHKGAPCPQPKQLTTDGLPQCAPLTVLDFFEGSSPGFAI
TIIALCCLPLVSLLLSGVVAYFRGREHKKLQKKLKESVKKEAAKDGVPAMEWPGPKERSS
PIIIQLLSDRCLQVLNRHLTVLRVVQLQPLQQVNLILSNNRGCRTLLLKIPKEYDLVLLF
SSEEERGAFVQQLWDFCVRWALGLHVAEMSEKELFRKAVTKQQRERILEIFFRHLFAQVL
DINQADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLS
FREFLDILVVFMKGSPEDKSRLMFTMYDLDENGFLSKDEFFTMMRSFIEISNNCLSKAQL
AEVVESMFRESGFQDKEELTWEDFHFMLRDHDSELRFTQLCVKGGGGGGNGIRDIFKQNI
SCRVSFITRTPGERSHPQGLGPPAPEAPELGGPGLKKRFGKKAAVPTPRLYTEALQEKMQ
RGFLAQKLQQYKRFVENYRRHIVCVAIFSAICVGVFADRAYYYGFASPPSDIAQTTLVGI
ILSRGTAASVSFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRWIAMAAVVLAIL
HSAGHAVNVYIFSVSPLSLLACIFPNVFVNDGSKLPQKFYWWFFQTVPGMTGVLLLLVLA
IMYVFASHHFRRRSFRGFWLTHHLYILLYALLIIHGSYALIQLPTFHIYFLVPAIIYGGD
KLVSLSRKKVEISVVKAELLPSGVTYLQFQRPQGFEYKSGQWVRIACLALGTTEYHPFTL
TSAPHEDTLSLHIRAVGPWTTRLREIYSSPKGNGCAGYPKLYLDGPFGEGHQEWHKFEVS
VLVGGGIGVTPFASILKDLVFKSSLGSQMLCKKIYFIWVTRTQRQFEWLADIIQEVEEND
HQDLVSVHIYVTQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFN
SLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLVNRQDRAHFMHHYENF
Enzyme 34 Number of Residues 1548
Enzyme 34 Molecular Weight 175362.9
Enzyme 34 Theoretical pI 7.90
Enzyme 34 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • antioxidant activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleoside binding
  • oxidoreductase activity
  • peroxidase activity
  • purine nucleoside binding
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 34 General Function Involved in calcium ion binding
Enzyme 34 Specific Function Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions
  • NAD(P)H + H+ + O2 = NAD(P)+ + H2O2 [RN:R07171 R07172]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • 1-25
Enzyme 34 Transmembrane Regions
  • 602-622 1042-1062 1077-1097 1149-1169 1186-1206 1224-1244 1245-1265
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 132566532 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9NRD8 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name DUOX2_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >4647 bp
ATGCTCCGTGCAAGACCAGAGGCACTGATGCTCCTGGGAGCTCTTCTGACTGGATCCCTG
GGTCCATCGGGCAATCAGGACGCACTCTCACTGCCCTGGGAAGTGCAGCGCTATGACGGC
TGGTTTAACAACCTGAGGCACCACGAGCGTGGTGCTGTTGGCTGCCGGTTGCAGCGCCGC
GTACCAGCCAATTACGCCGACGGTGTGTATCAGGCTCTGGAGGAGCCGCAGCTGCCCAAC
CCGCGCCGGCTCAGCAACGCAGCCACGCGGGGCATAGCCGGCCTGCCGTCGCTCCACAAC
CGCACCGTACTGGGGGTCTTCTTTGGCTACCATGTTCTTTCCGACGTGGTGAGCGTGGAA
ACGCCCGGTTGCCCCGCCGAGTTCCTCAACATCCGCATCCCACCTGGAGACCCCGTGTTC
GACCCCGACCAGCGCGGGGACGTGGTGCTGCCCTTCCAGAGGAGCCGCTGGGACCCCGAG
ACCGGACGGAGTCCCAGCAACCCCCGGGACCTGGCCAACCAGGTGACGGGCTGGCTGGAC
GGCAGCGCCATCTATGGCTCCTCGCACTCCTGGAGCGACGCGCTGCGGAGCTTCTCGGGG
GGACAGCTGGCGTCGGGGCCCGACCCCGCTTTCCCCCGAGACTCGCAGAACCCCCTGCTC
ATGTGGGCGGCGCCCGACCCCGCCACCGGGCAGAACGGGCCCCGGGGGCTGTACGCCTTC
GGGGCAGAGAGAGGGAACCGGGAACCCTTCCTGCAGGCGCTGGGCCTGCTCTGGTTCCGC
TACCACAACCTGTGGGCGCAGAGGCTGGCCCGCCAGCACCCAGACTGGGAGGACGAGGAG
CTGTTCCAGCACGCACGCAAGAGGGTCATCGCCACCTACCAGAACATCGCTGTGTATGAG
TGGCTGCCCAGCTTCCTGCAGAAAACACTCCCGGAGTATACAGGATACCGTCCTTTCCTA
GACCCCAGCATCTCCCCGGAATTTGTGGTGGCCTCTGAGCAGTTCTTCTCTACCATGGTG
CCCCCTGGTGTCTACATGAGAAATGCCAGCTGTCATTTCCGGAAGGTCCTGAACAAGGGT
TTTCAAAGCTCCCAAGCTCTCAGGGTCTGCAACAACTACTGGATTCGGGAGAACCCCAAT
CTGAACAGTACCCAGGAGGTGAATGAGCTGCTGCTGGGAATGGCCTCCCAGATTTCGGAG
TTGGAGGACAACATAGTGGTTGAAGATCTGAGGGATTACTGGCCTGGCCCTGGCAAATTC
TCCCGTACAGACTATGTGGCCAGCAGCATCCAACGTGGCCGAGATATGGGGCTGCCCAGC
TATAGCCAGGCCCTGCTGGCCTTTGGGCTGGACATCCCAAGGAACTGGAGTGATCTCAAC
CCTAATGTGGACCCCCAGGTGCTGGAGGCCACAGCTGCCCTGTACAACCAGGACCTATCC
CAGCTAGAGCTGCTCCTTGGGGGGCTCCTGGAGAGCCATGGGGACCCTGGACCCCTGTTC
AGTGCCATTGTCCTCGACCAGTTTGTACGGCTGCGGGATGGTGACCGCTACTGGTTTGAG
AACACCAGGAATGGGCTGTTCTCCAAGAAGGAGATTGAAGACATCCGAAATACCACCCTG
CGGGACGTGCTGGTCGCTGTTATCAACATTGACCCCAGTGCCCTGCAGCCCAATGTCTTT
GTCTGGCATAAAGGTGCACCCTGCCCTCAACCTAAGCAGCTCACAACTGACGGCCTGCCC
CAGTGTGCACCCCTGACTGTGCTTGACTTCTTTGAAGGCAGCAGCCCTGGTTTTGCCATC
ACCATCATTGCTCTCTGCTGCCTTCCCTTAGTGAGTCTGCTTCTCTCTGGAGTGGTGGCC
TATTTCCGGGGCCGAGAACACAAGAAGCTACAAAAGAAACTCAAAGAGAGCGTGAAGAAG
GAAGCAGCCAAAGATGGAGTGCCAGCGATGGAGTGGCCAGGCCCCAAGGAGAGGAGCAGT
CCCATCATCATCCAGCTGCTGTCAGACAGGTGTCTGCAGGTCCTGAACAGGCATCTCACT
GTGCTCCGTGTGGTCCAGCTGCAGCCTCTGCAGCAGGTCAACCTCATCCTGTCCAACAAC
CGAGGATGCCGCACCCTGCTGCTCAAGATCCCTAAGGAGTATGACCTGGTGCTGCTGTTT
AGTTCTGAAGAGGAACGGGGCGCCTTTGTGCAGCAGCTATGGGACTTCTGCGTGCGCTGG
GCTCTGGGCCTCCATGTGGCTGAGATGAGCGAGAAGGAGCTATTTAGGAAGGCTGTGACA
AAGCAGCAGCGGGAACGCATCCTGGAGATCTTCTTCAGACACCTTTTTGCTCAGGTGCTG
GACATCAACCAGGCCGACGCAGGGACCCTGCCCCTGGACTCCTCCCAGAAGGTGCGGGAG
GCCCTGACCTGCGAGCTGAGCAGGGCCGAGTTTGCCGAGTCCCTGGGCCTCAAGCCCCAG
GACATGTTTGTGGAGTCCATGTTCTCTCTGGCTGACAAGGATGGCAATGGCTACCTGTCC
TTCCGAGAGTTCCTGGACATCCTGGTGGTCTTCATGAAAGGCTCCCCAGAGGATAAGTCC
CGTCTAATGTTTACCATGTATGACCTGGATGAGAATGGCTTCCTCTCCAAGGACGAATTC
TTCACCATGATGCGATCCTTCATCGAGATCTCCAACAACTGCCTGTCCAAGGCCCAGCTG
GCCGAGGTGGTGGAGTCTATGTTCCGGGAGTCGGGATTCCAGGACAAGGAGGAGCTGACA
TGGGAGGATTTTCACTTCATGCTGCGGGACCATGACAGCGAGCTCCGCTTCACGCAGCTC
TGTGTCAAAGGTGGAGGTGGAGGTGGAAATGGTATTAGAGATATCTTTAAACAAAACATC
AGCTGTCGAGTCTCGTTCATCACTCGGACACCTGGGGAGCGCTCCCACCCCCAGGGACTG
GGGCCCCCTGCCCCAGAAGCCCCAGAGCTGGGAGGCCCTGGACTGAAGAAGAGGTTTGGC
AAAAAGGCAGCAGTGCCCACTCCCCGGCTGTACACAGAGGCGCTGCAAGAGAAGATGCAG
CGAGGCTTCCTAGCCCAAAAGCTGCAGCAGTACAAGCGCTTCGTGGAGAACTACCGGAGG
CACATCGTGTGTGTGGCAATCTTCTCGGCCATCTGTGTTGGCGTGTTTGCAGATCGTGCT
TACTACTATGGCTTTGCCTCGCCACCCTCGGACATTGCACAGACCACCCTCGTGGGCATC
ATCCTGTCACGAGGCACGGCGGCCAGCGTCTCCTTCATGTTCTCTTATATCTTGCTCACC
ATGTGCCGCAACCTCATAACCTTCCTGCGAGAGACTTTCCTCAACCGCTATGTGCCTTTT
GATGCCGCAGTGGACTTCCACCGCTGGATCGCCATGGCTGCTGTTGTCCTGGCCATTTTG
CACAGTGCTGGCCACGCAGTCAATGTCTACATCTTCTCAGTCAGCCCACTCAGCCTGCTG
GCCTGCATATTCCCCAACGTCTTTGTGAATGATGGGTCCAAGCTTCCCCAGAAGTTCTAT
TGGTGGTTCTTCCAGACCGTCCCAGGTATGACAGGTGTGCTTCTGCTCCTGGTCCTGGCC
ATCATGTATGTCTTCGCCTCCCACCACTTCCGCCGCCGCAGCTTCCGGGGCTTCTGGCTG
ACCCACCACCTCTACATCCTGCTCTATGCCCTGCTCATCATCCATGGCAGCTATGCTCTG
ATCCAGCTGCCCACTTTCCACATCTACTTCCTGGTCCCGGCAATCATCTATGGAGGTGAC
AAGCTGGTGAGCCTGAGCCGGAAGAAGGTGGAGATCAGCGTGGTGAAGGCGGAGCTGCTG
CCCTCAGGAGTGACCTACCTGCAATTCCAGAGGCCCCAAGGCTTTGAGTACAAGTCAGGA
CAGTGGGTGCGGATCGCCTGCCTGGCTCTGGGGACCACCGAGTACCACCCCTTCACACTG
ACCTCCGCGCCCCATGAGGACACACTCAGCCTGCACATCCGGGCAGTGGGGCCCTGGACC
ACTCGCCTCAGGGAGATCTACTCATCCCCAAAGGGCAATGGCTGTGCTGGATACCCAAAG
CTGTACCTTGATGGACCGTTTGGAGAGGGCCATCAGGAGTGGCATAAATTTGAGGTGTCA
GTGTTGGTGGGAGGGGGCATTGGGGTCACCCCCTTTGCCTCCATCCTCAAAGACCTGGTC
TTCAAGTCATCCTTGGGCAGCCAAATGCTGTGTAAGAAGATCTACTTCATCTGGGTGACA
CGGACCCAGCGTCAGTTTGAGTGGCTGGCTGACATCATCCAAGAGGTGGAGGAGAACGAC
CACCAGGACCTGGTGTCTGTGCACATTTATGTCACCCAGCTGGCTGAGAAGTTCGACCTC
AGGACCACCATGCTATACATCTGCGAGCGGCACTTCCAGAAAGTGCTGAACCGGAGTCTG
TTCACGGGCCTGCGCTCCATCACCCACTTTGGCCGTCCCCCCTTCGAGCCCTTCTTCAAC
TCCCTGCAGGAGGTCCACCCACAGGTGCGCAAGATCGGGGTGTTCAGCTGCGGCCCTCCA
GGAATGACCAAGAATGTAGAGAAGGCCTGTCAGCTCGTCAACAGGCAGGACCGAGCCCAC
TTCATGCACCACTATGAGAACTTCTGA
Enzyme 34 GenBank Gene ID NM_014080.4 Link Image
Enzyme 34 GeneCard ID DUOX2 Link Image
Enzyme 34 GenAtlas ID DUOX2 Link Image
Enzyme 34 HGNC ID HGNC:13273 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 15q15.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. De Deken X, Wang D, Many MC, Costagliola S, Libert F, Vassart G, Dumont JE, Miot F: Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J Biol Chem. 2000 Jul 28;275(30):23227-33. [PubMed Link Image]
  2. Edens WA, Sharling L, Cheng G, Shapira R, Kinkade JM, Lee T, Edens HA, Tang X, Sullards C, Flaherty DB, Benian GM, Lambeth JD: Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. J Cell Biol. 2001 Aug 20;154(4):879-91. [PubMed Link Image]
  3. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  4. Dupuy C, Ohayon R, Valent A, Noel-Hudson MS, Deme D, Virion A: Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cdnas. J Biol Chem. 1999 Dec 24;274(52):37265-9. [PubMed Link Image]
  5. De Deken X, Wang D, Dumont JE, Miot F: Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system. Exp Cell Res. 2002 Feb 15;273(2):187-96. [PubMed Link Image]
  6. Moreno JC, Bikker H, Kempers MJ, van Trotsenburg AS, Baas F, de Vijlder JJ, Vulsma T, Ris-Stalpers C: Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. N Engl J Med. 2002 Jul 11;347(2):95-102. [PubMed Link Image]
  7. Geiszt M, Witta J, Baffi J, Lekstrom K, Leto TL: Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. FASEB J. 2003 Aug;17(11):1502-4. Epub 2003 Jun 3. [PubMed Link Image]
  8. Schwarzer C, Machen TE, Illek B, Fischer H: NADPH oxidase-dependent acid production in airway epithelial cells. J Biol Chem. 2004 Aug 27;279(35):36454-61. Epub 2004 Jun 21. [PubMed Link Image]
  9. El Hassani RA, Benfares N, Caillou B, Talbot M, Sabourin JC, Belotte V, Morand S, Gnidehou S, Agnandji D, Ohayon R, Kaniewski J, Noel-Hudson MS, Bidart JM, Schlumberger M, Virion A, Dupuy C: Dual oxidase2 is expressed all along the digestive tract. Am J Physiol Gastrointest Liver Physiol. 2005 May;288(5):G933-42. Epub 2004 Dec 9. [PubMed Link Image]
  10. 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]
  11. Ameziane-El-Hassani R, Morand S, Boucher JL, Frapart YM, Apostolou D, Agnandji D, Gnidehou S, Ohayon R, Noel-Hudson MS, Francon J, Lalaoui K, Virion A, Dupuy C: Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity. J Biol Chem. 2005 Aug 26;280(34):30046-54. Epub 2005 Jun 22. [PubMed Link Image]
  12. Vigone MC, Fugazzola L, Zamproni I, Passoni A, Di Candia S, Chiumello G, Persani L, Weber G: Persistent mild hypothyroidism associated with novel sequence variants of the DUOX2 gene in two siblings. Hum Mutat. 2005 Oct;26(4):395. [PubMed Link Image]
  13. Varela V, Rivolta CM, Esperante SA, Gruneiro-Papendieck L, Chiesa A, Targovnik HM: Three mutations (p.Q36H, p.G418fsX482, and g.IVS19-2A>C) in the dual oxidase 2 gene responsible for congenital goiter and iodide organification defect. Clin Chem. 2006 Feb;52(2):182-91. Epub 2005 Dec 1. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 8702
Enzyme 35 Name Extracellular superoxide dismutase [Cu-Zn]
Enzyme 35 Synonyms
  1. EC-SOD
Enzyme 35 Gene Name SOD3
Enzyme 35 Protein Sequence >Extracellular superoxide dismutase [Cu-Zn]
MLALLCSCLLLAAGASDAWTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALH
AACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGD
LSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVV
HAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA
Enzyme 35 Number of Residues 240
Enzyme 35 Molecular Weight 25850.7
Enzyme 35 Theoretical pI 6.59
Enzyme 35 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
  • oxygen and reactive oxygen species metabolic process
  • superoxide metabolic process
Component
Enzyme 35 General Function Involved in metal ion binding
Enzyme 35 Specific Function Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions
  • 2 O2.- + 2 H+ = O2 + H2O2 [RN:R00275]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-18
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 338284 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P08294 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name SODE_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >723 bp
ATGCTGGCGCTACTGTGTTCCTGCCTGCTCCTGGCAGCCGGTGCCTCGGACGCCTGGACG
GGCGAGGACTCGGCGGAGCCCAACTCTGACTCGGCGGAGTGGATCCGAGACATGTACGCC
AAGGTCACGGAGATCTGGCAGGAGGTCATGCAGCGGCGGGACGACGACGGCACGCTCCAC
GCCGCCTGCCAGGTGCAGCCGTCGGCCACGCTGGACGCCGCGCAGCCCCGGGTGACCGGC
GTCGTCCTCTTCCGGCAGCTTGCGCCCCGCGCCAAGCTCGACGCCTTCTTCGCCCTGGAG
GGCTTCCCGACCGAGCCGAACAGCTCCAGCCGCGCCATCCACGTGCACCAGTTCGGGGAC
CTGAGCCAGGGCTGCGAGTCCACCGGGCCCCACTACAACCCGCTGGCCGTGCCGCACCCG
CAGCACCCGGGCGACTTCGGCAACTTCGCGGTCCGCGACGGCAGCCTCTGGAGGTACCGC
GCCGGCCTGGCCGCCTCGCTCGCGGGCCCGCACTCCATCGTGGGCCGGGCCGTGGTCGTC
CACGCTGGCGAGGACGACCTGGGCCGCGGCGGCAACCAGGCCAGCGTGGAGAACGGGAAC
GCGGGCCGGCGGCTGGCCTGCTGCGTGGTGGGCGTGTGCGGGCCCGGGCTCTGGGAGCGC
CAGGCGCGGGAGCACTCAGAGCGCAAGAAGCGGCGGCGCGAGAGCGAGTGCAAGGCCGCC
TGA
Enzyme 35 GenBank Gene ID J02947 Link Image
Enzyme 35 GeneCard ID SOD3 Link Image
Enzyme 35 GenAtlas ID SOD3 Link Image
Enzyme 35 HGNC ID HGNC:11181 Link Image
Enzyme 35 Chromosome Location 4
Enzyme 35 Locus 4p15.3-p15.1
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Hjalmarsson K, Marklund SL, Engstrom A, Edlund T: Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6340-4. [PubMed Link Image]
  2. Folz RJ, Crapo JD: Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene. Genomics. 1994 Jul 1;22(1):162-71. [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. Adachi T, Ohta H, Hayashi K, Hirano K, Marklund SL: The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro. Free Radic Biol Med. 1992 Sep;13(3):205-10. [PubMed Link Image]
  5. Nozik-Grayck E, Suliman HB, Piantadosi CA: Extracellular superoxide dismutase. Int J Biochem Cell Biol. 2005 Dec;37(12):2466-71. Epub 2005 Jul 21. [PubMed Link Image]
  6. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  7. 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]
  8. Antonyuk SV, Strange RW, Marklund SL, Hasnain SS: The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. J Mol Biol. 2009 May 1;388(2):310-26. Epub 2009 Mar 14. [PubMed Link Image]
  9. Sandstrom J, Nilsson P, Karlsson K, Marklund SL: 10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain. J Biol Chem. 1994 Jul 22;269(29):19163-6. [PubMed Link Image]
  10. Yamada H, Yamada Y, Adachi T, Goto H, Ogasawara N, Futenma A, Kitano M, Hirano K, Kato K: Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum. Jpn J Hum Genet. 1995 Jun;40(2):177-84. [PubMed Link Image]
  11. Adachi T, Yamada H, Yamada Y, Morihara N, Yamazaki N, Murakami T, Futenma A, Kato K, Hirano K: Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface. Biochem J. 1996 Jan 1;313 ( Pt 1):235-9. [PubMed Link Image]
  12. Adachi T, Morihara N, Yamazaki N, Yamada H, Futenma A, Kato K, Hirano K: An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases. J Biochem. 1996 Jul;120(1):184-8. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 8855
Enzyme 36 Name OTTHUMP00000017001
Enzyme 36 Synonyms Not Available
Enzyme 36 Gene Name DDO
Enzyme 36 Protein Sequence >OTTHUMP00000017001
MRPARHWETRFGARDFGGFQDCFFRDRLMDTARIAVVGAGVVGLSTAVCISKLVPRCSVT
IISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLV
SGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEK
RIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVE
HFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIR
EKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHAL
RTPIPKSNL
Enzyme 36 Number of Residues 369
Enzyme 36 Molecular Weight 40993
Enzyme 36 Theoretical pI 8.28
Enzyme 36 GO Classification
Function
  • D-amino-acid oxidase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 36 General Function Amino acid transport and metabolism
Enzyme 36 Specific Function Not Available
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals Not Available
Enzyme 36 Transmembrane Regions Not Available
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 57208418 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q5JXM5 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name Q5JXM5_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1110 bp
ATGAGACCAGCCAGGCACTGGGAAACAAGGTTTGGTGCCAGAGATTTTGGTGGCTTCCAA
GACTGCTTTTTCAGAGACAGGCTCATGGACACAGCACGGATTGCAGTTGTCGGGGCAGGT
GTGGTGGGGCTCTCCACGGCTGTGTGCATCTCCAAACTGGTGCCCCGATGCTCCGTTACC
ATCATTTCAGACAAGTTTACTCCAGATACCACCAGTGATGTGGCAGCCGGAATGCTTATT
CCTCACACTTATCCAGATACACCCATTCACACGCAGAAGCAGTGGTTCAGAGAAACCTTT
AATCACCTCTTTGCAATTGCCAATTCTGCAGAAGCTGGAGATGCTGGTGTTCATTTGGTA
TCAGGTTGGCAGATATTTCAGAGCACTCCGACTGAAGAAGTGCCATTCTGGGCTGACGTG
GTTCTGGGATTTCGAAAGATGACTGAGGCTGAGCTGAAGAAATTCCCCCAGTATGTGTTT
GGTCAGGCTTTTACAACCCTGAAATGTGAATGCCCTGCCTACCTCCCGTGGTTGGAGAAA
AGGATAAAGGGAAGTGGAGGCTGGACACTCACTCGGCGAATAGAAGACCTGTGGGAACTT
CATCCGTCCTTTGACATCGTGGTCAACTGTTCAGGCCTTGGAAGCAGACAGCTTGCAGGA
GACTCAAAGATTTTCCCTGTAAGGGGCCAAGTCCTCCAAGTTCAGGCTCCCTGGGTGGAG
CATTTTATCCGAGATGGCAGTGGGCTGACATATATTTATCCTGGTACATCCCATGTAACC
CTAGGTGGAACTAGGCAAAAAGGGGACTGGAATCTGTCCCCGGATGCAGAAAATAGCAGA
GAGATTCTTTCCCGATGCTGTGCTCTGGAGCCCTCCCTCCACGGAGCCTGCAACATCAGG
GAGAAGGTGGGCTTGAGGCCCTACAGGCCAGGCGTGCGACTGCAGACAGAGCTCCTTGCG
CGAGATGGACAGAGGCTGCCTGTAGTCCACCACTATGGCCATGGGAGTGGGGGCATCTCA
GTGCACTGGGGCACTGCTCTGGAGGCCGCCAGGCTGGTGAGCGAGTGTGTCCATGCCCTC
AGGACCCCCATTCCCAAGTCAAACCTGTAG
Enzyme 36 GenBank Gene ID AL050350 Link Image
Enzyme 36 GeneCard ID DDO Link Image
Enzyme 36 GenAtlas ID DDO Link Image
Enzyme 36 HGNC ID HGNC:2727 Link Image
Enzyme 36 Chromosome Location 6
Enzyme 36 Locus 6q21
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References Not Available
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 12689
Enzyme 37 Name Dual oxidase 1
Enzyme 37 Synonyms
  1. Large NOX 1
  2. Long NOX 1
  3. NADPH thyroid oxidase 1
  4. Thyroid oxidase 1
Enzyme 37 Gene Name DUOX1
Enzyme 37 Protein Sequence >Dual oxidase 1
MGFCLALAWTLLVGAWTPLGAQNPISWEVQRFDGWYNNLMEHRWGSKGSRLQRLVPASYA
DGVYQPLGEPHLPNPRDLSNTISRGPAGLASLRNRTVLGVFFGYHVLSDLVSVETPGCPA
EFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDPANQVTGWLDGSAIYG
SSHSWSDALRSFSRGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGN
REPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFL
QKTLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGVINRNSSVSRA
LRVCNSYWSREHPSLQSAEDVDALLLGMASQIAEREDHVLVEDVRDFWPGPLKFSRTDHL
ASCLQRGRDLGLPSYTKARAALGLSPITRWQDINPALSRSNDTVLEATAALYNQDLSWLE
LLPGGLLESHRDPGPLFSTIVLEQFVRLRDGDRYWFENTRNGLFSKKEIEEIRNTTLQDV
LVAVINIDPSALQPNVFVWHKGDPCPQPRQLSTEGLPACAPSVVRDYFEGSGFGFGVTIG
TLCCFPLVSLLSAWIVARLRMRNFKRLQGQDRQSIVSEKLVGGMEALEWQGHKEPCRPVL
VYLQPGQIRVVDGRLTVLRTIQLQPPQKVNFVLSSNRGRRTLLLKIPKEYDLVLLFNLEE
ERQALVENLRGALKESGLSIQEWELREQELMRAAVTREQRRHLLETFFRHLFSQVLDINQ
ADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREF
LDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISNNCLSKAQLAEVV
ESMFRESGFQDKEELTWEDFHFMLRDHNSELRFTQLCVKGVEVPEVIKDLCRRASYISQD
MICPSPRVSARCSRSDIETELTPQRLQCPMDTDPPQEIRRRFGKKVTSFQPLLFTEAHRE
KFQRSCLHQTVQQFKRFIENYRRHIGCVAVFYAIAGGLFLERAYYYAFAAHHTGITDTTR
VGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRLIASTAIVL
TVLHSVGHVVNVYLFSISPLSVLSCLFPGLFHDDGSELPQKYYWWFFQTVPGLTGVVLLL
ILAIMYVFASHHFRRRSFRGFWLTHHLYILLYVLLIIHGSFALIQLPRFHIFFLVPAIIY
GGDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHP
FTLTSAPHEDTLSLHIRAAGPWTTRLREIYSAPTGDRCARYPKLYLDGPFGEGHQEWHKF
EVSVLVGGGIGVTPFASILKDLVFKSSVSCQVFCKKIYFIWVTRTQRQFEWLADIIREVE
ENDHQDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEP
FFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLINRQDRTHFSHHYENF
Enzyme 37 Number of Residues 1551
Enzyme 37 Molecular Weight 177233.5
Enzyme 37 Theoretical pI 7.94
Enzyme 37 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • antioxidant activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleoside binding
  • oxidoreductase activity
  • peroxidase activity
  • purine nucleoside binding
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 37 General Function Involved in calcium ion binding
Enzyme 37 Specific Function Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions
  • NAD(P)H + H+ + O2 = NAD(P)+ + H2O2 [RN:R07171 R07172]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-21
Enzyme 37 Transmembrane Regions
  • 597-617 1045-1065 1081-1101 1149-1171 1189-1209 1227-1247 1249-1269
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 20149640 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9NRD9 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name DUOX1_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >4656 bp
ATGGGCTTCTGCCTGGCTCTAGCATGGACACTTCTGGTTGGGGCATGGACCCCTCTGGGA
GCTCAGAACCCCATTTCGTGGGAGGTGCAGCGATTTGATGGGTGGTACAACAACCTCATG
GAGCACAGATGGGGCAGCAAAGGCTCCCGGCTGCAGCGCCTGGTCCCAGCCAGCTATGCA
GATGGCGTGTACCAGCCCTTGGGAGAACCCCACCTGCCCAACCCCCGAGACCTTAGCAAC
ACCATCTCAAGGGGCCCTGCAGGGCTGGCCTCCCTGAGAAACCGCACAGTGTTGGGGGTC
TTCTTTGGCTATCACGTGCTTTCAGACCTGGTGAGCGTGGAAACTCCCGGCTGCCCCGCC
GAGTTCCTCAACATTCGCATCCCGCCCGGAGACCCCATGTTCGACCCCGACCAGCGCGGG
GACGTGGTGCTGCCCTTCCAGAGAAGCCGCTGGGACCCCGAGACCGGACGGAGTCCCAGC
AATCCCCGGGACCCGGCCAACCAGGTGACGGGCTGGCTGGACGGCAGCGCCATCTATGGT
TCCTCGCATTCCTGGAGCGACGCGCTGCGGAGCTTCTCCAGGGGACAGCTGGCGTCGGGG
CCCGACCCCGCTTTTCCCCGAGACTCGCAGAACCCCCTGCTCATGTGGGCGGCGCCCGAC
CCCGCCACCGGGCAGAACGGGCCCCGGGGGCTGTACGCCTTCGGGGCAGAGAGAGGGAAC
CGGGAACCCTTCCTGCAGGCGCTGGGCCTGCTCTGGTTCCGCTACCACAACCTGTGGGCG
CAGAGGCTGGCCCGCCAGCACCCAGACTGGGAGGACGAGGAGCTGTTCCAGCACGCACGC
AAGAGGGTCATCGCCACCTACCAGAACATCGCTGTGTATGAGTGGCTGCCCAGCTTCCTG
CAGAAAACACTCCCGGAGTATACAGGATACCGGCCATTTCTGGACCCCAGCATCTCCTCA
GAGTTCGTGGCGGCCTCTGAGCAGTTCCTGTCCACCATGGTGCCCCCTGGCGTCTACATG
AGAAATGCCAGCTGCCACTTCCAGGGGGTCATCAATCGGAACTCAAGTGTCTCCAGAGCT
CTCCGGGTCTGCAACAGCTACTGGAGCCGTGAGCACCCAAGCCTACAAAGTGCTGAAGAT
GTGGATGCACTGCTGCTGGGCATGGCCTCCCAGATCGCAGAGCGAGAGGACCATGTGTTG
GTTGAAGATGTGCGGGATTTCTGGCCTGGGCCACTGAAGTTTTCCCGCACAGACCACCTG
GCCAGCTGCCTGCAGCGGGGCCGGGATCTGGGCCTGCCCTCTTACACCAAGGCCAGGGCA
GCACTGGGCTTGTCTCCCATTACCCGCTGGCAGGACATCAACCCTGCACTCTCCCGGAGC
AATGACACTGTACTGGAGGCCACAGCTGCCCTGTACAACCAGGACTTATCCTGGCTAGAG
CTGCTCCCTGGGGGACTCCTGGAGAGCCACCGGGACCCTGGACCTCTGTTCAGCACCATC
GTCCTTGAACAATTTGTGCGGCTACGGGATGGTGACCGCTACTGGTTTGAGAACACCAGG
AATGGGCTGTTCTCCAAGAAGGAGATTGAAGAAATCCGAAATACCACCCTGCAGGACGTG
CTGGTCGCTGTTATCAACATTGACCCCAGTGCTCTGCAGCCCAATGTCTTTGTCTGGCAT
AAAGGAGACCCCTGTCCGCAGCCGAGACAGCTCAGCACTGAAGGCCTGCCAGCGTGTGCT
CCCTCTGTTGTTCGTGACTATTTTGAGGGCAGTGGATTTGGCTTCGGGGTCACCATCGGG
ACCCTCTGTTGCTTCCCTTTGGTGAGCCTGCTCAGTGCCTGGATTGTTGCCCGGCTCCGG
ATGAGAAATTTCAAGAGGCTCCAGGGCCAGGACCGCCAGAGCATCGTGTCTGAGAAGCTC
GTGGGAGGCATGGAAGCTTTGGAATGGCAAGGCCACAAGGAGCCCTGCCGGCCCGTGCTT
GTGTACCTGCAGCCCGGGCAGATCCGTGTGGTAGATGGCAGGCTCACCGTGCTCCGCACC
ATCCAGCTGCAGCCTCCACAGAAGGTCAACTTCGTCCTGTCCAGCAACCGTGGACGCCGC
ACTCTGCTGCTCAAGATCCCCAAGGAGTATGACCTGGTGCTGCTGTTTAACTTGGAGGAA
GAGCGGCAGGCGCTGGTGGAAAATCTCCGGGGAGCTCTGAAGGAGAGCGGGTTGAGCATC
CAGGAGTGGGAGCTGCGGGAGCAGGAGCTGATGAGAGCAGCTGTGACACGGGAGCAGCGG
AGGCACCTCCTGGAGACCTTTTTCAGGCACCTTTTCTCCCAGGTGCTGGACATCAACCAG
GCCGACGCAGGGACCCTGCCCCTGGACTCCTCCCAGAAGGTGCGGGAGGCCCTGACCTGT
GAGCTGAGCAGGGCCGAGTTTGCCGAGTCCCTGGGCCTCAAGCCCCAGGACATGTTTGTG
GAGTCCATGTTCTCTCTGGCTGACAAGGATGGCAATGGCTACCTGTCCTTCCGAGAGTTC
CTGGACATCCTGGTGGTCTTCATGAAAGGCTCTCCTGAGGAAAAGTCTCGCCTTATGTTC
CGCATGTACGACTTTGATGGGAATGGCCTCATTTCCAAGGATGAGTTCATCAGGATGCTG
AGATCCTTCATCGAGATCTCCAACAACTGCCTGTCCAAGGCCCAGCTGGCTGAGGTGGTG
GAGTCCATGTTCCGGGAGTCGGGATTCCAGGACAAGGAGGAACTGACATGGGAAGATTTT
CACTTCATGCTGCGGGACCACAATAGCGAGCTCCGCTTCACGCAGCTCTGTGTCAAAGGG
GTGGAGGTGCCTGAAGTCATCAAGGACCTCTGCCGGCGAGCCTCCTACATCAGCCAGGAT
ATGATCTGTCCCTCTCCCAGAGTGAGTGCCCGCTGTTCCCGCAGCGACATTGAGACTGAG
TTGACACCTCAGAGACTGCAGTGCCCCATGGACACAGACCCTCCCCAGGAGATTCGGCGG
AGGTTTGGCAAGAAGGTAACGTCATTCCAGCCCTTGCTGTTCACTGAGGCGCACCGAGAG
AAGTTCCAACGCAGCTGTCTCCACCAGACGGTGCAACAGTTCAAGCGCTTCATTGAGAAC
TACCGGCGCCACATCGGCTGCGTGGCCGTGTTCTACGCCATCGCTGGGGGGCTTTTCCTG
GAGAGGGCCTACTACTACGCCTTTGCCGCACATCACACGGGCATCACAGACACCACCCGC
GTGGGAATCATCCTGTCGCGGGGCACAGCAGCCAGCATCTCTTTCATGTTCTCCTACATC
TTGCTCACCATGTGCCGCAACCTCATCACCTTCCTGCGAGAAACCTTCCTCAACCGCTAC
GTGCCCTTCGACGCCGCCGTGGACTTCCATCGCCTCATTGCCTCCACCGCCATCGTCCTC
ACAGTCTTACACAGTGTGGGCCATGTGGTGAATGTGTACCTGTTCTCCATCAGCCCCCTC
AGCGTCCTCTCTTGCCTCTTTCCTGGCCTCTTCCATGATGATGGGTCTGAGCTCCCCCAG
AAGTATTACTGGTGGTTCTTCCAGACCGTACCAGGCCTCACGGGGGTTGTGCTGCTCCTG
ATCCTGGCCATCATGTATGTCTTTGCCTCCCACCACTTCCGCCGCCGCAGTTTCCGGGGC
TTCTGGCTGACCCACCACCTCTACATCCTGCTCTATGTCCTGCTCATCATCCATGGTAGC
TTTGCCCTGATCCAGCTGCCCCGTTTCCACATCTTCTTCCTGGTCCCAGCAATCATCTAT
GGGGGCGACAAGCTGGTGAGCCTGAGCCGGAAGAAGGTGGAGATCAGCGTGGTGAAGGCG
GAGCTGCTGCCCTCAGGAGTGACCCACCTGCGGTTCCAGCGGCCCCAGGGCTTTGAGTAC
AAGTCAGGGCAGTGGGTGCGGATCGCTTGCCTGGCTCTGGGGACCACCGAGTACCACCCC
TTCACACTGACCTCTGCGCCCCATGAGGACACGCTTAGCCTGCACATCCGGGCAGCAGGG
CCCTGGACCACTCGCCTCAGGGAGATCTACTCAGCCCCGACGGGTGACAGATGTGCCAGA
TACCCAAAGCTGTACCTTGATGGACCATTTGGAGAGGGCCACCAGGAGTGGCATAAGTTT
GAGGTGTCAGTGTTAGTGGGAGGGGGCATTGGGGTCACCCCTTTTGCCTCCATCCTCAAA
GACCTGGTCTTCAAGTCATCCGTCAGCTGCCAAGTGTTCTGTAAGAAGATCTACTTCATC
TGGGTGACGCGGACCCAGCGTCAGTTTGAGTGGCTGGCTGACATCATCCGAGAGGTGGAG
GAGAATGACCACCAGGACCTGGTGTCTGTGCACATCTACATCACCCAGCTGGCTGAGAAG
TTCGACCTCAGGACCACTATGCTGTACATCTGTGAGCGGCACTTCCAGAAGGTTCTGAAC
CGGAGTCTATTCACAGGCCTGCGCTCCATCACCCACTTTGGCCGTCCCCCCTTTGAGCCC
TTCTTCAACTCCCTGCAGGAGGTCCACCCCCAGGTCCGGAAGATCGGGGTGTTTAGCTGT
GGCCCCCCTGGCATGACCAAGAATGTGGAAAAGGCCTGTCAGCTCATCAACAGGCAGGAC
CGGACTCACTTCTCCCACCATTATGAGAACTTCTAG
Enzyme 37 GenBank Gene ID NM_017434.3 Link Image
Enzyme 37 GeneCard ID DUOX1 Link Image
Enzyme 37 GenAtlas ID DUOX1 Link Image
Enzyme 37 HGNC ID HGNC:3062 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 15q15.3
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. De Deken X, Wang D, Many MC, Costagliola S, Libert F, Vassart G, Dumont JE, Miot F: Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J Biol Chem. 2000 Jul 28;275(30):23227-33. [PubMed Link Image]
  2. Edens WA, Sharling L, Cheng G, Shapira R, Kinkade JM, Lee T, Edens HA, Tang X, Sullards C, Flaherty DB, Benian GM, Lambeth JD: Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. J Cell Biol. 2001 Aug 20;154(4):879-91. [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. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [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. De Deken X, Wang D, Dumont JE, Miot F: Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system. Exp Cell Res. 2002 Feb 15;273(2):187-96. [PubMed Link Image]
  7. Geiszt M, Witta J, Baffi J, Lekstrom K, Leto TL: Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. FASEB J. 2003 Aug;17(11):1502-4. Epub 2003 Jun 3. [PubMed Link Image]
  8. Schwarzer C, Machen TE, Illek B, Fischer H: NADPH oxidase-dependent acid production in airway epithelial cells. J Biol Chem. 2004 Aug 27;279(35):36454-61. Epub 2004 Jun 21. [PubMed Link Image]
  9. Harper RW, Xu C, Eiserich JP, Chen Y, Kao CY, Thai P, Setiadi H, Wu R: Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium. FEBS Lett. 2005 Aug 29;579(21):4911-7. [PubMed Link Image]
  10. 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]
  11. Ameziane-El-Hassani R, Morand S, Boucher JL, Frapart YM, Apostolou D, Agnandji D, Gnidehou S, Ohayon R, Noel-Hudson MS, Francon J, Lalaoui K, Virion A, Dupuy C: Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity. J Biol Chem. 2005 Aug 26;280(34):30046-54. Epub 2005 Jun 22. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 13058
Enzyme 38 Name Growth-inhibiting protein 16
Enzyme 38 Synonyms
  1. Hydroxyacid oxidase 2
  2. Long chain, isoform CRA_b
Enzyme 38 Gene Name GIG16
Enzyme 38 Protein Sequence >Growth-inhibiting protein 16
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDT
RTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAA
PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLT
DLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQG
IIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG
RPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
Enzyme 38 Number of Residues 351
Enzyme 38 Molecular Weight 38839
Enzyme 38 Theoretical pI 7.69
Enzyme 38 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 38 General Function Energy production and conversion
Enzyme 38 Specific Function Not Available
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 46981963 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q2TU86 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name Q2TU86_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence Not Available
Enzyme 38 GenBank Gene ID AY513277 Link Image
Enzyme 38 GeneCard ID Q2TU86 Link Image
Enzyme 38 GenAtlas ID GIG16 Link Image
Enzyme 38 HGNC ID HGNC:4810 Link Image
Enzyme 38 Chromosome Location Not Available
Enzyme 38 Locus Not Available
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References Not Available
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 13995
Enzyme 39 Name Prenylcysteine oxidase 1
Enzyme 39 Synonyms
  1. Prenylcysteine lyase
Enzyme 39 Gene Name PCYOX1
Enzyme 39 Protein Sequence >Prenylcysteine oxidase 1
MGRVVAELVSSLLGLWLLLCSCGCPEGAELRAPPDKIAIIGAGIGGTSAAYYLRQKFGKD
VKIDLFEREEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQASGGLLGI
YNGETLVFEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVE
KLLHALGGDDFLGMLNRTLLETLQKAGFSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSL
SCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEKTKTKYTGNPTKMYEVVYQIG
TETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSR
PIDKFGLNTVLTTDNSDLFINSIGIVPSVREKEDPEPSTDGTYVWKIFSQETLTKAQILK
LFLSYDYAVKKPWLAYPHYKPPEKCPSIILHDRLYYLNGIECAASAMEMSAIAAHNAALL
AYHRWNGHTDMIDQDGLYEKLKTEL
Enzyme 39 Number of Residues 505
Enzyme 39 Molecular Weight 56639.7
Enzyme 39 Theoretical pI 6.10
Enzyme 39 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
  • prenylcysteine catabolic process
  • prenylcysteine metabolic process
Component
Enzyme 39 General Function Involved in oxidoreductase activity
Enzyme 39 Specific Function Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2 [RN:R07360]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-27
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 166795301 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q9UHG3 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name PCYOX_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1518 bp
ATGGGGCGCGTCGTCGCGGAGCTCGTCTCCTCGCTGCTGGGGTTGTGGCTGTTGCTGTGC
AGCTGCGGATGCCCCGAGGGCGCCGAGCTGCGTGCTCCGCCAGATAAAATCGCGATTATT
GGAGCCGGAATTGGTGGCACTTCAGCAGCCTATTACCTGCGGCAGAAATTTGGGAAAGAT
GTGAAGATAGACCTGTTTGAAAGAGAAGAGGTCGGGGGCCGCCTGGCTACCATGATGGTG
CAGGGGCAAGAATACGAGGCAGGAGGTTCTGTCATCCATCCTTTAAATCTGCACATGAAA
CGTTTTGTCAAAGACCTGGGTCTCTCTGCTGTTCAGGCCTCTGGTGGCCTACTGGGGATA
TATAATGGAGAGACTCTGGTATTTGAGGAGAGCAACTGGTTCATAATTAACGTGATTAAA
TTAGTTTGGCGCTATGGATTTCAATCCCTCCGTATGCACATGTGGGTAGAGGACGTGTTA
GACAAGTTCATGAGGATCTACCGCTACCAGTCTCATGACTATGCCTTCAGTAGTGTCGAA
AAATTACTTCATGCTCTAGGAGGAGATGACTTCCTTGGAATGCTTAATCGAACACTTCTT
GAAACCTTGCAAAAGGCCGGCTTTTCTGAGAAGTTCCTCAATGAAATGATTGCTCCTGTT
ATGAGGGTCAATTATGGCCAAAGCACGGACATCAATGCCTTTGTGGGGGCGGTGTCACTG
TCCTGTTCTGATTCTGGCCTTTGGGCAGTAGAAGGTGGCAATAAACTTGTTTGCTCAGGG
CTTCTGCAGGCATCCAAAAGCAATCTTATATCTGGCTCAGTAATGTACATCGAGGAGAAA
ACAAAGACCAAGTACACAGGAAATCCAACAAAGATGTATGAAGTGGTCTACCAAATTGGA
ACTGAGACTCGTTCAGACTTCTATGACATCGTCTTGGTGGCCACTCCGTTGAATCGAAAA
ATGTCGAATATTACTTTTCTCAACTTTGATCCTCCAATTGAGGAATTCCATCAATATTAT
CAACATATAGTGACAACTTTAGTTAAGGGGGAATTGAATACATCTATCTTTAGCTCTAGA
CCCATAGATAAATTTGGCCTTAATACAGTTTTAACCACTGATAATTCAGATTTGTTCATT
AACAGTATTGGGATTGTGCCCTCTGTGAGAGAAAAGGAAGATCCTGAGCCATCAACAGAT
GGAACATATGTTTGGAAGATCTTTTCCCAAGAAACTCTTACTAAAGCACAAATTTTAAAG
CTCTTTCTGTCCTATGATTATGCTGTGAAGAAGCCATGGCTTGCATATCCTCACTATAAG
CCCCCGGAGAAATGCCCCTCTATCATTCTCCATGATCGACTTTATTACCTCAATGGCATA
GAGTGTGCAGCAAGTGCCATGGAGATGAGTGCCATTGCAGCCCACAACGCTGCACTCCTT
GCCTATCACCGCTGGAACGGGCACACAGACATGATTGATCAGGATGGCTTATATGAGAAA
CTTAAAACTGAACTATGA
Enzyme 39 GenBank Gene ID NM_016297.3 Link Image
Enzyme 39 GeneCard ID PCYOX1 Link Image
Enzyme 39 GenAtlas ID PCYOX1 Link Image
Enzyme 39 HGNC ID HGNC:20588 Link Image
Enzyme 39 Chromosome Location 2
Enzyme 39 Locus 2p13.3
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Tschantz WR, Zhang L, Casey PJ: Cloning, expression, and cellular localization of a human prenylcysteine lyase. J Biol Chem. 1999 Dec 10;274(50):35802-8. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [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. 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. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  7. Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D: Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. Proteomics. 2007 Mar;7(6):868-74. [PubMed Link Image]
  8. 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]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 14625
Enzyme 40 Name NADPH oxidase activator 1
Enzyme 40 Synonyms
  1. NOX activator 1
  2. Antigen NY-CO-31
  3. NCF2-like protein
  4. P67phox-like factor
  5. p51-nox
Enzyme 40 Gene Name NOXA1
Enzyme 40 Protein Sequence >NADPH oxidase activator 1
MASLGDLVRAWHLGAQAVDRGDWARALHLFSGVPAPPARLCFNAGCVHLLAGDPEAALRA
FDQAVTKDTCMAVGFFQRGVANFQLARFQEALSDFWLALEQLRGHAAIDYTQLGLRFKLQ
AWEVLHNVASAQCQLGLWTEAASSLREAMSKWPEGSLNGLDSALDQVQRRGSLPPRQVPR
GEVFRPHRWHLKHLEPVDFLGKAKVVASAIPDDQGWGVRPQQPQGPGANHDARSLIMDSP
RAGTHQGPLDAETEVGADRCTSTAYQEQRPQVEQVGKQAPLSPGLPAMGGPGPGPCEDPA
GAGGAGAGGSEPLVTVTVQCAFTVALRARRGADLSSLRALLGQALPHQAQLGQLSYLAPG
EDGHWVPIPEEESLQRAWQDAAACPRGLQLQCRGAGGRPVLYQVVAQHSYSAQGPEDLGF
RQGDTVDVLCEVDQAWLEGHCDGRIGIFPKCFVVPAGPRMSGAPGRLPRSQQGDQP
Enzyme 40 Number of Residues 476
Enzyme 40 Molecular Weight 50933.1
Enzyme 40 Theoretical pI 6.50
Enzyme 40 GO Classification
Function
  • binding
Process
Component
Enzyme 40 General Function Involved in binding
Enzyme 40 Specific Function Functions as an activator of NOX1, a superoxide- producing NADPH oxidase. Functions in the production of reactive oxygen species (ROS) which participate in a variety of biological processes including host defense, hormone biosynthesis, oxygen sensing and signal transduction. May also activate CYBB/gp91phox and NOX3
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 30844228 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q86UR1 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name NOXA1_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1431 bp
ATGGCCTCTCTGGGGGACCTGGTGCGCGCCTGGCACCTGGGCGCGCAGGCTGTGGATCGT
GGGGACTGGGCCCGCGCCTTGCACCTCTTCTCGGGCGTCCCGGCGCCGCCCGCCAGGCTG
TGCTTCAACGCGGGCTGCGTGCACCTGCTGGCCGGGGACCCCGAGGCCGCGCTGCGGGCA
TTTGACCAAGCCGTGACCAAGGACACCTGCATGGCGGTTGGCTTCTTCCAGCGAGGAGTG
GCCAACTTCCAGCTGGCAAGGTTCCAGGAGGCTCTGTCTGACTTCTGGCTGGCCCTGGAG
CAGCTGAGGGGCCACGCTGCCATCGACTACACGCAGCTGGGCCTGCGGTTCAAGCTGCAA
GCCTGGGAGGTGCTACACAATGTGGCGTCGGCACAGTGCCAGCTGGGGCTCTGGACAGAG
GCGGCCAGCAGCCTAAGGGAGGCCATGTCCAAGTGGCCGGAGGGGTCCCTGAATGGCCTG
GACTCAGCCCTGGACCAAGTGCAGAGACGGGGCTCACTGCCGCCACGGCAGGTCCCCAGG
GGCGAGGTCTTCCGGCCCCACCGGTGGCACCTGAAGCACTTGGAGCCCGTGGATTTCCTG
GGCAAGGCCAAGGTGGTGGCCTCTGCCATCCCCGACGACCAGGGCTGGGGCGTCCGCCCT
CAGCAGCCACAGGGACCAGGAGCGAACCATGATGCCAGGTCCCTAATCATGGACTCCCCA
AGAGCTGGCACCCACCAGGGCCCCCTCGATGCAGAGACAGAGGTCGGTGCTGACCGCTGC
ACGTCGACTGCCTACCAGGAGCAGAGGCCCCAGGTGGAGCAAGTTGGCAAACAGGCTCCT
CTCTCCCCAGGGCTGCCGGCAATGGGGGGGCCTGGCCCCGGCCCCTGTGAGGACCCCGCG
GGTGCTGGGGGAGCAGGTGCAGGGGGCTCCGAGCCCCTGGTGACTGTCACCGTGCAGTGC
GCCTTCACAGTGGCCCTGAGGGCACGAAGAGGAGCCGACCTGTCCAGCCTGCGGGCACTG
CTGGGCCAAGCCCTCCCTCACCAGGCCCAGCTTGGGCAACTCAGTTACCTAGCCCCAGGT
GAGGACGGGCACTGGGTCCCCATCCCCGAGGAGGAGTCGCTGCAGAGGGCCTGGCAGGAC
GCAGCTGCCTGCCCCAGGGGGCTGCAGCTGCAGTGCAGGGGAGCCGGGGGTCGGCCGGTC
CTCTACCAGGTGGTGGCCCAGCACAGCTACTCCGCCCAGGGGCCAGAGGACCTGGGCTTC
CGACAGGGGGACACGGTGGACGTCCTGTGTGAAGTGGACCAGGCATGGCTGGAGGGCCAC
TGTGACGGCCGCATCGGCATCTTCCCCAAGTGCTTCGTGGTCCCCGCCGGCCCTCGGATG
TCAGGAGCCCCCGGCCGCCTGCCCCGATCCCAGCAGGGAGATCAGCCCTAA
Enzyme 40 GenBank Gene ID AB095031 Link Image
Enzyme 40 GeneCard ID NOXA1 Link Image
Enzyme 40 GenAtlas ID NOXA1 Link Image
Enzyme 40 HGNC ID HGNC:10668 Link Image
Enzyme 40 Chromosome Location 9
Enzyme 40 Locus 9q34.3
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Geiszt M, Lekstrom K, Witta J, Leto TL: Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J Biol Chem. 2003 May 30;278(22):20006-12. Epub 2003 Mar 25. [PubMed Link Image]
  2. 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]
  3. Valente AJ, El Jamali A, Epperson TK, Gamez MJ, Pearson DW, Clark RA: NOX1 NADPH oxidase regulation by the NOXA1 SH3 domain. Free Radic Biol Med. 2007 Aug 1;43(3):384-96. Epub 2007 Apr 29. [PubMed Link Image]
  4. 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]
  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. Scanlan MJ, Chen YT, Williamson B, Gure AO, Stockert E, Gordan JD, Tureci O, Sahin U, Pfreundschuh M, Old LJ: Characterization of human colon cancer antigens recognized by autologous antibodies. Int J Cancer. 1998 May 29;76(5):652-8. [PubMed Link Image]
  7. Cheng G, Lambeth JD: NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain. J Biol Chem. 2004 Feb 6;279(6):4737-42. Epub 2003 Nov 14. [PubMed Link Image]
  8. Cheng G, Ritsick D, Lambeth JD: Nox3 regulation by NOXO1, p47phox, and p67phox. J Biol Chem. 2004 Aug 13;279(33):34250-5. Epub 2004 Jun 4. [PubMed Link Image]
  9. Kawahara T, Kuwano Y, Teshima-Kondo S, Takeya R, Sumimoto H, Kishi K, Tsunawaki S, Hirayama T, Rokutan K: Role of nicotinamide adenine dinucleotide phosphate oxidase 1 in oxidative burst response to Toll-like receptor 5 signaling in large intestinal epithelial cells. J Immunol. 2004 Mar 1;172(5):3051-8. [PubMed Link Image]
  10. 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]
  11. Cheng G, Diebold BA, Hughes Y, Lambeth JD: Nox1-dependent reactive oxygen generation is regulated by Rac1. J Biol Chem. 2006 Jun 30;281(26):17718-26. Epub 2006 Apr 24. [PubMed Link Image]
  12. Miyano K, Ueno N, Takeya R, Sumimoto H: Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1. J Biol Chem. 2006 Aug 4;281(31):21857-68. Epub 2006 Jun 8. [PubMed Link Image]
  13. Ueyama T, Geiszt M, Leto TL: Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases. Mol Cell Biol. 2006 Mar;26(6):2160-74. [PubMed Link Image]
  14. Yamamoto A, Kami K, Takeya R, Sumimoto H: Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1). Biochem Biophys Res Commun. 2007 Jan 12;352(2):560-5. Epub 2006 Nov 20. [PubMed Link Image]
  15. Kim JS, Diebold BA, Babior BM, Knaus UG, Bokoch GM: Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding. J Biol Chem. 2007 Nov 30;282(48):34787-800. Epub 2007 Oct 3. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 14987
Enzyme 41 Name NADPH oxidase organizer 1
Enzyme 41 Synonyms
  1. NADPH oxidase regulatory protein
  2. Nox organizer 1
  3. Nox-organizing protein 1
  4. SH3 and PX domain-containing protein 5
Enzyme 41 Gene Name NOXO1
Enzyme 41 Protein Sequence >NADPH oxidase organizer 1
MAGPRYPVSVQGAALVQIKRLQTFAFSVRWSDGSDTFVRRSWDEFRQLKKTLKETFPVEA
GLLRRSDRVLPKLLGQASLDAPLLGRVGRTSRGLARLQLLETYSRRLLATAERVARSPTI
TGFFAPQPLDLEPALPPGSRVILPTPEEQPLSRAAGRLSIHSLEAQSLRCLQPFCTQDTR
DRPFQAQAQESLDVLLRHPSGWWLVENEDRQTAWFPAPYLEEAAPGQGREGGPSLGSSGP
QFCASRAYESSRADELSVPAGARVRVLETSDRGWWLCRYGDRAGLLPAVLLRPEGLGALL
SGTGFRGGDDPAGEARGFPEPSQATAPPPTVPTRPSPGAIQSRCCTVTRRALERRPRRQG
RPRGCVDSVPHPTTEQ
Enzyme 41 Number of Residues 376
Enzyme 41 Molecular Weight 41252.3
Enzyme 41 Theoretical pI 10.23
Enzyme 41 GO Classification
Function
  • binding
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
Component
Enzyme 41 General Function Involved in protein binding
Enzyme 41 Specific Function Constitutively potentiates the superoxide-generating activity of NOX1 and NOX3 and is required for the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. Isoform 3 is more potent than isoform 1 in activating NOX3. Together with NOXA1, may also substitute to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte NOX2/gp91phox superoxide-generating activity
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 41281828 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q8NFA2 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name NOXO1_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1131 bp
ATGGCAGGCCCCCGATACCCAGTTTCAGTGCAAGGGGCAGCCCTGGTGCAGATCAAGAGG
CTCCAAACGTTTGCCTTCTCTGTGCGCTGGTCAGACGGCAGCGACACCTTCGTGCGCAGG
AGTTGGGACGAATTCAGGCAGCTCAAGAAGACCCTCAAGGAGACCTTCCCGGTGGAGGCG
GGCCTGCTGCGGAGATCTGACCGCGTTCTCCCAAAGCTTCTCGGTCAGGCCAGCCTGGAT
GCACCACTGTTGGGACGCGTGGGGCGCACGAGCCGCGGCCTGGCGCGCCTGCAGCTGTTG
GAAACCTATTCTCGGAGGCTGCTGGCGACTGCAGAGCGCGTGGCACGGAGCCCGACGATC
ACTGGCTTCTTCGCACCGCAACCCCTGGACCTGGAGCCCGCGCTGCCACCCGGCAGCCGG
GTGATCCTGCCCACCCCAGAGGAGCAGCCTCTTTCTCGCGCTGCGGGCCGCCTCTCCATC
CACAGTCTGGAGGCTCAGAGCCTGCGCTGCCTGCAGCCCTTCTGTACCCAGGACACGCGG
GATAGGCCTTTTCAGGCGCAGGCCCAGGAGAGCCTGGACGTGCTGCTGCGGCACCCCTCA
GGCTGGTGGCTGGTGGAGAACGAAGACCGGCAGACCGCCTGGTTTCCAGCGCCCTACCTG
GAGGAGGCGGCCCCGGGCCAAGGCCGGGAGGGAGGCCCGTCCCTAGGGAGCAGCGGTCCC
CAGTTCTGTGCTTCCCGCGCCTACGAGAGCAGCCGCGCAGATGAGCTGTCCGTGCCCGCG
GGGGCGCGCGTGCGCGTGTTGGAAACGTCAGACCGCGGCTGGTGGCTATGCAGGTACGGC
GACCGGGCGGGCCTACTCCCCGCGGTGCTGCTGCGGCCGGAAGGGCTGGGCGCTCTCCTG
AGCGGGACGGGGTTCCGTGGAGGAGACGACCCGGCGGGTGAGGCCCGGGGCTTCCCTGAA
CCCTCCCAGGCCACCGCCCCTCCCCCCACCGTGCCCACCCGACCTTCGCCGGGCGCCATC
CAGAGCCGCTGCTGCACCGTCACACGCAGGGCCCTGGAGCGGCGCCCACGGCGCCAGGGC
CGCCCTCGAGGGTGCGTGGACTCTGTGCCGCACCCCACGACGGAGCAGTGA
Enzyme 41 GenBank Gene ID NM_172168.1 Link Image
Enzyme 41 GeneCard ID NOXO1 Link Image
Enzyme 41 GenAtlas ID NOXO1 Link Image
Enzyme 41 HGNC ID HGNC:19404 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 16p13.3
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Banfi B, Clark RA, Steger K, Krause KH: Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J Biol Chem. 2003 Feb 7;278(6):3510-3. Epub 2002 Dec 6. [PubMed Link Image]
  2. Geiszt M, Lekstrom K, Witta J, Leto TL: Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J Biol Chem. 2003 May 30;278(22):20006-12. Epub 2003 Mar 25. [PubMed Link Image]
  3. 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]
  4. Cheng G, Lambeth JD: NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain. J Biol Chem. 2004 Feb 6;279(6):4737-42. Epub 2003 Nov 14. [PubMed Link Image]
  5. Cheng G, Lambeth JD: Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3. Gene. 2005 Aug 15;356:118-26. [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. Banfi B, Malgrange B, Knisz J, Steger K, Dubois-Dauphin M, Krause KH: NOX3, a superoxide-generating NADPH oxidase of the inner ear. J Biol Chem. 2004 Oct 29;279(44):46065-72. Epub 2004 Aug 23. [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. Park HS, Park D, Bae YS: Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1. Biochem Biophys Res Commun. 2006 Jan 20;339(3):985-90. [PubMed Link Image]
  10. Yamamoto A, Kami K, Takeya R, Sumimoto H: Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1). Biochem Biophys Res Commun. 2007 Jan 12;352(2):560-5. Epub 2006 Nov 20. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 15208
Enzyme 42 Name Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a
Enzyme 42 Synonyms
  1. SubName: cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA
  2. SubName: cDNA, FLJ94465, Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1),mRNA
Enzyme 42 Gene Name HAO1
Enzyme 42 Protein Sequence >Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a
MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET
DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE
AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ
LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR
GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV
LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV
RKNPLAVSKI
Enzyme 42 Number of Residues 370
Enzyme 42 Molecular Weight 40923.9
Enzyme 42 Theoretical pI 8.29
Enzyme 42 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 42 General Function Involved in FMN binding
Enzyme 42 Specific Function Not Available
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 158259869 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID A8K058 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name A8K058_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1113 bp
ATGCTCCCCCGGCTAATTTGTATCAATGATTATGAACAACATGCTAAATCAGTACTTCCA
AAGTCTATATATGACTATTACAGGTCTGGGGCAAATGATGAAGAAACTTTGGCTGATAAT
ATTGCAGCATTTTCCAGATGGAAGCTGTATCCAAGGATGCTCCGGAATGTTGCTGAAACA
GATCTGTCGACTTCTGTTTTAGGACAGAGGGTCAGCATGCCAATATGTGTGGGGGCTACG
GCCATGCAGCGCATGGCTCATGTGGACGGCGAGCTTGCCACTGTGAGAGCCTGTCAGTCC
CTGGGAACGGGCATGATGTTGAGTTCCTGGGCCACCTCCTCAATTGAAGAAGTGGCGGAA
GCTGGTCCTGAGGCACTTCGTTGGCTGCAACTGTATATCTACAAGGACCGAGAAGTCACC
AAGAAGCTAGTGCGGCAGGCAGAGAAGATGGGCTACAAGGCCATATTTGTGACAGTGGAC
ACACCTTACCTGGGCAACCGTCTGGATGATGTGCGTAACAGATTCAAACTGCCGCCACAA
CTCAGGATGAAAAATTTTGAAACCAGTACTTTATCATTTTCTCCTGAGGAAAATTTTGGA
GACGACAGTGGACTTGCTGCATATGTGGCTAAAGCAATAGACCCATCTATCAGCTGGGAA
GATATCAAATGGCTGAGAAGACTGACATCATTGCCAATTGTTGCAAAGGGCATTTTGAGA
GGTGATGATGCCAGGGAGGCTGTTAAACATGGCTTGAATGGGATCTTGGTGTCGAATCAT
GGGGCTCGACAACTCGATGGGGTGCCAGCCACTATTGATGTTCTGCCAGAAATTGTGGAG
GCTGTGGAAGGGAAGGTGGAAGTCTTCCTGGACGGGGGTGTGCGGAAAGGCACTGATGTT
CTGAAAGCTCTGGCTCTTGGCGCCAAGGCTGTGTTTGTGGGGAGACCAATCGTTTGGGGC
TTAGCTTTCCAGGGGGAGAAAGGTGTTCAAGATGTCCTCGAGATACTAAAGGAAGAATTC
CGGTTGGCCATGGCTCTGAGTGGGTGCCAGAATGTGAAAGTCATCGACAAGACATTGGTG
AGGAAAAATCCTTTGGCCGTTTCCAAGATCTGA
Enzyme 42 GenBank Gene ID AK289423 Link Image
Enzyme 42 GeneCard ID HAO1 Link Image
Enzyme 42 GenAtlas ID HAO1 Link Image
Enzyme 42 HGNC ID HGNC:4809 Link Image
Enzyme 42 Chromosome Location 2
Enzyme 42 Locus 20p12
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 15226
Enzyme 43 Name Myeloperoxidase (Myeloperoxidase, isoform CRA_a)
Enzyme 43 Synonyms Not Available
Enzyme 43 Gene Name MPO
Enzyme 43 Protein Sequence >Myeloperoxidase (Myeloperoxidase, isoform CRA_a)
MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTS
LVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLH
VALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMC
NNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTD
QLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPND
PRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQL
GLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLL
REHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYR
SYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLE
GGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYN
AWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPL
LACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMS
NSYPRDFVNCSTLPALNLASWREAS
Enzyme 43 Number of Residues 745
Enzyme 43 Molecular Weight 83870
Enzyme 43 Theoretical pI 9.14
Enzyme 43 GO Classification
Function
  • antioxidant activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Not Available
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 120660232 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID A1L4B8 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name A1L4B8_HUMAN Link Image
Enzyme 43 PDB ID 1MYP Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >2238 bp
ATGGGGGTTCCCTTCTTCTCTTCTCTCAGATGCATGGTGGACTTAGGACCTTGCTGGGCT
GGGGGTCTCACTGCAGAGATGAAGCTGCTTCTGGCCCTAGCAGGGCTCCTGGCCATTCTG
GCCACGCCCCAGCCCTCTGAAGGTGCTGCTCCAGCTGTCCTGGGGGAGGTGGACACCTCG
TTGGTGCTGAGCTCCATGGAGGAGGCCAAGCAGCTGGTGGACAAGGCCTACAAGGAGCGG
CGGGAAAGCATCAAGCAGCGGCTTCGCAGCGGCTCAGCCAGCCCCATGGAACTCCTATCC
TACTTCAAGCAGCCGGTGGCAGCCACCAGGACGGCGGTGAGGGCCGCTGACTACCTGCAC
GTGGCTCTAGACCTGCTGGAGAGGAAGCTGCGGTCCCTGTGGCGAAGGCCATTCAATGTC
ACTGATGTGCTGACGCCCGCCCAGCTGAATGTGTTGTCCAAGTCAAGCGGCTGCGCCTAC
CAGGACGTGGGGGTGACTTGCCCGGAGCAGGACAAATACCGCACCATCACCGGGATGTGC
AACAACAGACGCAGCCCCACGCTGGGGGCCTCCAACCGTGCCTTTGTGCGCTGGCTGCCG
GCGGAGTATGAGGACGGCTTCTCTCTTCCCTACGGCTGGACGCCCGGGGTCAAGCGCAAC
GGCTTCCCGGTGGCTCTGGCTCGCGCGGTCTCCAACGAGATCGTGCGCTTCCCCACTGAT
CAGCTGACTCCGGACCAGGAGCGCTCACTCATGTTCATGCAATGGGGCCAGCTGTTGGAC
CACGACCTCGACTTCACCCCTGAGCCGGCCGCCCGGGCCTCCTTCGTCACTGGCGTCAAC
TGCGAGACCAGCTGCGTTCAGCAGCCGCCCTGCTTCCCGCTCAAGATCCCGCCCAATGAC
CCCCGCATCAAGAACCAAGCCGACTGCATCCCGTTCTTCCGCTCCTGCCCGGCTTGCCCC
GGGAGCAACATCACCATCCGCAACCAGATCAACGCGCTCACTTCCTTCGTGGACGCCAGC
ATGGTGTACGGCAGCGAGGAGCCCCTGGCCAGGAACCTGCGCAACATGTCCAACCAGCTG
GGGCTGCTGGCCGTCAACCAGCGCTTCCAAGACAACGGCCGGGCCCTGCTGCCCTTTGAC
AACCTGCACGATGACCCCTGTCTCCTCACCAACCGCTCAGCGCGCATCCCCTGCTTCCTG
GCAGGGGACACCCGTTCCAGTGAGATGCCCGAGCTCACCTCCATGCACACCCTCTTACTT
CGGGAGCACAACCGGCTGGCCACAGAGCTCAAGAGCCTGAACCCTAGGTGGGATGGGGAG
AGGCTCTACCAGGAAGCCCGGAAGATCGTGGGGGCCATGGTCCAGATCATCACTTACCGG
GACTACCTGCCCCTGGTGCTGGGGCCAACGGCCATGAGGAAGTACCTGCCCACGTACCGT
TCCTACAATGACTCAGTGGACCCACGCATCGCCAACGTCTTCACCAATGCCTTCCGCTAC
GGCCACACCCTCATCCAACCCTTCATGTTCCGCCTGGACAATCGGTACCAGCCCATGGAA
CCCAACCCCCGTGTCCCCCTCAGCAGGGTCTTTTTTGCCTCCTGGAGGGTCGTGCTGGAA
GGTGGCATTGACCCCATCCTCCGGGGCCTCATGGCCACCCCTGCCAAGCTGAATCGTCAG
AACCAAATTGCAGTGGATGAGATCCGGGAGCGATTGTTTGAGCAGGTCATGAGGATTGGG
CTGGACCTGCCTGCTCTGAACATGCAGCGCAGCAGGGACCACGGCCTCCCAGGATACAAT
GCCTGGAGGCGCTTCTGTGGGCTCCCGCAGCCTGAAACTGTGGGCCAGCTGGGCACGGTG
CTGAGGAACCTGAAATTGGCGAGGAAACTGATGGAGCAGTATGGCACGCCCAACAACATC
GACATCTGGATGGGCGGCGTGTCCGAGCCTCTGAAGCGCAAAGGCCGCGTGGGCCCACTC
CTCGCCTGCATCATCGGTACCCAGTTCAGGAAGCTCCGGGATGGTGATCGGTTTTGGTGG
GAGAACGAGGGTGTGTTCAGCATGCAGCAGCGACAGGCCCTGGCCCAGATCTCATTGCCC
CGGATCATCTGCGACAACACAGGCATCACCACCGTGTCTAAGAACAACATCTTCATGTCC
AACTCATATCCCCGGGACTTTGTCAACTGCAGTACACTTCCTGCATTGAACCTGGCTTCC
TGGAGGGAAGCCTCCTAG
Enzyme 43 GenBank Gene ID BC130476 Link Image
Enzyme 43 GeneCard ID A1L4B8 Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID Not Available
Enzyme 43 Chromosome Location 17
Enzyme 43 Locus 17q23.1
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 15227
Enzyme 44 Name cDNA FLJ76595, highly similar to Homo sapiens peroxiredoxin 6 (PRDX6), mRNA (Peroxiredoxin 6, isoform CRA_a)
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name PRDX6
Enzyme 44 Protein Sequence >cDNA FLJ76595, highly similar to Homo sapiens peroxiredoxin 6 (PRDX6), mRNA (Peroxiredoxin 6, isoform CRA_a)
MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPE
FAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPA
EKDEKGMPVTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVD
WKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP
Enzyme 44 Number of Residues 224
Enzyme 44 Molecular Weight 25035
Enzyme 44 Theoretical pI 6.29
Enzyme 44 GO Classification Not Available
Enzyme 44 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function Not Available
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 158259727 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID A8JZY7 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name A8JZY7_HUMAN Link Image
Enzyme 44 PDB ID 1PRX Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >675 bp
ATGCCCGGAGGTCTGCTTCTCGGGGACGTGGCTCCCAACTTTGAGGCCAATACCACCGTC
GGCCGCATCCGTTTCCACGACTTTCTGGGAGACTCATGGGGCATTCTCTTCTCCCACCCT
CGGGACTTTACCCCAGTGTGCACCACAGAGCTTGGCAGAGCTGCAAAGCTGGCACCAGAA
TTTGCCAAGAGGAATGTTAAGTTGATTGCCCTTTCAATAGACAGTGTTGAGGACCATCTT
GCCTGGAGCAAGGATATCAATGCTTACAATTGTGAAGAGCCCACAGAAAAGTTACCTTTT
CCCATCATCGATGATAGGAATCGGGAGCTTGCCATCCTGTTGGGCATGCTGGATCCAGCA
GAGAAGGATGAAAAGGGCATGCCTGTGACAGCTCGTGTGGTGTTTGTTTTTGGTCCTGAT
AAGAAGCTGAAGCTGTCTATCCTCTACCCAGCTACCACTGGCAGGAACTTTGATGAGATT
CTCAGGGTAGTCATCTCTCTCCAGCTGACAGCAGAAAAAAGGGTTGCCACCCCAGTTGAT
TGGAAGGATGGGGATAGTGTGATGGTCCTTCCAACCATCCCTGAAGAAGAAGCCAAAAAA
CTTTTCCCGAAAGGAGTCTTCACCAAAGAGCTCCCATCTGGCAAGAAATACCTCCGCTAC
ACACCCCAGCCTTAA
Enzyme 44 GenBank Gene ID AK289352 Link Image
Enzyme 44 GeneCard ID A8JZY7 Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID Not Available
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References Not Available
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 15475
Enzyme 45 Name Peroxisomal N1-acetyl-spermine/spermidine oxidase (PAO) (Polyamine oxidase (Exo-N4-amino), isoform CRA_a)
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name RP11-122K13.11
Enzyme 45 Protein Sequence >Peroxisomal N1-acetyl-spermine/spermidine oxidase (PAO) (Polyamine oxidase (Exo-N4-amino), isoform CRA_a)
MESTGSVGEAPGGPRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCF
GGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLVETGGHVGLPSVSYASSGA
SVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKEIGQHVAGWTEDEETRKLK
LAVLNSFFNLECCVSGTHSMDLVALAPFGEYTVLPGLDCTFSKGYQGLTNCMMAALPEDT
VVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAHHVIVTVPLGFLREHLDTFF
DPPLPAEKAEAIRKIGFGTNNKIFLEFEEPFWEPDCQLIQLVWEDTSPLEDAAPELQDAW
FRKLIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLCLTQVLRRVTGNPRLPAPK
SVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAGAQLQILFAGEATHRTFYS
TTHGALLSGWREADRLLSLWAPQVQQPRPRL
Enzyme 45 Number of Residues 511
Enzyme 45 Molecular Weight 55514
Enzyme 45 Theoretical pI 4.91
Enzyme 45 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 45 General Function Amino acid transport and metabolism
Enzyme 45 Specific Function Not Available
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
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 Q5VWY0 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name Q5VWY0_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence Not Available
Enzyme 45 GenBank Gene ID AL360181 Link Image
Enzyme 45 GeneCard ID Q5VWY0 Link Image
Enzyme 45 GenAtlas ID PAOX Link Image
Enzyme 45 HGNC ID HGNC:20837 Link Image
Enzyme 45 Chromosome Location Not Available
Enzyme 45 Locus Not Available
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References Not Available
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 16425
Enzyme 46 Name cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name MAOB
Enzyme 46 Protein Sequence >cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
Enzyme 46 Number of Residues 520
Enzyme 46 Molecular Weight 58764
Enzyme 46 Theoretical pI 7.55
Enzyme 46 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 46 General Function Amino acid transport and metabolism
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID B2R6R3 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name B2R6R3_HUMAN Link Image
Enzyme 46 PDB ID 2BK3 Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence Not Available
Enzyme 46 GenBank Gene ID AK312679 Link Image
Enzyme 46 GeneCard ID B2R6R3 Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 16461
Enzyme 47 Name cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c)
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name DAO
Enzyme 47 Protein Sequence >cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c)
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
Enzyme 47 Number of Residues 347
Enzyme 47 Molecular Weight 39475
Enzyme 47 Theoretical pI 6.84
Enzyme 47 GO Classification
Function
  • ATP binding
  • D-amino-acid oxidase activity
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
Enzyme 47 General Function Amino acid transport and metabolism
Enzyme 47 Specific Function Not Available
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID B2R7I5 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name B2R7I5_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID AK312995 Link Image
Enzyme 47 GeneCard ID B2R7I5 Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location 12
Enzyme 47 Locus 12q24
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References Not Available
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 16475
Enzyme 48 Name cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
Enzyme 48 Synonyms
  1. SubName: Pipecolic acid oxidase, isoform CRA_b
Enzyme 48 Gene Name PIPOX
Enzyme 48 Protein Sequence >cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL
Enzyme 48 Number of Residues 390
Enzyme 48 Molecular Weight 44067
Enzyme 48 Theoretical pI 8.54
Enzyme 48 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
  • sarcosine oxidase activity
Process
  • aromatic compound metabolism
  • cellular metabolism
  • electron transport
  • folic acid and derivative metabolism
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
  • tetrahydrofolate metabolism
Component
Enzyme 48 General Function Amino acid transport and metabolism
Enzyme 48 Specific Function Not Available
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions
  • sarcosine + H2O + O2 = glycine + formaldehyde + H2O2 [RN:R00610] ALL_REAC R00610
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein Not Available
Enzyme 48 UniProtKB/Swiss-Prot ID B3KNH0 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name B3KNH0_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence Not Available
Enzyme 48 GenBank Gene ID AK027498 Link Image
Enzyme 48 GeneCard ID B3KNH0 Link Image
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID Not Available
Enzyme 48 Chromosome Location 17
Enzyme 48 Locus 17q11.2
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References Not Available
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 16634
Enzyme 49 Name cDNA, FLJ95254, highly similar to Homo sapiens prenylcysteine lyase (PCL1), mRNA (Prenylcysteine oxidase 1)
Enzyme 49 Synonyms Not Available
Enzyme 49 Gene Name PCYOX1
Enzyme 49 Protein Sequence >cDNA, FLJ95254, highly similar to Homo sapiens prenylcysteine lyase (PCL1), mRNA (Prenylcysteine oxidase 1)
MGRVVAELVSSLLGLWLLLCSCGCPEGAELRAPPDKIAIIGAGIGGTSAAYYLRQKFGKD
VKIDLFEREEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQASGGLLGI
YNGETLVFEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVE
KLLHALGGDDFLGMLNRTLLETLQKAGFSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSL
SCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEKTKTKYTGNPTKMYEVVYQIG
TETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSR
PIDKFGLNTVLTTDNSDLFINSIGIVPSVREKEDPEPSTDGTYVWKIFSQETLTKAQILK
LFLSYDYAVKKPWLAYPHYKPPEKCPSIILHDRLYYLNGIECAASAMEMSAIAAHNAALL
AYHRWNGHTDMIDQDGLYEKLKTEL
Enzyme 49 Number of Residues 505
Enzyme 49 Molecular Weight 56641
Enzyme 49 Theoretical pI 6.10
Enzyme 49 GO Classification Not Available
Enzyme 49 General Function Not Available
Enzyme 49 Specific Function Not Available
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
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 B2RB14 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name B2RB14_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence Not Available
Enzyme 49 GenBank Gene ID AK314453 Link Image
Enzyme 49 GeneCard ID B2RB14 Link Image
Enzyme 49 GenAtlas ID Not Available
Enzyme 49 HGNC ID Not Available
Enzyme 49 Chromosome Location Not Available
Enzyme 49 Locus Not Available
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References Not Available
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 16642
Enzyme 50 Name cDNA, FLJ93564, highly similar to Homo sapiens superoxide dismutase 2, mitochondrial (SOD2), mRNA (Superoxide dismutase 2, mitochondrial, isoform CRA_b)
Enzyme 50 Synonyms Not Available
Enzyme 50 Gene Name SOD2
Enzyme 50 Protein Sequence >cDNA, FLJ93564, highly similar to Homo sapiens superoxide dismutase 2, mitochondrial (SOD2), mRNA (Superoxide dismutase 2, mitochondrial, isoform CRA_b)
MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVN
NLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEA
IKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLL
GIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
Enzyme 50 Number of Residues 222
Enzyme 50 Molecular Weight 24750
Enzyme 50 Theoretical pI 8.45
Enzyme 50 GO Classification
Function
  • binding
  • catalytic activity
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on superoxide radicals as acceptor
  • superoxide dismutase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • superoxide metabolism
Component
Enzyme 50 General Function Inorganic ion transport and metabolism
Enzyme 50 Specific Function Not Available
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein Not Available
Enzyme 50 UniProtKB/Swiss-Prot ID B2R7R1 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name B2R7R1_HUMAN Link Image
Enzyme 50 PDB ID 1LUV Link Image
Enzyme 50 PDB File Show
Enzyme 50 3D Structure
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence Not Available
Enzyme 50 GenBank Gene ID AK313082 Link Image
Enzyme 50 GeneCard ID B2R7R1 Link Image
Enzyme 50 GenAtlas ID Not Available
Enzyme 50 HGNC ID Not Available
Enzyme 50 Chromosome Location Not Available
Enzyme 50 Locus Not Available
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References Not Available
Enzyme 50 Metabolite References Not Available