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Human Metabolome Database Version 2.5

 

Showing metabocard for Methylmalonic acid (HMDB00202)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-13 12:54:24
Accession Number HMDB00202
Secondary Accession Numbers Not Available
Common Name Methylmalonic acid
Description A malonic acid derivative which is a vital intermediate in the metabolism of fat and protein. Abnormalities in methylmalonic acid metabolism lead to methylmalonic aciduria. This metabolic disease is attributed to a block in the enzymatic conversion of methylmalonyl CoA to succinyl CoA.
Synonyms
  1. 1,1-Ethanedicarboxylate
  2. 1,1-Ethanedicarboxylic acid
  3. 2-Methylmalonate
  4. 2-Methylmalonic acid
  5. Isosuccinate
  6. Isosuccinic acid
  7. Methylmalonate
  8. Methylmalonic acid
  9. Methylpropanedioate
  10. Methylpropanedioic acid
  11. methyl-Malonate
  12. methyl-Malonic acid
  13. methyl-Propanedioate
  14. methyl-Propanedioic acid
Chemical IUPAC Name 2-methylpropanedioic acid
Chemical Formula C4H6O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Dicarboxylic Acids
Sub Class
  • Short chain dicarboxylic acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 118.088
Monoisotopic Molecular Weight 118.026611
Isomeric SMILES CC(C(O)=O)C(O)=O
Canonical SMILES CC(C(O)=O)C(O)=O
KEGG Compound ID C02170 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Methylmalonic acid Link Image
NuGOwiki Link HMDB00202 Link Image
Metagene Link HMDB00202 Link Image
METLIN ID 3712 Link Image
PubChem Compound 487 Link Image
PubChem Substance 86442 Link Image
ChEBI ID 17453 Link Image
CAS Registry Number 516-05-2
InChI Identifier InChI=1/C4H6O4/c1-2(3(5)6)4(7)8/h2H,1H3,(H,5,6)(H,7,8)
Synthesis Reference Edamura, Koji; Arai, Takeshi. Malonic and methylmalonic acids from b-hydroxypropionic acids. Jpn. Kokai Tokkyo Koho (1979), 5 pp.
Melting Point (Experimental) 135 oC
Experimental Water Solubility 679.0 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 149.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.17 [Predicted by ALOGPS]; -0.1 [Predicted by PubChem via XLOGP]; -0.83 [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 1CW8 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Kidney
Liver
Concentrations (Normal)
Biofluid Blood
Value 0.200 (0.00-0.400) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Magera MJ, Helgeson JK, Matern D, Rinaldo P: Methylmalonic acid measured in plasma and urine by stable-isotope dilution and electrospray tandem mass spectrometry. Clin Chem. 2000 Nov;46(11):1804-10. [PubMed Link Image]
Biofluid Blood
Value 0.14 (0.04-0.26) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid Blood
Value 0.187 +/- 0.084 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Schneede J, Ueland PM: Automated assay of methylmalonic acid in serum and urine by derivatization with 1-pyrenyldiazomethane, liquid chromatography, and fluorescence detection. Clin Chem. 1993 Mar;39(3):392-9. [PubMed Link Image]
Biofluid Blood
Value 0.17 (0.073-0.27) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Allen RH, Stabler SP, Savage DG, Lindenbaum J: Elevation of 2-methylcitric acid I and II levels in serum, urine, and cerebrospinal fluid of patients with cobalamin deficiency. Metabolism. 1993 Aug;42(8):978-88. [PubMed Link Image]
Biofluid CSF
Value 0.51 +/- 0.13 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Serot JM, Barbe F, Arning E, Bottiglieri T, Franck P, Montagne P, Nicolas JP: Homocysteine and methylmalonic acid concentrations in cerebrospinal fluid: relation with age and Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2005 Nov;76(11):1585-7. [PubMed Link Image]
Biofluid CSF
Value 0.32 +/- 0.11 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Serot JM, Barbe F, Arning E, Bottiglieri T, Franck P, Montagne P, Nicolas JP: Homocysteine and methylmalonic acid concentrations in cerebrospinal fluid: relation with age and Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2005 Nov;76(11):1585-7. [PubMed Link Image]
Biofluid CSF
Value 0.40 (0.16-0.59) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Allen RH, Stabler SP, Savage DG, Lindenbaum J: Elevation of 2-methylcitric acid I and II levels in serum, urine, and cerebrospinal fluid of patients with cobalamin deficiency. Metabolism. 1993 Aug;42(8):978-88. [PubMed Link Image]
Biofluid Urine
Value 1.6 (0-3.60) umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Magera MJ, Helgeson JK, Matern D, Rinaldo P: Methylmalonic acid measured in plasma and urine by stable-isotope dilution and electrospray tandem mass spectrometry. Clin Chem. 2000 Nov;46(11):1804-10. [PubMed Link Image]
Biofluid Urine
Value 9.4 (0.1-79.4) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 29.9 (0.1-78.9) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 8.2 (1.5-30.8) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 3.7 (1.1-21.6) umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 1.8 (0.00-3.6) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Magera MJ, Helgeson JK, Matern D, Rinaldo P: Methylmalonic acid measured in plasma and urine by stable-isotope dilution and electrospray tandem mass spectrometry. Clin Chem. 2000 Nov;46(11):1804-10. [PubMed Link Image]
Biofluid Urine
Value 0.92 +/- 1.97 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 0.64 +/- 0.39 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 0.17 +/- 0.11 umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 2.51 +/- 1.01 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 1.58 (0.0-3.29) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 2.0 +/- 0.7 umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 4.0 +/- 0.9 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 2.50 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Blood
Value 22.0 (4.3-37.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Vitamin B12 deficiency
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid Blood
Value 0.480 +/- 0.062 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Kristensen MO, Gulmann NC, Christensen JE, Ostergaard K, Rasmussen K: Serum cobalamin and methylmalonic acid in Alzheimer dementia. Acta Neurol Scand. 1993 Jun;87(6):475-81. [PubMed Link Image]
Biofluid CSF
Value 0.30 +/- 0.12 uM
Age Elderly:>65 yrs old
Sex N/A
Condition Alzheimer's disease
Comments Not Available
References
  • Serot JM, Barbe F, Arning E, Bottiglieri T, Franck P, Montagne P, Nicolas JP: Homocysteine and methylmalonic acid concentrations in cerebrospinal fluid: relation with age and Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2005 Nov;76(11):1585-7. [PubMed Link Image]
Biofluid Urine
Value 16.0 (1.5-30.8) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Cobalamin malabsorption
Comments Not Available
References
Biofluid Urine
Value 275.0 (50.0-500.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Cobalamin malabsorption
Comments Not Available
References
Biofluid Urine
Value 7825.00 (150.00-15500.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Malonyl-Coa decarboxylase deficiency
Comments Not Available
References
Biofluid Urine
Value 325.00 (150.00-500.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Transcobalamin II deficiency
Comments Not Available
References
Associated Disorders
Condition References
Alzheimer's disease
Cobalamin malabsorption
Malonyl-Coa decarboxylase deficiency
Transcobalamin II deficiency
Vitamin B12 deficiency
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
OMIM ID
  • 104300 Link Image (Alzheimer's disease)
  • 248360 Link Image (Malonyl-Coa decarboxylase deficiency)
  • 275350 Link Image (Transcobalamin II deficiency)
Pathways
Name SMPDB Link KEGG Link
Propanoate Metabolism SMP00016 Link Image map00640 Link Image
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. van Asselt DZ, Karlietis MH, Poels PJ, de Jong JG, Wevers RA, Hoefnagels WH: Cerebrospinal fluid methylmalonic acid concentrations in neurological patients with low and normal serum cobalamin concentrations. Acta Neurol Scand. 1998 Jun;97(6):413-6. [PubMed Link Image]
  2. Magera MJ, Helgeson JK, Matern D, Rinaldo P: Methylmalonic acid measured in plasma and urine by stable-isotope dilution and electrospray tandem mass spectrometry. Clin Chem. 2000 Nov;46(11):1804-10. [PubMed Link Image]
  3. Nakamura E, Rosenberg LE, Tanaka K: Microdetermination of methylmalonic acid and other short chain dicarboxylic acids by gas chromatography: use in prenatal diagnosis of methylmalonic acidemia and in studies of isovaleric acidemia. Clin Chim Acta. 1976 Apr 15;68(2):127-40. [PubMed Link Image]
  4. Jakobs C, Sweetman L, Nyhan WL: Hydroxy acid metabolites of branched-chain amino acids in amniotic fluid. Clin Chim Acta. 1984 Jul 16;140(2):157-66. [PubMed Link Image]
  5. Coude MM, Charpentier C, Bonnefont JP, Cheron G, Kamoun P: Organic acids in aqueous humour and plasma: post mortem study in infants and diagnosis of enzymopathies. J Inherit Metab Dis. 1991;14(5):668-73. [PubMed Link Image]
  6. Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
  7. Aleszczyk J: [Connection between changing the vitamin and immune status and the character of the throat microflora in patients with chronic tonsillitis] Otolaryngol Pol. 2003;57(2):221-4. [PubMed Link Image]
  8. Nagarajan S, Enns GM, Millan MT, Winter S, Sarwal MM: Management of methylmalonic acidaemia by combined liver-kidney transplantation. J Inherit Metab Dis. 2005;28(4):517-24. [PubMed Link Image]
  9. Stabler SP, Marcell PD, Podell ER, Allen RH, Lindenbaum J: Assay of methylmalonic acid in the serum of patients with cobalamin deficiency using capillary gas chromatography-mass spectrometry. J Clin Invest. 1986 May;77(5):1606-12. [PubMed Link Image]
  10. Jellum E, Stokke O, Eldjarn L: Combined use of gas chromatography, mass spectrometry, and computer in diagnosis and studies of metabolic disorders. Clin Chem. 1972 Aug;18(8):800-9. [PubMed Link Image]
  11. Leupold D: [Methylmalonic aciduria. Classification, diagnosis and therapy (author's transl)] Klin Wochenschr. 1977 Jan 15;55(2):57-63. [PubMed Link Image]
  12. Vrethem M, Mattsson E, Hebelka H, Leerbeck K, Osterberg A, Landtblom AM, Balla B, Nilsson H, Hultgren M, Brattstrom L, Kagedal B: Increased plasma homocysteine levels without signs of vitamin B12 deficiency in patients with multiple sclerosis assessed by blood and cerebrospinal fluid homocysteine and methylmalonic acid. Mult Scler. 2003 Jun;9(3):239-45. [PubMed Link Image]
  13. Bennett MJ, Ragni MC, Hood I, Hale DE: Comparison of post-mortem urinary and vitreous humour organic acids. Ann Clin Biochem. 1992 Sep;29 ( Pt 5):541-5. [PubMed Link Image]
  14. Haurani FI, Hall CA, Rubin R: Megaloblastic anemia as a result of an abnormal transcobalamin II (Cardeza). J Clin Invest. 1979 Nov;64(5):1253-9. [PubMed Link Image]
  15. Frenkel EP, Kitchens RL: Applicability of an enzymatic quantitation of methylmalonic, propionic, and acetic acids in normal and megaloblastic states. Blood. 1977 Jan;49(1):125-37. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Aldehyde oxidase
  2. 4-trimethylaminobutyraldehyde dehydrogenase
  3. Alpha-aminoadipic semialdehyde dehydrogenase
  4. Aldehyde dehydrogenase family 1 member A3
  5. Aldehyde dehydrogenase, mitochondrial
  6. Fatty aldehyde dehydrogenase
  7. Aldehyde dehydrogenase X, mitochondrial
  8. Aldehyde oxidase 1
Enzyme 1 [top]
Enzyme 1 ID 5358
Enzyme 1 Name Aldehyde oxidase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name AOX1
Enzyme 1 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 1 Number of Residues 1338
Enzyme 1 Molecular Weight 147916.7
Enzyme 1 Theoretical pI 7.17
Enzyme 1 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 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 71773480 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q06278 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ADO_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID NM_001159.3 Link Image
Enzyme 1 GeneCard ID AOX1 Link Image
Enzyme 1 GenAtlas ID AOX1 Link Image
Enzyme 1 HGNC ID HGNC:553 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q33
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5526
Enzyme 2 Name 4-trimethylaminobutyraldehyde dehydrogenase
Enzyme 2 Synonyms
  1. TMABADH
  2. Aldehyde dehydrogenase E3 isozyme
  3. Aldehyde dehydrogenase family 9 member A1
  4. Gamma-aminobutyraldehyde dehydrogenase
  5. R-aminobutyraldehyde dehydrogenase
Enzyme 2 Gene Name ALDH9A1
Enzyme 2 Protein Sequence >4-trimethylaminobutyraldehyde dehydrogenase
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
Enzyme 2 Number of Residues 494
Enzyme 2 Molecular Weight 53801.5
Enzyme 2 Theoretical pI 5.61
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+ [RN:R03283]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 7248636 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P49189 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AL9A1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1485 bp
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCCGCGTG
GAGCCGGCGGACGCCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATA
GCTACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCT
GCTTTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCT
GCCAGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGC
AAGTCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTAT
GCGGGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGT
TATACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTT
CAGATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAA
CCTTCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGT
GTACCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGT
CAGCATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATC
ATGGAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCA
CTCATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAAC
TTCCTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATT
CTTGATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCC
CTTCTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTT
GGGTTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATAT
GTACCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAAT
TGCAGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTA
TCATTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCA
GCTGGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCT
GGGACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATAT
AAGAAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTG
AAGACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
Enzyme 2 GenBank Gene ID AF172093 Link Image
Enzyme 2 GeneCard ID ALDH9A1 Link Image
Enzyme 2 GenAtlas ID ALDH9A1 Link Image
Enzyme 2 HGNC ID HGNC:412 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1q23.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed Link Image]
  2. Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed Link Image]
  6. Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed Link Image]
  7. Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5528
Enzyme 3 Name Alpha-aminoadipic semialdehyde dehydrogenase
Enzyme 3 Synonyms
  1. Alpha-AASA dehydrogenase
  2. Aldehyde dehydrogenase family 7 member A1
  3. Antiquitin-1
  4. Betaine aldehyde dehydrogenase
  5. Delta1-piperideine-6-carboxylate dehydrogenase
  6. P6c dehydrogenase
Enzyme 3 Gene Name ALDH7A1
Enzyme 3 Protein Sequence >Alpha-aminoadipic semialdehyde dehydrogenase
MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWG
GRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDA
LREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIE
QWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLED
NKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN
NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVG
NPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHD
ASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGI
VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
Enzyme 3 Number of Residues 539
Enzyme 3 Molecular Weight 58486.7
Enzyme 3 Theoretical pI 8.09
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+ [RN:R03102 R03103]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 188035924 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P49419 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AL7A1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1620 bp
ATGTGGCGCCTTCCTCGCGCGCTGTGTGTGCACGCTGCAAAGACCAGCAAGCTCTCTGGA
CCTTGGAGCAGGCCTGCCGCCTTCATGTCCACTCTCCTCATCAATCAGCCCCAGTATGCG
TGGCTGAAAGAGCTGGGGCTCCGCGAGGAAAACGAGGGCGTGTATAATGGAAGCTGGGGA
GGCCGGGGAGAGGTTATTACGACCTATTGCCCTGCTAACAACGAGCCAATAGCAAGAGTC
CGACAGGCCAGTGTGGCAGACTATGAAGAAACTGTAAAGAAAGCAAGAGAAGCATGGAAA
ATCTGGGCAGATATTCCTGCTCCAAAACGAGGAGAAATAGTAAGACAGATTGGCGATGCC
TTGCGGGAGAAGATCCAAGTACTAGGAAGCTTGGTGTCTTTGGAGATGGGGAAAATCTTA
GTGGAAGGTGTGGGTGAAGTTCAGGAGTATGTGGATATCTGTGACTATGCTGTTGGTTTA
TCAAGGATGATTGGAGGACCTATCTTGCCTTCTGAAAGATCTGGCCATGCACTGATTGAG
CAGTGGAATCCCGTAGGCCTGGTTGGAATCATCACGGCATTCAATTTCCCTGTGGCAGTG
TATGGTTGGAACAACGCCATCGCCATGATCTGTGGAAATGTCTGCCTCTGGAAAGGAGCT
CCAACCACTTCCCTCATTAGTGTGGCTGTCACAAAGATAATAGCCAAGGTTCTGGAGGAC
AACAAGCTGCCTGGTGCAATTTGTTCCTTGACTTGTGGTGGAGCAGATATTGGCACAGCA
ATGGCCAAAGATGAACGAGTGAACCTGCTGTCCTTCACTGGGAGCACTCAGGTGGGAAAA
CAGGTGGGCCTGATGGTGCAGGAGAGGTTTGGGAGAAGTCTGTTGGAACTTGGAGGAAAC
AATGCCATTATTGCCTTTGAAGATGCAGACCTCAGCTTAGTTGTTCCATCAGCTCTCTTC
GCTGCTGTGGGAACAGCTGGCCAGAGGTGTACCACTGCGAGGCGACTGTTTATACATGAA
AGCATCCATGATGAGGTTGTAAACAGACTTAAAAAGGCCTATGCACAGATCCGAGTTGGG
AACCCATGGGACCCTAATGTTCTCTATGGGCCACTCCACACCAAGCAGGCAGTGAGCATG
TTTCTTGGAGCAGTGGAAGAAGCAAAGAAAGAAGGTGGCACAGTGGTCTATGGGGGCAAG
GTTATGGATCGCCCTGGAAATTATGTAGAACCGACAATTGTGACAGGTCTTGGCCACGAT
GCGTCCATTGCACACACAGAGACTTTTGCTCCGATTCTCTATGTCTTTAAATTCAAGAAT
GAAGAAGAGGTCTTTGCATGGAATAATGAAGTAAAACAGGGACTTTCAAGTAGCATCTTT
ACCAAAGATCTGGGCAGAATCTTTCGCTGGCTTGGACCTAAAGGATCAGACTGTGGCATT
GTAAATGTCAACATTCCAACAAGTGGGGCTGAGATTGGAGGTGCCTTTGGAGGAGAAAAG
CACACTGGTGGTGGCAGGGAGTCTGGCAGTGATGCCTGGAAACAGTACATGAGAAGGTCT
ACTTGTACTATCAACTACAGTAAAGACCTTCCTCTGGCCCAAGGAATCAAGTTTCAGTAA
Enzyme 3 GenBank Gene ID NM_001182.3 Link Image
Enzyme 3 GeneCard ID ALDH7A1 Link Image
Enzyme 3 GenAtlas ID ALDH7A1 Link Image
Enzyme 3 HGNC ID HGNC:877 Link Image
Enzyme 3 Chromosome Location 5
Enzyme 3 Locus 5q31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Lee P, Kuhl W, Gelbart T, Kamimura T, West C, Beutler E: Homology between a human protein and a protein of the green garden pea. Genomics. 1994 May 15;21(2):371-8. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Skvorak AB, Robertson NG, Yin Y, Weremowicz S, Her H, Bieber FR, Beisel KW, Lynch ED, Beier DR, Morton CC: An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics. 1997 Dec 1;46(2):191-9. [PubMed Link Image]
  6. Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V: Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. J Biol Chem. 2010 Jun 11;285(24):18452-63. Epub 2010 Mar 5. [PubMed Link Image]
  7. Mills PB, Struys E, Jakobs C, Plecko B, Baxter P, Baumgartner M, Willemsen MA, Omran H, Tacke U, Uhlenberg B, Weschke B, Clayton PT: Mutations in antiquitin in individuals with pyridoxine-dependent seizures. Nat Med. 2006 Mar;12(3):307-9. Epub 2006 Feb 19. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5529
Enzyme 4 Name Aldehyde dehydrogenase family 1 member A3
Enzyme 4 Synonyms
  1. Aldehyde dehydrogenase 6
  2. Retinaldehyde dehydrogenase 3
  3. RALDH-3
  4. RalDH3
Enzyme 4 Gene Name ALDH1A3
Enzyme 4 Protein Sequence >Aldehyde dehydrogenase family 1 member A3
MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
Enzyme 4 Number of Residues 512
Enzyme 4 Molecular Weight 56108.0
Enzyme 4 Theoretical pI 7.29
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 4 General Function Involved in oxidoreductase activity
Enzyme 4 Specific Function Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system
Enzyme 4 Pathways
Enzyme 4 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+ [RN:R00538 R00634]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 46621670 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P47895 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AL1A3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1539 bp
ATGGCCACCGCTAACGGGGCCGTGGAAAACGGGCAGCCGGACAGGAAGCCGCCGGCCCTG
CCGCGCCCCATCCGCAACCTGGAGGTCAAGTTCACCAAGATATTTATCAACAATGAATGG
CACGAATCCAAGAGTGGGAAAAAGTTTGCTACATGTAACCCTTCAACTCGGGAGCAAATA
TGTGAAGTGGAAGAAGGAGATAAGCCCGACGTGGACAAGGCTGTGGAGGCTGCACAGGTT
GCCTTCCAGAGGGGCTCGCCATGGCGCCGGCTGGATGCCCTGAGTCGTGGGCGGCTGCTG
CACCAGCTGGCTGACCTGGTGGAGAGGGACCGCGCCACCTTGGCCGCCCTGGAGACGATG
GATACAGGGAAGCCATTTCTTCATGCTTTTTTCATCGACCTGGAGGGCTGTATTAGAACC
CTCAGATACTTTGCAGGGTGGGCAGACAAAATCCAGGGCAAGACCATCCCCACAGATGAC
AACGTCGTGTGCTTCACCAGGCATGAGCCCATTGGTGTCTGTGGGGCCATCACTCCATGG
AACTTCCCCCTGCTGATGCTGGTGTGGAAGCTGGCACCCGCCCTCTGCTGTGGGAACACC
ATGGTCCTGAAGCCTGCGGAGCAGACACCTCTCACCGCCCTTTATCTCGGCTCTCTGATC
AAAGAGGCCGGGTTCCCTCCAGGAGTGGTGAACATTGTGCCAGGATTCGGGCCCACAGTG
GGAGCAGCAATTTCTTCTCACCCTCAGATCAACAAGATCGCCTTCACCGGCTCCACAGAG
GTTGGAAAACTGGTTAAAGAAGCTGCGTCCCGGAGCAATCTGAAGCGGGTGACGCTGGAG
CTGGGGGGGAAGAACCCCTGCATCGTGTGTGCGGACGCTGACTTGGACTTGGCAGTGGAG
TGTGCCCATCAGGGAGTGTTCTTCAACCAAGGCCAGTGTTGCACGGCAGCCTCCAGGGTG
TTCGTGGAGGAGCAGGTCTACTCTGAGTTTGTCAGGCGGAGCGTGGAGTATGCCAAGAAA
CGGCCCGTGGGAGACCCCTTCGATGTCAAAACAGAACAGGGGCCTCAGATTGATCAAAAG
CAGTTCGACAAAATCTTAGAGCTGATCGAGAGTGGGAAGAAGGAAGGGGCCAAGCTGGAA
TGCGGGGGCTCAGCCATGGAAGACAAGGGGCTCTTCATCAAACCCACTGTCTTCTCAGAA
GTCACAGACAACATGCGGATTGCCAAAGAGGAGATTTTCGGGCCAGTGCAACCAATACTG
AAGTTCAAAAGTATCGAAGAAGTGATAAAAAGAGCGAATAGCACCGACTATGGACTCACA
GCAGCCGTGTTCACAAAAAATCTCGACAAAGCCCTGAAGTTGGCTTCTGCCTTAGAGTCT
GGAACGGTCTGGATCAACTGCTACAACGCCCTCTATGCACAGGCTCCATTTGGTGGCTTT
AAAATGTCAGGAAATGGCAGAGAACTAGGTGAATACGCTTTGGCCGAATACACAGAAGTG
AAAACTGTCACCATCAAACTTGGCGACAAGAACCCCTGA
Enzyme 4 GenBank Gene ID BC069274 Link Image
Enzyme 4 GeneCard ID ALDH1A3 Link Image
Enzyme 4 GenAtlas ID ALDH1A3 Link Image
Enzyme 4 HGNC ID HGNC:409 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 15q26.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Hsu LC, Chang WC, Hiraoka L, Hsieh CL: Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6. Genomics. 1994 Nov 15;24(2):333-41. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5530
Enzyme 5 Name Aldehyde dehydrogenase, mitochondrial
Enzyme 5 Synonyms
  1. ALDH class 2
  2. ALDH-E2
  3. ALDHI
Enzyme 5 Gene Name ALDH2
Enzyme 5 Protein Sequence >Aldehyde dehydrogenase, mitochondrial
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Enzyme 5 Number of Residues 517
Enzyme 5 Molecular Weight 56380.9
Enzyme 5 Theoretical pI 7.05
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 An aldehyde + NAD(+) + H(2)O = an acid + NADH
Enzyme 5 Pathways
Enzyme 5 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 28606 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P05091 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Enzyme 5 PDB ID 1OF7 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1551 bp
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
Enzyme 5 GenBank Gene ID X05409 Link Image
Enzyme 5 GeneCard ID ALDH2 Link Image
Enzyme 5 GenAtlas ID ALDH2 Link Image
Enzyme 5 HGNC ID HGNC:404 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 12q24.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed Link Image]
  2. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed Link Image]
  3. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed Link Image]
  6. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed Link Image]
  7. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed Link Image]
  8. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  9. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  10. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed Link Image]
  11. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed Link Image]
  12. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed Link Image]
  13. Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5531
Enzyme 6 Name Fatty aldehyde dehydrogenase
Enzyme 6 Synonyms
  1. Aldehyde dehydrogenase 10
  2. Aldehyde dehydrogenase family 3 member A2
  3. Microsomal aldehyde dehydrogenase
Enzyme 6 Gene Name ALDH3A2
Enzyme 6 Protein Sequence >Fatty aldehyde dehydrogenase
MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQE
VITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQ
PLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDH
IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT
CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKI
AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLA
LYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS
HQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLV
KAEYY
Enzyme 6 Number of Residues 485
Enzyme 6 Molecular Weight 54847.4
Enzyme 6 Theoretical pI 7.99
Enzyme 6 GO Classification
Function
  • aldehyde dehydrogenase [NAD(P)+] activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • cellular aldehyde metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
Enzyme 6 General Function Involved in oxidoreductase activity
Enzyme 6 Specific Function Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length
Enzyme 6 Pathways
Enzyme 6 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 464-480
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID P51648 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AL3A2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1458 bp
ATGGAGCTCGAAGTCCGGCGGGTCCGACAGGCGTTCCTGTCCGGCCGGTCGCGACCTCTG
CGGTTTCGGCTGCAGCAGCTGGAGGCCCTGCGGAGGATGGTGCAGGAGCGCGAGAAGGAT
ATCCTGACGGCCATCGCCGCCGACCTGTGCAAGAGTGAATTCAATGTGTACAGTCAGGAA
GTCATTACTGTCCTTGGGGAAATTGATTTTATGCTTGAGAATCTTCCTGAATGGGTTACT
GCTAAACCAGTTAAGAAGAACGTGCTCACCATGCTGGATGAGGCCTATATTCAGCCACAG
CCTCTGGGAGTGGTGCTGATAATCGGAGCTTGGAATTACCCCTTCGTTCTCACCATTCAG
CCACTGATAGGAGCCATCGCTGCAGGAAATGCTGTGATTATAAAGCCTTCTGAACTGAGT
GAAAATACAGCCAAGATCTTGGCAAAGCTTCTCCCTCAGTATTTAGACCAGGATCTCTAT
ATTGTTATTAATGGTGGTGTTGAGGAAACCACGGAGCTCCTGAAGCAGCGATTTGACCAC
ATTTTCTATACGGGAAACACTGCGGTTGGCAAAATTGTCATGGAAGCTGCTGCCAAGCAT
CTGACCCCTGTGACTCTTGAACTGGGAGGGAAAAGTCCATGTTATATTGATAAAGATTGT
GACCTGGACATTGTTTGCAGACGCATAACCTGGGGAAAATACATGAATTGTGGCCAAACC
TGCATTGCACCCGACTATATTCTCTGTGAAGCATCCCTCCAAAATCAAATTGTATGGAAG
ATTAAGGAAACAGTGAAGGAATTTTATGGAGAAAATATAAAAGAGTCTCCTGATTATGAA
AGGATCATCAATCTTCGTCATTTTAAGAGGATACTAAGTTTGCTTGAAGGACAAAAGATA
GCTTTTGGTGGGGAGACTGATGAGGCCACACGCTACATAGCCCCAACAGTACTTACCGAT
GTTGATCCTAAAACCAAGGTGATGCAAGAAGAAATTTTTGGACCAATTCTTCCAATAGTG
CCTGTGAAAAATGTAGATGAGGCCATAAATTTCATAAATGAACGTGAAAAGCCTCTGGCT
CTTTATGTATTTTCGCATAACCATAAGCTCATCAAACGGATGATTGATGAGACATCCAGT
GGAGGTGTCACAGGCAATGACGTCATTATGCACTTCACGCTCAACTCTTTCCCATTTGGA
GGAGTGGGTTCCAGTGGGATGGGAGCTTATCACGGAAAACATAGTTTTGATACTTTTTCT
CATCAGCGTCCCTGTTTATTAAAAAGTTTAAAGAGAGAAGGTGCTAACAAACTCAGATAT
CCTCCCAACAGCCAGTCAAAGGTGGATTGGGGGAAATTTTTTCTCTTGAAACGGTTCAAC
AAAGAAAAACTCGGTCTCCTGTTGCTCACTTTCCTGGGTATTGTAGCCGCTGTGCTTGTC
AAGGCAGAATATTACTGA
Enzyme 6 GenBank Gene ID L47162 Link Image
Enzyme 6 GeneCard ID ALDH3A2 Link Image
Enzyme 6 GenAtlas ID ALDH3A2 Link Image
Enzyme 6 HGNC ID HGNC:403 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 17p11.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. De Laurenzi V, Rogers GR, Hamrock DJ, Marekov LN, Steinert PM, Compton JG, Markova N, Rizzo WB: Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. Nat Genet. 1996 Jan;12(1):52-7. [PubMed Link Image]
  2. Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG: Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Genomics. 1997 Jan 15;39(2):127-35. [PubMed Link Image]
  3. Chang C, Yoshida A: Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression. Genomics. 1997 Feb 15;40(1):80-5. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Sillen A, Jagell S, Wadelius C: A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden. Hum Genet. 1997 Aug;100(2):201-3. [PubMed Link Image]
  6. Sillen A, Anton-Lamprecht I, Braun-Quentin C, Kraus CS, Sayli BS, Ayuso C, Jagell S, Kuster W, Wadelius C: Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome. Hum Mutat. 1998;12(6):377-84. [PubMed Link Image]
  7. Rizzo WB, Carney G, Lin Z: The molecular basis of Sjogren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene. Am J Hum Genet. 1999 Dec;65(6):1547-60. [PubMed Link Image]
  8. Aoki N, Suzuki H, Ito K, Ito M: A novel point mutation of the FALDH gene in a Japanese family with Sjogren-Larsson syndrome. J Invest Dermatol. 2000 May;114(5):1065-6. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5532
Enzyme 7 Name Aldehyde dehydrogenase X, mitochondrial
Enzyme 7 Synonyms
  1. Aldehyde dehydrogenase 5
  2. Aldehyde dehydrogenase family 1 member B1
Enzyme 7 Gene Name ALDH1B1
Enzyme 7 Protein Sequence >Aldehyde dehydrogenase X, mitochondrial
MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
Enzyme 7 Number of Residues 517
Enzyme 7 Molecular Weight 57238.0
Enzyme 7 Theoretical pI 6.79
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 7 General Function Involved in oxidoreductase activity
Enzyme 7 Specific Function ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation
Enzyme 7 Pathways
Enzyme 7 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
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 P30837 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name AL1B1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1554 bp
ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCGCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGGATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAG
Enzyme 7 GenBank Gene ID BT007418 Link Image
Enzyme 7 GeneCard ID ALDH1B1 Link Image
Enzyme 7 GenAtlas ID ALDH1B1 Link Image
Enzyme 7 HGNC ID HGNC:407 Link Image
Enzyme 7 Chromosome Location 9
Enzyme 7 Locus 9p11.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 13071
Enzyme 8 Name Aldehyde oxidase 1
Enzyme 8 Synonyms
  1. SubName: Aldehyde oxidase 1, isoform CRA_b
  2. SubName: Aldeyde oxidase
Enzyme 8 Gene Name hAO
Enzyme 8 Protein Sequence >Aldehyde oxidase 1
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSER
MMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHA
YNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
Enzyme 8 Number of Residues 1338
Enzyme 8 Molecular Weight 147916.7
Enzyme 8 Theoretical pI 7.17
Enzyme 8 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 8 General Function Involved in oxidoreductase activity
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways
Enzyme 8 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 13516379 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9BYF0 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q9BYF0_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 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 8 GenBank Gene ID AB046692 Link Image
Enzyme 8 GeneCard ID hAO Link Image
Enzyme 8 GenAtlas ID hAO Link Image
Enzyme 8 HGNC ID HGNC:553 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T: Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. Biochem Biophys Res Commun. 2001 Apr 20;282(5):1194-200. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available