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Human Metabolome Database Version 2.5

 

Showing metabocard for 5-Hydroxyindoleacetic acid (HMDB00763)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-24 12:57:11
Accession Number HMDB00763
Secondary Accession Numbers Not Available
Common Name 5-Hydroxyindoleacetic acid
Description 5-hydroxyindoleacetic acid (5HIAA) is a breakdown product of serotonin that is excreted in the urine. Serotonin is a hormone found at high levels in many body tissues. Serotonin and 5HIAA are produced in excess amounts by carcinoid tumors, and levels of these substances may be measured in the urine to test for carcinoid tumors. (NCI)
Synonyms
  1. 5-Hydroxy-1H-indole-3-acetate
  2. 5-Hydroxy-1H-indole-3-acetic acid
  3. 5-Hydroxy-3-indolylacetate
  4. 5-Hydroxy-IAA
  5. 5-Hydroxyheteroauxin
  6. 5-Hydroxyindol-3-ylacetate
  7. 5-Hydroxyindol-3-ylacetic acid
  8. 5-Hydroxyindole-3-acetate
  9. 5-Hydroxyindole-3-acetic acid
  10. 5-Hydroxyindoleacetate
  11. 5-Hydroxyindoleacetic acid
  12. 5-Oxyindoleacetate
  13. 5-Oxyindoleacetic acid
  14. 5-hydroxy-Indole-3-acetate
  15. 5-hydroxy-Indole-3-acetic acid
  16. Hydroxyindoleacetate
  17. 5-HIAA
  18. 5HIAA
Chemical IUPAC Name 2-(5-hydroxy-1H-indol-3-yl)acetic acid
Chemical Formula C10H9NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Indoles and Indole Derivatives
Sub Class
  • Indole acids
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 191.183
Monoisotopic Molecular Weight 191.058243
Isomeric SMILES OC(=O)CC1=CNC2=CC=C(O)C=C12
Canonical SMILES OC(=O)CC1=CNC2=CC=C(O)C=C12
KEGG Compound ID C05635 Link Image
BioCyc ID 5-HYDROXYINDOLE_ACETATE Link Image
BiGG ID 46167 Link Image
Wikipedia Link 5-Hydroxyindoleacetic acid Link Image
NuGOwiki Link HMDB00763 Link Image
Metagene Link HMDB00763 Link Image
METLIN ID 2975 Link Image
PubChem Compound 1826 Link Image
PubChem Substance 3133455 Link Image
ChEBI ID Not Available
CAS Registry Number 54-16-0
InChI Identifier InChI=1/C10H9NO3/c12-7-1-2-9-8(4-7)6(5-11-9)3-10(13)14/h1-2,4-5,11-12H,3H2,(H,13,14)
Synthesis Reference Asero, B.; Colo, V. A.; Vercellone, A. Preparation of 5-hydroxy-3-indoleacetic acid. Farmaco, Edizione Scientifica (1956), 11 219-20.
Melting Point (Experimental) 161-163 oC
Experimental Water Solubility 24 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 56.9 mg/mL [MEYLAN,WM et al. (1996)]; 1.80 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.28 [Predicted by ALOGPS]; 1.1 [Predicted by PubChem via XLOGP]; 1.01 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
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
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Brain —
Central Nervous System —
Hippocampus —
Hypothalamus —
Liver —
Nerve Cells —
Platelet —
Spinal Cord —
Spleen —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 0.0516 +/- 0.0068 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid CSF
Value 0.143 +/- 0.045 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 0.61 +/- 0.06 uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shaywitz BA, Cohen DJ, Bowers MB: Reduced cerebrospinal fluid 5-hydroxyindoleacetic acid and homovanillic acid in children with epilepsy. Neurology. 1975 Jan;25(1):72-9. [PubMed Link Image]
Biofluid CSF
Value 0.4 +/- 0.07 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Eklundh T, Eriksson M, Sjoberg S, Nordin C: Monoamine precursors, transmitters and metabolites in cerebrospinal fluid: a prospective study in healthy male subjects. J Psychiatr Res. 1996 May-Jun;30(3):201-8. [PubMed Link Image]
Biofluid CSF
Value 0.307 (0.152-0.462) uM
Age Infant:0-1 yr old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid CSF
Value 0.025 +/- 0.011 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid CSF
Value 0.47 (0.15-0.80) uM
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Spaapen LJ, Bakker JA, Velter C, Loots W, Rubio-Gozalbo ME, Forget PP, Dorland L, De Koning TJ, Poll-The BT, Ploos van Amstel HK, Bekhof J, Blau N, Duran M: Tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency in Dutch neonates. J Inherit Metab Dis. 2001 Jun;24(3):352-8. [PubMed Link Image]
Biofluid Urine
Value 3.0 (0.48-4.5) 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. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.57 +/- 0.38 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 11.0 (4.0-18.0) umol/mmol creatinine
Age Infant:0-1 yr old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid Urine
Value 4.75 +/- 5.38 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 1.18 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Biofluid Urine
Value 2.4 +/- 0.40 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Ishida J, Iizuka R, Yamaguchi M: High-performance liquid chromatographic determination of 5-hydroxyindoles by post-column fluorescence derivatization. Analyst. 1993 Feb;118(2):165-9. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.0475 +/- 0.0130 uM
Age Adult:>18 yrs old
Sex Male
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid Blood
Value 0.0449 +/- 0.0140 uM
Age Adult:>18 yrs old
Sex Female
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid CSF
Value 0.33 +/- 0.04 uM
Age Children:1-13 yrs old
Sex Both
Condition Epilepsy
Comments Not Available
References
  • Shaywitz BA, Cohen DJ, Bowers MB: Reduced cerebrospinal fluid 5-hydroxyindoleacetic acid and homovanillic acid in children with epilepsy. Neurology. 1975 Jan;25(1):72-9. [PubMed Link Image]
Biofluid CSF
Value 0.08 +/- 0.08 uM
Age Adult:>18 yrs old
Sex Both
Condition Major depressive disorder
Comments Also known as major depressive disorder, clinical depression, unipolar depression, unipolar major depression or unipolar disorder
References
  • Sheline Y, Bardgett ME, Csernansky JG: Correlated reductions in cerebrospinal fluid 5-HIAA and MHPG concentrations after treatment with selective serotonin reuptake inhibitors. J Clin Psychopharmacol. 1997 Feb;17(1):11-4. [PubMed Link Image]
Biofluid CSF
Value 0.1 +/- 0.01 uM
Age Adult:>18 yrs old
Sex Both
Condition Friedreich's ataxia
Comments Not Available
References
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Biofluid CSF
Value 0.11 +/- 0.01 uM
Age Adult:>18 yrs old
Sex Both
Condition Olivopontocerebral atrophy
Comments Not Available
References
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Biofluid CSF
Value 0.1 +/- 0.02 uM
Age Adult:>18 yrs old
Sex Both
Condition Hereditary spastic paraplegia
Comments Not Available
References
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Biofluid CSF
Value 0.0025 (0.0000-0.0050) uM
Age Infant:0-1 yr old
Sex Male
Condition Aromatic L-amino acid decarboxylase deficiency
Comments Not Available
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid CSF
Value 0.019 +/- 0.0094 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Urine
Value 0.9 +/- 0.0 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Male
Condition Aromatic L-amino acid decarboxylase deficiency
Comments Not Available
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid Urine
Value 5.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Comments Not Available
References
  • Ishida J, Iizuka R, Yamaguchi M: High-performance liquid chromatographic determination of 5-hydroxyindoles by post-column fluorescence derivatization. Analyst. 1993 Feb;118(2):165-9. [PubMed Link Image]
Associated Disorders
Condition References
Aromatic L-amino acid decarboxylase deficiency
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Epilepsy
  • Shaywitz BA, Cohen DJ, Bowers MB: Reduced cerebrospinal fluid 5-hydroxyindoleacetic acid and homovanillic acid in children with epilepsy. Neurology. 1975 Jan;25(1):72-9. [PubMed Link Image]
Friedreich's ataxia
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Hereditary spastic paraplegia
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Major depressive disorder
  • Sheline Y, Bardgett ME, Csernansky JG: Correlated reductions in cerebrospinal fluid 5-HIAA and MHPG concentrations after treatment with selective serotonin reuptake inhibitors. J Clin Psychopharmacol. 1997 Feb;17(1):11-4. [PubMed Link Image]
Olivopontocerebral atrophy
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Schizophrenia
OMIM ID
  • 107930 Link Image (Aromatic L-amino acid decarboxylase deficiency)
  • 229300 Link Image (Friedreich's ataxia)
  • 182601 Link Image (Hereditary spastic paraplegia)
  • 608516 Link Image (Major depressive disorder)
  • 181500 Link Image (Schizophrenia)
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References
  1. Carpenter LL, Anderson GM, Siniscalchi JM, Chappell PB, Price LH: Acute changes in cerebrospinal fluid 5-HIAA following oral paroxetine challenge in healthy humans. Neuropsychopharmacology. 2003 Feb;28(2):339-47. [PubMed Link Image]
  2. Owens MJ, Nemeroff CB: Role of serotonin in the pathophysiology of depression: focus on the serotonin transporter. Clin Chem. 1994 Feb;40(2):288-95. [PubMed Link Image]
  3. Li JM, Kong LD, Wang YM, Cheng CH, Zhang WY, Tan WZ: Behavioral and biochemical studies on chronic mild stress models in rats treated with a Chinese traditional prescription Banxia-houpu decoction. Life Sci. 2003 Nov 21;74(1):55-73. [PubMed Link Image]
  4. Christofides J, Bridel M, Egerton M, Mackay GM, Forrest CM, Stoy N, Darlington LG, Stone TW: Blood 5-hydroxytryptamine, 5-hydroxyindoleacetic acid and melatonin levels in patients with either Huntington's disease or chronic brain injury. J Neurochem. 2006 May;97(4):1078-88. Epub 2006 Mar 29. [PubMed Link Image]
  5. Csernansky JG, Sheline YI: Abnormalities of serotonin metabolism and nonpsychotic psychiatric disorders. Ann Clin Psychiatry. 1993 Dec;5(4):275-81. [PubMed Link Image]
  6. Rotondo A, Schuebel K, Bergen A, Aragon R, Virkkunen M, Linnoila M, Goldman D, Nielsen D: Identification of four variants in the tryptophan hydroxylase promoter and association to behavior. Mol Psychiatry. 1999 Jul;4(4):360-8. [PubMed Link Image]
  7. Walendzik H, Zimmer G, Skopp G: [Serotonin, 5-hydroxyindolylacetic acid and cholesterol content in blood, cerebrospinal fluid and brain areas for differentiation of suicidal from non-suicidal cause of death] Arch Kriminol. 2000 May-Jun;205(5-6):131-44. [PubMed Link Image]
  8. Fukuda H, Nakamura S, Hara K, Udaka F, Kameyama M: [Study on the concentration of 5-hydroxyindoleacetic acid (5-HIAA) in the lumbar cerebrospinal fluid (CSF) in neurological diseases] Rinsho Shinkeigaku. 1989 Sep;29(9):1192-4. [PubMed Link Image]
  9. Meltzer H: Serotonergic dysfunction in depression. Br J Psychiatry Suppl. 1989 Dec;(8):25-31. [PubMed Link Image]
  10. Yamamoto M: Depression in Parkinson's disease: its prevalence, diagnosis, and neurochemical background. J Neurol. 2001 Sep;248 Suppl 3:III5-11. [PubMed Link Image]
  11. Korpi ER, Kleinman JE, Goodman SI, Phillips I, DeLisi LE, Linnoila M, Wyatt RJ: Serotonin and 5-hydroxyindoleacetic acid in brains of suicide victims. Comparison in chronic schizophrenic patients with suicide as cause of death. Arch Gen Psychiatry. 1986 Jun;43(6):594-600. [PubMed Link Image]
  12. Castejon AM, Paez X, Hernandez L, Cubeddu LX: Use of intravenous microdialysis to monitor changes in serotonin release and metabolism induced by cisplatin in cancer patients: comparative effects of granisetron and ondansetron. J Pharmacol Exp Ther. 1999 Dec;291(3):960-6. [PubMed Link Image]
  13. Lambert GW, Kaye DM, Cox HS, Vaz M, Turner AG, Jennings GL, Esler MD: Regional 5-hydroxyindoleacetic acid production in humans. Life Sci. 1995;57(3):255-67. [PubMed Link Image]
  14. Borg S, Kvande H, Liljeberg P, Mossberg D, Valverius P: 5-Hydroxyindoleacetic acid in cerebrospinal fluid in alcoholic patients under different clinical conditions. Alcohol. 1985 May-Jun;2(3):415-8. [PubMed Link Image]
  15. Celada P, Sarrias MJ, Artigas F: Serotonin and 5-hydroxyindoleacetic acid in plasma. Potential use as peripheral measures of MAO-A activity. J Neural Transm Suppl. 1990;32:149-54. [PubMed Link Image]
  16. Feldman JM: Urinary serotonin in the diagnosis of carcinoid tumors. Clin Chem. 1986 May;32(5):840-4. [PubMed Link Image]
  17. Mann JJ, McBride PA, Brown RP, Linnoila M, Leon AC, DeMeo M, Mieczkowski T, Myers JE, Stanley M: Relationship between central and peripheral serotonin indexes in depressed and suicidal psychiatric inpatients. Arch Gen Psychiatry. 1992 Jun;49(6):442-6. [PubMed Link Image]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. Hydroxyindole O-methyltransferase
  2. Aldehyde oxidase
  3. 4-trimethylaminobutyraldehyde dehydrogenase
  4. Alpha-aminoadipic semialdehyde dehydrogenase
  5. Aldehyde dehydrogenase 1A3
  6. Aldehyde dehydrogenase, mitochondrial precursor
  7. Fatty aldehyde dehydrogenase
  8. Aldehyde dehydrogenase X, mitochondrial precursor
  9. Aldeyde oxidase
Enzyme 1 [top]
Enzyme 1 ID 5333
Enzyme 1 Name Hydroxyindole O-methyltransferase
Enzyme 1 Synonyms
  1. HIOMT
  2. Acetylserotonin O-methyltransferase
  3. ASMT
Enzyme 1 Gene Name ASMT
Enzyme 1 Protein Sequence >Hydroxyindole O-methyltransferase 
MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVAAGVRASAHGT
ELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPTSQCSMLKYMGRTSYRCWGHL
ADAVREGRNQYLETFGVPAEELFTAIYRSEGERLQFMQALQEVWSVNGRSVLTAFDLSVF
PLMCDLGGGAGALAKECMSLYPGCKITVFDIPEVVWTAKQHFSFQEEEQIDFQEGDFFKD
PLPEADLYILARVLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYS
LNMLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARK
Enzyme 1 Number of Residues 345
Enzyme 1 Molecular Weight 38453
Enzyme 1 Theoretical pI 4.82
Enzyme 1 GO Classification
Function
  • O-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
—
Component
—
Enzyme 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID P46597 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HIOM_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence Not Available
Enzyme 1 GenBank Gene ID U11098 Link Image
Enzyme 1 GeneCard ID ASMT Link Image
Enzyme 1 GenAtlas ID ASMT Link Image
Enzyme 1 HGNC ID HGNC:750 Link Image
Enzyme 1 Chromosome Location X
Enzyme 1 Locus Xp22.3 or Yp11.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Rodriguez IR, Mazuruk K, Schoen TJ, Chader GJ: Structural analysis of the human hydroxyindole-O-methyltransferase gene. Presence of two distinct promoters. J Biol Chem. 1994 Dec 16;269(50):31969-77. [PubMed Link Image]
  2. Donohue SJ, Roseboom PH, Illnerova H, Weller JL, Klein DC: Human hydroxyindole-O-methyltransferase: presence of LINE-1 fragment in a cDNA clone and pineal mRNA. DNA Cell Biol. 1993 Oct;12(8):715-27. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5358
Enzyme 2 Name Aldehyde oxidase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name AOX1
Enzyme 2 Protein Sequence >Aldehyde oxidase 
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTPYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYPLLRNHPEPTLDQLTDALGGNLCRCHGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMADKQSQRTRVFGSER
MMWFSPVTLKDLLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPGYNSPDRIEEPECCKPC
IYGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPISR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAVLITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLAS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
Enzyme 2 Number of Residues 1338
Enzyme 2 Molecular Weight 147933
Enzyme 2 Theoretical pI 7.11
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 438656 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q06278 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ADO_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >4017 bp 
ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
CCGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACCCCCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCCATGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGATAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGACCTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGGTTATAATTCTCCTGATAGAATTGAAGAACCTGAGTGTTGTAAACCATGC
ATATATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCATCTCAAGG
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
CGTGGGTTTGGCTTTCCTCAGGCAGTGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGCGTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA
Enzyme 2 GenBank Gene ID L11005 Link Image
Enzyme 2 GeneCard ID AOX1 Link Image
Enzyme 2 GenAtlas ID AOX1 Link Image
Enzyme 2 HGNC ID HGNC:553 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2q33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5526
Enzyme 3 Name 4-trimethylaminobutyraldehyde dehydrogenase
Enzyme 3 Synonyms
  1. TMABADH
  2. Aldehyde dehydrogenase 9A1
  3. Aldehyde dehydrogenase E3 isozyme
  4. Gamma-aminobutyraldehyde dehydrogenase
  5. R- aminobutyraldehyde dehydrogenase
Enzyme 3 Gene Name ALDH9A1
Enzyme 3 Protein Sequence >4-trimethylaminobutyraldehyde dehydrogenase 
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
Enzyme 3 Number of Residues 494
Enzyme 3 Molecular Weight 53802
Enzyme 3 Theoretical pI 5.61
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Energy production and conversion
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • 4-trimethylammoniobutanal + NAD+ = 4-trimethylammoniobutanoate + NADH + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1049219 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P49189 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AL9A1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1482 bp 
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCGCTGGA
GCCGGCGGACGCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATAGCT
ACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCTGCT
TTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCTGCC
AGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGCAAG
TCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTATGCG
GGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGTTAT
ACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTTCAG
ATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAACCT
TCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGTGTA
CCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGTCAG
CATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATCATG
GAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCACTC
ATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAACTTC
CTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATTCTT
GATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCCCTT
CTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTTGGG
TTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATATGTA
CCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAATTGC
AGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTATCA
TTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCAGCT
GGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCTGGG
ACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATATAAG
AAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTGAAG
ACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
Enzyme 3 GenBank Gene ID U34252 Link Image
Enzyme 3 GeneCard ID ALDH9A1 Link Image
Enzyme 3 GenAtlas ID ALDH9A1 Link Image
Enzyme 3 HGNC ID HGNC:412 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1q23.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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. 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]
  4. 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]
  5. 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5528
Enzyme 4 Name Alpha-aminoadipic semialdehyde dehydrogenase
Enzyme 4 Synonyms
  1. Alpha-AASA dehydrogenase
  2. Delta1-piperideine-6-carboxylate dehydrogenease
  3. P6c dehydrogenase
  4. Aldehyde dehydrogenase family 7 member A1
  5. Antiquitin-1
Enzyme 4 Gene Name ALDH7A1
Enzyme 4 Protein Sequence >Alpha-aminoadipic semialdehyde dehydrogenase 
MSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADY
EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ
EYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIA
MICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVN
LLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQ
RCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA
KKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWN
NEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES
GSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
Enzyme 4 Number of Residues 511
Enzyme 4 Molecular Weight 55367
Enzyme 4 Theoretical pI 6.86
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function L-2-aminoadipate 6-semialdehyde + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H
Enzyme 4 Pathways
Enzyme 4 Reactions
  • L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 797410 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P49419 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AL7A1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1536 bp 
ATGTCCACTCTCCTCATCAATCAGCCCCAGTATGCGTGGCTGAAAGAGCTGGGGCTCCGC
GAGGAAAACGAGGGCGTGTATAATGGAAGCTGGGGAGGCCGGGGAGAGGTTATTACGACC
TATTGCCCCGCTAACAACGAGCCAATAGCAAGAGTCCGACAGGCCAGTGTGGCAGACTAT
GAAGAAACTGTAAAGAAAGCAAGAGAAGCATGGAAAATCTGGGCAGATATTCCTGCTCCA
AAACGAGGAGAAATAGTAAGACAGATTGGCGATGCCTTGCGGGAGAAGATCCAAGTACTA
GGAAGCTTGGTGTCTTTGGAGATGGGGAAAATCTTAGTGGAAGGTGTGGGTGAAGTTCAG
GAGTATGTGGATATCTGTGACTATGCTGTTGGTTTATCAAGGATGATTGGAGGACCTATC
TTGCCTTCTGAAAGATCTGGCCATGCACTGATTGAGCAGTGGAATCCCGTAGGCCTGGTT
GGAATCATCACGGCATTCAATTTCCCTGTGGCAGTGTATGGTTGGAACAACGCCATCGCC
ATGATCTGTGGAAATGTCTGCCTCTGGAAAGGAGCTCCAACCACTTCCCTCATTAGTGTG
GCTGTCACAAAGATAATAGCCAAGGTTCTGGAGGACAACAAGCTGCCTGGTGCAATTTGT
TCCTTGACTTGTGGTGGAGCAGATATTGGCACAGCAATGGCCAAAGATGAACGAGTGAAC
CTGCTGTCCTTCACTGGGAGCACTCAGGTGGGAAAACAGGTGGGCCTGATGGTGCAGGAG
AGGTTTGGGAGAAGTCTGTTGGAACTTGGAGGAAACAATGCCATTATTGCCTTTGAAGAT
GCAGACCTCAGCTTAGTTGTTCCATCAGCTCTCTTCGCTGCTGTGGGAACAGCTGGCCAG
AGGTGTACCACTGCGAGGCGACTGTTTATACATGAAAGCATCCATGATGAGGTTGTAAAC
AGACTTAAAAAGGCCTATGCACAGATCCGAGTTGGGAACCCATGGGACCCTAATGTTCTC
TATGGGCCACTCCACACCAAGCAGGCAGTGAGCATGTTTCTTGGAGCAGTGGAAGAAGCA
AAGAAAGAAGGTGGCACAGTGGTCTATGGGGGCAAGGTTATGGATCGCCCTGGAAATTAT
GTAGAACCGACAATTGTGACAGGTCTTGGCCACGATGCGTCCATTGCACACACAGAGACT
TTCGCTCCGATTCTCTATGTCTTTAAATTCAAGAATGAAGAAGAGGTCTTTGCATGGAAT
AATGAAGTAAAACAGGGACTTTCAAGTAGCATCTTTACCAAAGATCTGGGCAGAATCTTT
CGCTGGCTTGGACCTAAAGGATCAGACTGTGGCATTGTAAATGTCAACATTCCAACAAGT
GGGGCTGAGATTGGAGGTGCCTTTGGAGGAGAAAAGCACACTGGTGGTGGCAGGGAGTCT
GGCAGTGATGCCTGGAAACAGTACATGAGAAGGTCTACTTGTACTATCAACTACAGTAAA
GACCTTCCTCTGGCCCAAGGAATCAAGTTTCAGTAA
Enzyme 4 GenBank Gene ID S74728 Link Image
Enzyme 4 GeneCard ID ALDH7A1 Link Image
Enzyme 4 GenAtlas ID ALDH7A1 Link Image
Enzyme 4 HGNC ID HGNC:877 Link Image
Enzyme 4 Chromosome Location 5
Enzyme 4 Locus 5q31
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5529
Enzyme 5 Name Aldehyde dehydrogenase 1A3
Enzyme 5 Synonyms
  1. Aldehyde dehydrogenase 6
  2. Retinaldehyde dehydrogenase 3
  3. RALDH-3
Enzyme 5 Gene Name ALDH1A3
Enzyme 5 Protein Sequence >Aldehyde dehydrogenase 1A3 
MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
Enzyme 5 Number of Residues 512
Enzyme 5 Molecular Weight 56109
Enzyme 5 Theoretical pI 7.29
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Energy production and conversion
Enzyme 5 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 5 Pathways
Enzyme 5 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 544482 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P47895 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AL1A3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1539 bp 
ATGGCCACCGCTAACGGGGCCGTGGAAAACGGGCAGCCGGACGGGAAGCCGCCGGCCCTG
CCGCGCCCCATCCGCAACCTGGAGGTCAAGTTCACCAAGATATTTATCAACAATGAATGG
CACGAATCCAAGAGTGGGAAAAAGTTTGCTACATGTAACCCTTCAACTCGGGAGCAAATA
TGTGAAGTGGAAGAAGGAGATAAGCCCGACGTGGACAAGGCTGTGGAGGCTGCACAGGTT
GCCTTCCAGAGGGGCTCGCCATGGCGCCGGCTGGATGCCCTGAGTCGTGGGCGGCTGCTG
CACCAGCTGGCTGACCTGGTGGAGAGGGACCGCGCCACCTTGGCCGCCCTGGAGACGATG
GATACAGGGAAGCCATTTCTTCATGCTTTTTTCATCGACCTGGAGGGCTGTATTAGAACC
CTCAGATACTTTGCAGGGTGGGCAGACAAAATCCAGGGCAAGACCATCCCCACAGATGAC
AACGTCGTATGCTTCACCAGGCATGAGCCCATTGGTGTCTGTGGGGCCATCACTCCATGG
AACTTCCCCCTGCTGATGCTGGTGTGGAAGCTGGCACCCGCCCTCTGCTGTGGGAACACC
ATGGTCCTGAAGCCTGCGGAGCAGACACCTCTCACCGCCCTTTATCTCGGCTCTCTGATC
AAAGAGGCCGGGTTCCCTCCAGGAGTGGTGAACATTGTGCCAGGATTCGGGCCCACAGTG
GGAGCAGCAATTTCTTCTCACCCTCAGATCAACAAGATCGCCTTCACCGGCTCCACAGAG
GTTGGAAAACTGGTTAAAGAAGCTGCGTCCCGGAGCAATCTGAAGCGGGTGACGCTGGAG
CTGGGGGGGAAGAACCCCTGCATCGTGTGTGCGGACGCTGACTTGGACTTGGCAGTGGAG
TGTGCCCATCAGGGAGTGTTCTTCAACCAAGGCCAGTGTTGCACGGCAGCCTCCAGGGTG
TTCGTGGAGGAGCAGGTCTACTCTGAGTTTGTCAGGCGGAGCGTGGAGTATGCCAAGAAA
CGGCCCGTGGGAGACCCCTTCGATGTCAAAACAGAACAGGGGCCTCAGATTGATCAAAAG
CAGTTCGACAAAATCTTAGAGCTGATCGAGAGTGGGAAGAAGGAAGGGGCCAAGCTGGAA
TGCGGGGGCTCAGCCATGGAAGACAAGGGGCTCTTCATCAAACCCACTGTCTTCTCAGAA
GTCACAGACAACATGCGGATTGCCAAAGAGGAGATTTTCGGGCCAGTGCAACCAATACTG
AAGTTCAAAAGTATCGAAGAAGTGATAAAAAGAGCGAATAGCACCGACTATGGACTCACA
GCAGCCGTGTTCACAAAAAATCTCGACAAAGCCCTGAAGTTGGCTTCTGCCTTAGAGTCT
GGAACGGTCTGGATCAACTGCTACAACGCCCTCTATGCACAGGCTCCATTTGGTGGCTTT
AAAATGTCAGGAAATGGCAGAGAACTAGGTGAATACGCTTTGGCCGAATACACAGAAGTG
AAAACTGTCACCATCAAACTTGGCGACAAGAACCCCTGA
Enzyme 5 GenBank Gene ID U07919 Link Image
Enzyme 5 GeneCard ID ALDH1A3 Link Image
Enzyme 5 GenAtlas ID ALDH1A3 Link Image
Enzyme 5 HGNC ID HGNC:409 Link Image
Enzyme 5 Chromosome Location 15
Enzyme 5 Locus 15q26.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5530
Enzyme 6 Name Aldehyde dehydrogenase, mitochondrial precursor
Enzyme 6 Synonyms
  1. ALDH class 2
  2. ALDHI
  3. ALDH-E2
Enzyme 6 Gene Name ALDH2
Enzyme 6 Protein Sequence >Aldehyde dehydrogenase, mitochondrial precursor 
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Enzyme 6 Number of Residues 517
Enzyme 6 Molecular Weight 56382
Enzyme 6 Theoretical pI 7.05
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Energy production and conversion
Enzyme 6 Specific Function An aldehyde + NAD(+) + H(2)O = an acid + NADH
Enzyme 6 Pathways
Enzyme 6 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-24
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 28606 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P05091 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Enzyme 6 PDB ID 1OF7 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID X05409 Link Image
Enzyme 6 GeneCard ID ALDH2 Link Image
Enzyme 6 GenAtlas ID ALDH2 Link Image
Enzyme 6 HGNC ID HGNC:404 Link Image
Enzyme 6 Chromosome Location 12
Enzyme 6 Locus 12q24.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. 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]
  5. 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]
  6. 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]
  7. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  8. 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]
  9. 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]
  10. 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]
  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]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5531
Enzyme 7 Name Fatty aldehyde dehydrogenase
Enzyme 7 Synonyms
  1. Aldehyde dehydrogenase, microsomal
  2. Aldehyde dehydrogenase family 3 member A2
  3. Aldehyde dehydrogenase 10
Enzyme 7 Gene Name ALDH3A2
Enzyme 7 Protein Sequence >Fatty aldehyde dehydrogenase 
MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQE
VITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQ
PLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDH
IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT
CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKI
AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLA
LYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS
HQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLV
KAEYY
Enzyme 7 Number of Residues 485
Enzyme 7 Molecular Weight 54849
Enzyme 7 Theoretical pI 7.99
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Energy production and conversion
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 464-480
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 1082036 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P51648 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name AL3A2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID L47162 Link Image
Enzyme 7 GeneCard ID ALDH3A2 Link Image
Enzyme 7 GenAtlas ID ALDH3A2 Link Image
Enzyme 7 HGNC ID HGNC:403 Link Image
Enzyme 7 Chromosome Location 17
Enzyme 7 Locus 17p11.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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. 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]
  5. 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]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5532
Enzyme 8 Name Aldehyde dehydrogenase X, mitochondrial precursor
Enzyme 8 Synonyms
  1. Aldehyde dehydrogenase family 1 member B1
  2. ALDH class 2
Enzyme 8 Gene Name ALDH1B1
Enzyme 8 Protein Sequence >Aldehyde dehydrogenase X, mitochondrial precursor 
MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
Enzyme 8 Number of Residues 517
Enzyme 8 Molecular Weight 57239
Enzyme 8 Theoretical pI 6.79
Enzyme 8 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Energy production and conversion
Enzyme 8 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 8 Pathways
Enzyme 8 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-22
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1263008 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P30837 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name AL1B1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1554 bp 
ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCTCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGCATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAA
Enzyme 8 GenBank Gene ID M63967 Link Image
Enzyme 8 GeneCard ID ALDH1B1 Link Image
Enzyme 8 GenAtlas ID ALDH1B1 Link Image
Enzyme 8 HGNC ID HGNC:407 Link Image
Enzyme 8 Chromosome Location 9
Enzyme 8 Locus 9p11.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 13071
Enzyme 9 Name Aldeyde oxidase
Enzyme 9 Synonyms
  1. Aldehyde oxidase 1, isoform CRA_b
  2. Aldehyde oxidase 1
Enzyme 9 Gene Name hAO
Enzyme 9 Protein Sequence >Aldeyde 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 9 Number of Residues 1338
Enzyme 9 Molecular Weight 147920
Enzyme 9 Theoretical pI 7.17
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 9 General Function Nucleotide transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways
Enzyme 9 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635] ALL_REAC R00635 > R02657 R04904
  • (other) R01709 R02655 R03871 R04085
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 109658814 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9BYF0 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q9BYF0_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID BC117179 Link Image
Enzyme 9 GeneCard ID Q9BYF0 Link Image
Enzyme 9 GenAtlas ID hAO Link Image
Enzyme 9 HGNC ID HGNC:553 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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. 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 9 Metabolite References Not Available