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Human Metabolome Database Version 2.5

 

Showing metabocard for p-Hydroxyphenylacetic acid (HMDB00020)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-23 09:50:42
Accession Number HMDB00020
Secondary Accession Numbers Not Available
Common Name p-Hydroxyphenylacetic acid
Description An oxidative deaminated metabolite of p-tyramine. Also a metabolite of tyrosine via enteric bacteria. The bacterial origin of this compound was confirmed by the finding that this compound in urine decreased significantly after the use of the antibiotic neomycin.
Synonyms
  1. (4-Hydroxy-phenyl)-essigsaeure
  2. (4-hydroxy-phenyl)-acetate
  3. (4-hydroxy-phenyl)-acetic acid
  4. (4-hydroxyphenyl)acetate
  5. (4-hydroxyphenyl)acetic acid
  6. (p-Hydroxyphenyl)acetate
  7. (p-Hydroxyphenyl)acetic acid
  8. (p-hydroxyphenyl)-Acetate
  9. (p-hydroxyphenyl)-Acetic acid
  10. 4-Hydroxy-Benzeneacetate
  11. 4-Hydroxy-Benzeneacetic acid
  12. 4-Hydroxybenzeneacetate
  13. 4-Hydroxybenzeneacetic acid
  14. 4-hydroxyphenylacetate
  15. 4-hydroxyphenylacetic acid
  16. Parahydroxy phenylacetate
  17. Parahydroxy phenylacetic acid
  18. Parahydroxyphenylacetate
  19. p-hydroxyphenylacetate
  20. p-hydroxyphenylacetic acid
Chemical IUPAC Name 2-(4-hydroxyphenyl)acetic acid
Chemical Formula C8H8O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Aromatic Acids
Sub Class
  • Phenolic acids
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • carboxylic acid
  • aromatic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 152.147
Monoisotopic Molecular Weight 152.047348
Isomeric SMILES OC(=O)CC1=CC=C(O)C=C1
Canonical SMILES OC(=O)CC1=CC=C(O)C=C1
KEGG Compound ID C00642 Link Image
BioCyc ID 4-HYDROXYPHENYLACETATE Link Image
BiGG ID 35599 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00020 Link Image
Metagene Link HMDB00020 Link Image
METLIN ID 130 Link Image
PubChem Compound 127 Link Image
PubChem Substance 7885355 Link Image
ChEBI ID 18101 Link Image
CAS Registry Number 156-38-7
InChI Identifier InChI=1/C8H8O3/c9-7-3-1-6(2-4-7)5-8(10)11/h1-4,9H,5H2,(H,10,11)
Synthesis Reference Qiao, Xi-long; Tian, Hui; Li, Wen; Zhao, Xiu-yun; Zhang, Jin-fang. Study of 4-hydroxyphenylacetic acid synthesis from glyoxalic acid. Hebei Gongye Keji (2005), 22(5), 264-266.
Melting Point (Experimental) 148-150 oC
Experimental Water Solubility 60.7 mg/mL [GRACIN,S & RASMUSON,AC (2002)] Source: PhysProp
Predicted Water Solubility 7.12 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity 0.75 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 0.93 [Predicted by ALOGPS]; 1 [Predicted by PubChem via XLOGP] 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 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
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Bladder —
Epidermis —
Kidney —
Concentrations (Normal)
Biofluid Blood
Value 0.230 (0.070-0.390) uM
Age Adult:>18 yrs old
Sex Both
Patient information Adults
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 0.05 +/- 0.007 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Kobayashi K, Koide Y, Yoshino K, Shohmori T: [P-hydroxyphenylacetic acid concentrations in cerebrospinal fluid] No To Shinkei. 1982 Aug;34(8):769-74. [PubMed Link Image]
Biofluid Saliva
Value 7.0 (2.0-10.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Takahama U, Oniki T, Murata H: The presence of 4-hydroxyphenylacetic acid in human saliva and the possibility of its nitration by salivary nitrite in the stomach. FEBS Lett. 2002 May 8;518(1-3):116-8. [PubMed Link Image]
Biofluid Urine
Value 24.2 umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
Biofluid Urine
Value 36.7 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
Biofluid Urine
Value 20.3 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
Biofluid Urine
Value 31.4 umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
Biofluid Urine
Value 15.3 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
Biofluid Urine
Value 24.2 (8.6-73.2) 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 36.7 (8.4-142.0) 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 20.3 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 31.4 (9.7-187.4) 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 15.3 (3.2-180.2) 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 7.0 (2.8-11.0) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • McKibbin B, O'Gorman L, Duckworth T: Catecholamine metabolite excretion in spina bifida. J Clin Pathol. 1969 Nov;22(6):687-9. [PubMed Link Image]
Biofluid Urine
Value 134 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Based on one measurement
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
Biofluid Urine
Value 917.00 +/- 341.8 umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hoehn T, Janssen S, Mani AR, Brauers G, Moore KP, Schadewaldt P, Mayatepek E: Urinary excretion of the nitrotyrosine metabolite 3-nitro-4-hydroxyphenylacetic acid in preterm and term infants. Neonatology. 2008;93(2):73-6. Epub 2007 Aug 6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 0.31 +/- 0.0.03 uM
Age Adult:>18 yrs old
Sex N/A
Condition Schizophrenia
Comments Not Available
References
  • Kobayashi K, Koide Y, Yoshino K, Shohmori T: [P-hydroxyphenylacetic acid concentrations in cerebrospinal fluid] No To Shinkei. 1982 Aug;34(8):769-74. [PubMed Link Image]
Biofluid CSF
Value 0.038 +/- 0.005 uM
Age Adult:>18 yrs old
Sex N/A
Condition Epilepsy
Comments Not Available
References
  • Kobayashi K, Koide Y, Yoshino K, Shohmori T: [P-hydroxyphenylacetic acid concentrations in cerebrospinal fluid] No To Shinkei. 1982 Aug;34(8):769-74. [PubMed Link Image]
Biofluid Urine
Value 16.0 +/- 15.0 umol/mmol creatinine
Age N/A
Sex Both
Condition Lung Cancer
Comments Not Available
References
  • HMP experimental
Biofluid Urine
Value 25.0 (7.0-50.5) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Spina Bifida
Comments Not Available
References
  • McKibbin B, O'Gorman L, Duckworth T: Catecholamine metabolite excretion in spina bifida. J Clin Pathol. 1969 Nov;22(6):687-9. [PubMed Link Image]
Biofluid Urine
Value 428.00 +/- 164.00 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Hoehn T, Janssen S, Mani AR, Brauers G, Moore KP, Schadewaldt P, Mayatepek E: Urinary excretion of the nitrotyrosine metabolite 3-nitro-4-hydroxyphenylacetic acid in preterm and term infants. Neonatology. 2008;93(2):73-6. Epub 2007 Aug 6. [PubMed Link Image]
Associated Disorders
Condition References
Epilepsy
  • Kobayashi K, Koide Y, Yoshino K, Shohmori T: [P-hydroxyphenylacetic acid concentrations in cerebrospinal fluid] No To Shinkei. 1982 Aug;34(8):769-74. [PubMed Link Image]
Lung Cancer
  • HMP experimental
Schizophrenia
  • Kobayashi K, Koide Y, Yoshino K, Shohmori T: [P-hydroxyphenylacetic acid concentrations in cerebrospinal fluid] No To Shinkei. 1982 Aug;34(8):769-74. [PubMed Link Image]
Spina Bifida
  • McKibbin B, O'Gorman L, Duckworth T: Catecholamine metabolite excretion in spina bifida. J Clin Pathol. 1969 Nov;22(6):687-9. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
General References
  1. Hirota S, Takahama U, Ly TN, Yamauchi R: Quercetin-dependent inhibition of nitration induced by peroxidase/H2O2/nitrite systems in human saliva and characterization of an oxidation product of quercetin formed during the inhibition. J Agric Food Chem. 2005 May 4;53(9):3265-72. [PubMed Link Image]
  2. Takahama U, Oniki T, Murata H: The presence of 4-hydroxyphenylacetic acid in human saliva and the possibility of its nitration by salivary nitrite in the stomach. FEBS Lett. 2002 May 8;518(1-3):116-8. [PubMed Link Image]
  3. Kobayashi K, Koide Y, Shohmori T: Determination of p-hydroxyphenylacetic acid in cerebrospinal fluid by high-performance liquid chromatography with electrochemical detection. Clin Chim Acta. 1982 Aug 4;123(1-2):161-8. [PubMed Link Image]
  4. Tyce GM, Stockard J, Sharpless NS, Muenter MD: Excretion of amines and their metabolites by two patients in hepatic coma treated with L-dopa. Clin Pharmacol Ther. 1983 Sep;34(3):390-8. [PubMed Link Image]
  5. Young SN, Davis BA, Gauthier S: Precursors and metabolites of phenylethylamine, m and p-tyramine and tryptamine in human lumbar and cisternal cerebrospinal fluid. J Neurol Neurosurg Psychiatry. 1982 Jul;45(7):633-9. [PubMed Link Image]
  6. Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
  7. Muskiet FA, Groen A: Urinary excretion of conjugated homovanillic acid, 3,4-dihydroxyphenylacetic acid, p-hydroxyphenylacetic acid, and vanillic acid by persons on their usual diet and patients with neuroblastoma. Clin Chem. 1979 Jul;25(7):1281-4. [PubMed Link Image]
  8. 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]
  9. McKibbin B, O'Gorman L, Duckworth T: Catecholamine metabolite excretion in spina bifida. J Clin Pathol. 1969 Nov;22(6):687-9. [PubMed Link Image]
  10. Mani AR, Pannala AS, Orie NN, Ollosson R, Harry D, Rice-Evans CA, Moore KP: Nitration of endogenous para-hydroxyphenylacetic acid and the metabolism of nitrotyrosine. Biochem J. 2003 Sep 1;374(Pt 2):521-7. [PubMed Link Image]
  11. Takahama U, Hirota S, Nishioka T, Oniki T: Human salivary peroxidase-catalyzed oxidation of nitrite and nitration of salivary components 4-hydroxyphenylacetic acid and proteins. Arch Oral Biol. 2003 Oct;48(10):679-90. [PubMed Link Image]
  12. Quijano C, Hernandez-Saavedra D, Castro L, McCord JM, Freeman BA, Radi R: Reaction of peroxynitrite with Mn-superoxide dismutase. Role of the metal center in decomposition kinetics and nitration. J Biol Chem. 2001 Apr 13;276(15):11631-8. Epub 2001 Jan 4. [PubMed Link Image]
  13. Raw I, Schmidt BJ, Merzel J: Catecholamines and congenital pain insensitivity. Braz J Med Biol Res. 1984;17(3-4):271-9. [PubMed Link Image]
  14. Jenner AM, Rafter J, Halliwell B: Human fecal water content of phenolics: the extent of colonic exposure to aromatic compounds. Free Radic Biol Med. 2005 Mar 15;38(6):763-72. [PubMed Link Image]
Metabolic Enzymes
  1. Aldehyde dehydrogenase, dimeric NADP-preferring
  2. Aldehyde dehydrogenase 1A3
  3. Aldehyde dehydrogenase 3B2
  4. Aldehyde dehydrogenase 3B1
  5. Copper amine oxidase precursor
  6. Aldehyde dehydrogenase 3B1 (Aldehyde dehydrogenase 3 family, member B1, isoform CRA_c) (cDNA FLJ77312, highly similar to Homo sapiens aldehyde dehydrogenase 3 family, member B1 (ALDH3B1),mRNA)
Enzyme 1 [top]
Enzyme 1 ID 5527
Enzyme 1 Name Aldehyde dehydrogenase, dimeric NADP-preferring
Enzyme 1 Synonyms
  1. ALDH class 3
  2. ALDHIII
Enzyme 1 Gene Name ALDH3A1
Enzyme 1 Protein Sequence >Aldehyde dehydrogenase, dimeric NADP-preferring 
MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAY
YEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNL
TIQPMVGAIAAGNAVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKER
FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNS
GQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEG
QKVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREK
PLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFE
TFSHRRSCLVRPLMNDEGLKVRYPPSPAKMTQH
Enzyme 1 Number of Residues 453
Enzyme 1 Molecular Weight 50380
Enzyme 1 Theoretical pI 6.52
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Energy production and conversion
Enzyme 1 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. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes
Enzyme 1 Pathways
Enzyme 1 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 178402 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P30838 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AL3A1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1362 bp 
ATGAGCAAGATCAGCGAGGCCGTGAAGCGCGCCCGCGCCGCCTTCAGCTCGGGCAGGACC
CGTCCGCTGCAGTTCCGATTCCAGCAGCTGGAGGCGCTGCAGCGCCTGATCCAGGAGCAG
GAGCAGGAGCTGGTGGGCGCGCTGGCCGCAGACCTGCACAAGAATGAATGGAACGCCTAC
TATGAGGAGGTGGTGTACGTCCTAGAGGAGATCGAGTACATGATCCAGAAGCTCCCTGAG
TGGGCCGCGGATGAGCCCGTGGAGAAGACGCCCCAGACTCAGCAGGACGAGCTCTACATC
CACTCGGAGCCACTGGGCGTGGTCCTCGTCATTGGCACCTGGAACTACCCCTTCAACCTC
ACCATCCAGCCCATGGTGGGCGCCATCGCTGCAGGGAACGCAGTGGTCCTCAAGCCCTCG
GAGCTGAGTGAGAACATGGCGAGCCTGCTGGCTACCATCATCCCCCAGTACCTGGACAAG
GATCTGTACCCAGTAATCAATGGGGGTGTCCCTGAGACCACGGAGCTGCTCAAGGAGAGG
TTCGACCATATCCTGTACACGGGCAGCACGGGGGTGGGGAAGATCATCATGACGGCTGCT
GCCAAGCACCTGACCCCTGTCACGCTGGAGCTGGGAGGGAAGAGTCCCTGCTACGTGGAC
AAGAACTGTGACCTGGACGTGGCCTGCCGACGCATCGCCTGGGGGAAATTCATGAACAGT
GGCCAGACCTGCGTGGCCCCAGACTACATCCTCTGTGACCCCTCGATCCAGAACCAAATT
GTGGAGAAGCTCAAGAAGTCACTGAAAGAGTTCTACGGGGAAGATGCTAAGAAATCCCGG
GACTATGGAAGAATCATTAGTGCCCGGCACTTCCAGAGGGTGATGGGCCTGATTGAGGGC
CAGAAGGTGGCTTATGGGGGCACCGGGGATGCCGCCACTCGCTACATAGCCCCCACCATC
CTCACGGACGTGGACCCCCAGTCCCCGGTGATGCAAGAGGAGATCTTCGGGCCTGTGCTG
CCCATCGTGTGCGTGCGCAGCCTGGAGGAGGCCATCCAGTTCATCAACCAGCGTGAGAAG
CCCCTGGCCCTCTACATGTTCTCCAGCAACGACAAGGTGATTAAGAAGATGATTGCAGAG
ACATCCAGTGGTGGGGTGGCGGCCAACGATGTCATCGTCCACATCACCTTGCACTCTCTG
CCCTTCGGGGGCGTGGGGAACAGCGGCATGGGATCCTACCATGGCAAGAAGAGCTTCGAG
ACTTTCTCTCACCGCCGCTCTTGCCTGGTGAGGCCTCTGATGAATGATGAAGGCCTGAAG
GTCAGATACCCCCCGAGCCCGGCCAAGATGACCCAGCACTGA
Enzyme 1 GenBank Gene ID M74542 Link Image
Enzyme 1 GeneCard ID ALDH3A1 Link Image
Enzyme 1 GenAtlas ID ALDH3A1 Link Image
Enzyme 1 HGNC ID HGNC:405 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17p11.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hsu LC, Chang WC, Shibuya A, Yoshida A: Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli. J Biol Chem. 1992 Feb 15;267(5):3030-7. [PubMed Link Image]
  2. Hsu LC, Yoshida A: Human stomach aldehyde dehydrogenase, ALDH3. Adv Exp Med Biol. 1993;328:141-52. [PubMed Link Image]
  3. Yin SJ, Vagelopoulos N, Wang SL, Jornvall H: Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families. FEBS Lett. 1991 May 20;283(1):85-8. [PubMed Link Image]
  4. Tsukamoto N, Chang C, Yoshida A: Mutations associated with Sjogren-Larsson syndrome. Ann Hum Genet. 1997 May;61(Pt 3):235-42. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5529
Enzyme 2 Name Aldehyde dehydrogenase 1A3
Enzyme 2 Synonyms
  1. Aldehyde dehydrogenase 6
  2. Retinaldehyde dehydrogenase 3
  3. RALDH-3
Enzyme 2 Gene Name ALDH1A3
Enzyme 2 Protein Sequence >Aldehyde dehydrogenase 1A3 
MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
Enzyme 2 Number of Residues 512
Enzyme 2 Molecular Weight 56109
Enzyme 2 Theoretical pI 7.29
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 544482 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P47895 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AL1A3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID U07919 Link Image
Enzyme 2 GeneCard ID ALDH1A3 Link Image
Enzyme 2 GenAtlas ID ALDH1A3 Link Image
Enzyme 2 HGNC ID HGNC:409 Link Image
Enzyme 2 Chromosome Location 15
Enzyme 2 Locus 15q26.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5810
Enzyme 3 Name Aldehyde dehydrogenase 3B2
Enzyme 3 Synonyms
  1. Aldehyde dehydrogenase 8
Enzyme 3 Gene Name ALDH3B2
Enzyme 3 Protein Sequence >Aldehyde dehydrogenase 3B2 
MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGNCVVLKPSE
ISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAAT
KHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQERLL
PALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSNESDRYIAPTVL
VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERT
SSGSFGGNEGFTYISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEKLKEI
RYPPYTDWNQQLLRWGMGSQSCTLL
Enzyme 3 Number of Residues 385
Enzyme 3 Molecular Weight 42670
Enzyme 3 Theoretical pI 5.97
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 An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H
Enzyme 3 Pathways
Enzyme 3 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + 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 1051281 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P48448 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AL3B2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1158 bp 
ATGAAGGATGAACCACGGTCCACGAACCTGTTCATGAAGCTGGACTCGGTCTTCATCTGG
AAGGAACCCTTTGGCCTGGTCCTCATCATCGCACCCTGGAACTACCCATTGAACCTGACC
CTGGTGCTCCTGGTGGGCACCCTCCCCGCAGGGAATTGCGTGGTGCTGAAGCCGTCAGAA
ATCAGCCAGGGCACAGAGAAGGTCCTGGCTGAGGTGCTGCCCCAGTACCTGGACCAGAGC
TGCTTTGCCGTGGTGCTGGGCGGACCCCAGGAGACAGGGCAGCTGCTAGAGCACAAGTTG
GACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTCATGACTGCTGCCACC
AAGCACCTGACGCCTGTCACCCTGGAGCTGGGGGGCAAGAACCCCTGCTACGTGGACGAC
AACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCTGCTACTTCAATGCCGGC
CAGACCTGCGTGGCCCCTGACTACGTCCTGTGCAGCCCCGAGATGCAGGAGAGGCTGCTG
CCCGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCAAAC
CTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGCGGC
CGCGTGGCCATTGGGGGCCAGAGCAACGAGAGCGATCGCTACATCGCCCCCACGGTGCTG
GTGGACGTGCAGGAGACGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTGCCC
ATCGTGAACGTGCAGAGCGTGGACGAGGCCATCAAGTTCATCAACCGGCAGGAGAAGCCC
CTGGCCCTGTACGCCTTCTCCAACAGCAGACAGGTTGTGAACCAGATGCTGGAGCGGACC
AGCAGCGGCAGCTTTGGAGGCAATGAGGGCTTCACCTACATATCTCTGCTGTCCGTGCCA
TTCGGGGGAGTCGGCCACAGTGGGATGGGCCGGTACCACGGCAAGTTCACCTTCGACACC
TTCTCCCACCACCGCACCTGCCTGCTCGCCCCCTCCGGCCTGGAGAAATTAAAGGAGATC
CGCTACCCACCCTATACCGACTGGAACCAGCAGCTGTTACGCTGGGGCATGGGCTCCCAG
AGCTGCACCCTCCTGTGA
Enzyme 3 GenBank Gene ID U37519 Link Image
Enzyme 3 GeneCard ID ALDH3B2 Link Image
Enzyme 3 GenAtlas ID ALDH3B2 Link Image
Enzyme 3 HGNC ID HGNC:411 Link Image
Enzyme 3 Chromosome Location 11
Enzyme 3 Locus 11q13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Hsu LC, Chang WC, Lin SW, Yoshida A: Cloning and characterization of genes encoding four additional human aldehyde dehydrogenase isozymes. Adv Exp Med Biol. 1995;372:159-68. [PubMed Link Image]
  2. Hsu LC, Chang WC: Sequencing and expression of the human ALDH8 encoding a new member of the aldehyde dehydrogenase family. Gene. 1996 Oct 3;174(2):319-22. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5811
Enzyme 4 Name Aldehyde dehydrogenase 3B1
Enzyme 4 Synonyms
  1. Aldehyde dehydrogenase 7
Enzyme 4 Gene Name ALDH3B1
Enzyme 4 Protein Sequence >Aldehyde dehydrogenase 3B1 
MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE
VSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNL
TLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHR
FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA
GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC
GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK
PLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFD
TFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL
Enzyme 4 Number of Residues 468
Enzyme 4 Molecular Weight 51840
Enzyme 4 Theoretical pI 7.67
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 An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H
Enzyme 4 Pathways
Enzyme 4 Reactions
  • an aldehyde + NAD(P)+ + H2O = an acid + 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 601780 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P43353 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AL3B1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1407 bp 
ATGGACCCCCTTGGGGACACGCTGCGGCGACTGCGGGAGGCCTTCCACGCGGGGCGCACG
CGGCCAGCTGAGTTCCGGGCTGCGCAGCTCCAAGGCCTGGGCCGCTTCCTGCAAGAAAAC
AAGCAGCTTCTGCACGACGCACTGGCCCAGGACCTGCACAAGTCAGCCTTCGAGTCGGAG
GTGTCTGAGGTTGCCATCAGCCAGGGCGAGGTCACCCTGGCCCTCAGGAACCTCCGGGCC
TGGATGAAGGACGAGCGTGTGCCCAAGAACCTGGCCACGCAGCTGGACTCCGCCTTCATC
CGGAAGGAGCCCTTTGGCCTGGTCCTCATCATTGCGCCCTGGAACTATCCGCTGAACCTG
ACGCTGGTGCCCCTCGTGGGAGCCCTCGCTGCAGGGAACTGTGTGGTGCTGAAGCCATCG
GAGATTAGCAAGAACGTCGAGAAGATCCTGGCCGAGGTGCTGCCCCAATACGTGGACCAG
AGCTGCTTTGCTGTGGTGCTGGGCGGGCCCCAGGAGACGGGGCAGCTGCTAGAGCACAGG
TTCGACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTTATGACTGCTGCC
GCCAAGCACCTGACACCTGTCACCCTGGAGCTGGGGGGCAAGAACCCTTGCTACGTGGAC
GACAACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCCGCTACTTCAACGCC
GGCCAGACCTGCGTGGCCCCCGACTACGTCCTATGCAGCCCTGAGATGCAGGAGAGGCTG
CTGCCTGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCA
AACCTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGC
GGCCGTGTGGCCATTGGGGGCCAGAGCGATGAGAGCGATCGCTACATCGCCCCCACGGTG
CTGGTGGATGTGCAGGAGATGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTG
CCCATCGTGAACGTGCAGAGCTTGGACGAGGCCATCGAGTTCATCAACCGGCGGGAGAAG
CCCCTGGCCCTGTACGCCTTCTCCAACAGCAGCCAGGTGGTCAAGCGGGTGCTGACCCAG
ACCAGCAGCGGGGGCTTCTGTGGGAACGACGGCTTCATGCACATGACCCTGGCCAGCCTG
CCTTTTGGAGGAGTGGGTGCCAGTGGGATGGGCCGGTACCATGGCAAGTTCTCCTTCGAC
ACCTTCTCCCACCATCGCGCCTGCCTCCTGCGCAGCCCGGGGATGGAGAAGCTCAACGCC
CTCCGCTACCCGCCGCAATCGCCGCGCCGCCTGAGGATGCTGCTGGTGGCCATGGAGGCC
CAAGGCTGCAGCTGCACACTGCTCTGA
Enzyme 4 GenBank Gene ID U10868 Link Image
Enzyme 4 GeneCard ID ALDH3B1 Link Image
Enzyme 4 GenAtlas ID ALDH3B1 Link Image
Enzyme 4 HGNC ID HGNC:410 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11q13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Hsu LC, Chang WC, Yoshida A: Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family. Gene. 1994 Dec 30;151(1-2):285-9. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14848
Enzyme 5 Name Copper amine oxidase precursor
Enzyme 5 Synonyms
  1. Tyramine oxidase
  2. 2- phenylethylamine oxidase
Enzyme 5 Gene Name tynA
Enzyme 5 Protein Sequence >Copper amine oxidase precursor 
MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLF
TLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVE
KRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPR
KADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVK
KRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDL
EQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDF
HLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMG
TLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVST
ERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTR
YGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNI
GNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHR
LSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHV
ARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK
Enzyme 5 Number of Residues 757
Enzyme 5 Molecular Weight 84379
Enzyme 5 Theoretical pI 5.71
Enzyme 5 GO Classification
Function
  • binding
  • cation binding
  • copper ion binding
  • ion binding
  • transition metal ion binding
Process
—
Component
—
Enzyme 5 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 5 Specific Function The enzyme prefers aromatic over aliphatic amines
Enzyme 5 Pathways
Enzyme 5 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853] ALL_REAC R01853 > R01151 R02150 R02173 R02382 R02529 R02613 R03139 R04300 R05334 R06154 R06740
  • (other) R04027 R06133
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-30
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 809499 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P46883 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AMO_ECOLI Link Image
Enzyme 5 PDB ID 1DYU Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2274 bp 
ATGGGAAGCCCCTCTCTGTATTCTGCCCGTAAAACAACCCTGGCGTTGGCAGTCGCCTTA
AGTTTCGCCTGGCAAGCGCCGGTATTTGCCCACGGTGGTGAAGCGCATATGGTGCCAATG
GATAAAACGCTTAAAGAATTTGGTGCCGATGTGCAGTGGGACGACTACGCCCAGCTCTTT
ACCCTGATTAAAGATGGCGCGTACGTGAAAGTGAAGCCTGGTGCGCAAACAGCAATTGTT
AATGGTCAGCCTCTGGCACTGCAAGTACCGGTAGTGATGAAAGACAATAAAGCCTGGGTT
TCTGACACCTTTATTAACGATGTTTTCCAGTCCGGGCTGGATCAAACTTTCCAGGTAGAA
AAGCGCCCTCACCCACTTAATGCGCTAACTGCGGACGAAATTAAACAGGCCGTTGAAATT
GTTAAAGCTTCCGCGGACTTCAAACCCAATACCCGTTTTACTGAGATCTCCCTGCTACCG
CCAGATAAAGAAGCTGTCTGGGCGTTTGCGCTGGAAAACAAACCGGTTGACCAGCCGCGC
AAAGCCGACGTCATTATGCTCGACGGCAAACATATCATCGAAGCGGTGGTGGATCTGCAA
AACAACAAACTGCTCTCCTGGCAACCCATTAAAGACGCCCACGGTATGGTGTTGCTGGAT
GATTTCGCCAGTGTGCAGAACATTATTAACAACAGTGAAGAATTTGCCGCTGCCGTGAAG
AAACGCGGTATTACTGATGCCGAAAAAGTGATTACCACGCCGCTGACCGTAGTTATTTTC
GATGGTAAAGATGGCCTGAAACAAGATGCCCGGTTGCTCAAAGTCATCATCAGCTATCTT
GATGTCGGTGATGGCAACTACTGGCACATCATCGAAAACCTGGTGGCGGTCGTTGATTTA
GAACAGAAAAAAATCGTTAAGATTGAAGAAGGTCCGGTAGTTCCGGTGCCAATGACCGCA
CGCCCATTTGATGGCCGTGACCGCGTTGCTCCGGCAGTTAAGCCTATGCAAATCATTGAG
CCTGAAGGTAAAAATTACACCATTACTGGCGATATGATTCACTGGCGGAACTGGGATTTT
CACCTCAGCATGAACTCGCGCGTCGGGCCGATGATCTCCACCGTGACTTATAACGACAAT
GGCACAAAACGCAAAGTCATGTACGAAGGTTCTCTCGGCGGCATGATTGTGCCTTACGGT
GATCCTGATATTGGCTGGTACTTTAAAGCGTATCTGGACTCTGGTGACTACGGTATGGGC
ACGCTAACCTCACCAATTGCTCGTGGTAAAGATGCCCCGTCTAACGCAGTGCTCCTTAAT
GAAACCATCGCCGACTACACTGGCGTGCCGATGGAGATCCCTCGGCCTATCGCGGTATTT
GAACGTTATGCCGGGCCGGAGTATAAGCATCAGGAAATGGGCCAGCCCAACGTCAGTACC
GAACGCCGGGAGTTAGTGGTGCGCTGGATCAGTACAGTGGGTAACTATGACTACATTTTT
GACTGGATCTTCCATGAAAACGGCACTATTGGCATCGATGCCGGTGCTACGGGCATCGAA
GCGGTGAAAGGTGTTAAAGCGAAAACCATGCACGATGAGACGGCGAAAGATGACACGCGC
TACGGCACGCTTATCGATCACAATATCGTGGGTACTACACACCAACATATTTATAATTTC
CGCCTCGATCTGGATGTAGATGGCGAGAATAACAGCCTGGTGGCGATGGACCCAGTGGTA
AAACCGAATACTGCCGGTGGCCCACGCACCAGTACCATGCAAGTTAATCAGTACAACATC
GGCAATGAACAGGATGCCGCACAGAAATTTGATCCGGGCACGATTCGTCTGTTGAGTAAC
CCGAACAAAGAGAACCGCATGGGCAATCCGGTTTCCTATCAAATTATTCCTTATGCAGGT
GGTACTCACCCGGTAGCAAAAGGTGCCCAGTTCGCGCCGGACGAGTGGATCTATGATCGT
TTAAGCTTTATGGACAAGCAGCTCTGGGTAACGCGTTATCATCCTGGCGAGCGTTTCCCG
GAAGGCAAATATCCGAACCGTTCTACTCATGACACCGGTCTTGGACAATACAGTAAGGAT
AACGAGTCGCTGGACAACACCGACGCCGTTGTCTGGATGACCACCGGCACCACACATGTG
GCCCGCGCCGAAGAGTGGCCGATTATGCCGACCGAATGGGTACATACTCTGCTGAAACCA
TGGAACTTCTTTGACGAAACGCCAACGCTAGGGGCGCTGAAGAAAGATAAGTGA
Enzyme 5 GenBank Gene ID D23670 Link Image
Enzyme 5 GeneCard ID Not Available
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF: Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure. 1995 Nov 15;3(11):1171-84. [PubMed Link Image]
  2. Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [PubMed Link Image]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  4. Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E: Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. [PubMed Link Image]
  5. Ferrandez A, Prieto MA, Garcia JL, Diaz E: Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli. FEBS Lett. 1997 Apr 7;406(1-2):23-7. [PubMed Link Image]
  6. Yamashita M, Azakami H, Yokoro N, Roh JH, Suzuki H, Kumagai H, Murooka Y: maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli. J Bacteriol. 1996 May;178(10):2941-7. [PubMed Link Image]
  7. Hanlon SP, Hill TK, Flavell MA, Stringfellow JM, Cooper RA: 2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression. Microbiology. 1997 Feb;143 ( Pt 2):513-8. [PubMed Link Image]
  8. Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE: Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction. Biochemistry. 1997 Feb 18;36(7):1608-20. [PubMed Link Image]
  9. Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ: The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants. Biochemistry. 1999 Jun 29;38(26):8217-27. [PubMed Link Image]
  10. Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE: Visualization of dioxygen bound to copper during enzyme catalysis. Science. 1999 Nov 26;286(5445):1724-8. [PubMed Link Image]
Enzyme 5 Metabolite References
  1. Schulz R, Antonin KH, Hoffmann E, Jedrychowski M, Nilsson E, Schick C, Bieck PR: Tyramine kinetics and pressor sensitivity during monoamine oxidase inhibition by selegiline. Clin Pharmacol Ther. 1989 Nov;46(5):528-36. [PubMed Link Image]
Enzyme 6 [top]
Enzyme 6 ID 15063
Enzyme 6 Name Aldehyde dehydrogenase 3B1 (Aldehyde dehydrogenase 3 family, member B1, isoform CRA_c) (cDNA FLJ77312, highly similar to Homo sapiens aldehyde dehydrogenase 3 family, member B1 (ALDH3B1),mRNA)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name ALDH3B1
Enzyme 6 Protein Sequence >Aldehyde dehydrogenase 3B1 (Aldehyde dehydrogenase 3 family, member B1, isoform CRA_c) (cDNA FLJ77312, highly similar to Homo sapiens aldehyde dehydrogenase 3 family, member B1 (ALDH3B1),mRNA) 
MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE
VSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNL
TLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHR
FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA
GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC
GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK
PLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFD
TFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL
Enzyme 6 Number of Residues 468
Enzyme 6 Molecular Weight 51840
Enzyme 6 Theoretical pI 7.67
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 Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 125950429 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID A3FMP9 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A3FMP9_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1407 bp 
ATGGACCCCCTTGGGGACACGCTGCGGCGACTGCGGGAGGCCTTCCACGCGGGGCGCACG
CGGCCAGCTGAGTTCCGGGCTGCGCAGCTCCAAGGCCTGGGCCGCTTCCTGCAAGAAAAC
AAGCAGCTTCTGCACGACGCACTGGCCCAGGACCTGCACAAGTCAGCCTTCGAGTCGGAG
GTGTCTGAGGTTGCCATCAGCCAGGGCGAGGTCACCCTGGCCCTCAGGAACCTCCGGGCC
TGGATGAAGGACGAGCGTGTGCCCAAGAACCTGGCCACGCAGCTGGACTCCGCCTTCATC
CGGAAGGAGCCCTTTGGCCTGGTCCTCATCATTGCGCCCTGGAACTATCCGCTGAACCTG
ACGCTGGTGCCCCTCGTGGGAGCCCTCGCTGCAGGGAACTGTGTGGTGCTGAAGCCATCG
GAGATTAGCAAGAACGTCGAGAAGATCCTGGCCGAGGTGCTGCCCCAATACGTGGACCAG
AGCTGCTTTGCTGTGGTGCTGGGCGGGCCCCAGGAGACGGGGCAGCTGCTAGAGCACAGG
TTCGACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTTATGACTGCTGCC
GCCAAGCACCTGACACCTGTCACCCTGGAGCTGGGGGGCAAGAACCCTTGCTACGTGGAC
GACAACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCCGCTACTTCAACGCC
GGCCAGACCTGCGTGGCCCCCGACTACGTCCTATGCAGCCCTGAGATGCAGGAGAGGCTG
CTGCCTGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCA
AACCTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGC
GGCCGTGTGGCCATTGGGGGCCAGAGCGATGAGAGCGATCGCTACATCGCCCCCACGGTG
CTGGTGGATGTGCAGGAGATGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTG
CCCATCGTGAACGTGCAGAGCTTGGACGAGGCCATCGAGTTCATCAACCGGCGGGAGAAG
CCCCTGGCCCTGTACGCCTTCTCCAACAGCAGCCAGGTGGTCAAGCGGGTGCTGACCCAG
ACCAGCAGCGGGGGCTTCTGTGGGAACGACGGCTTCATGCACATGACCCTGGCCAGCCTG
CCTTTTGGAGGAGTGGGTGCCAGTGGGATGGGCCGGTACCATGGCAAGTTCTCCTTCGAC
ACCTTCTCCCACCATCGCGCCTGCCTCCTGCGCAGCCCGGGGATGGAGAAGCTCAACGCC
CTCCGCTACCCGCCGCAATCGCCGCGCCGCCTGAGGATGCTGCTGGTGGCCATGGAGGCC
CAAGGCTGCAGCTGCACACTGCTCTGA
Enzyme 6 GenBank Gene ID EF411198 Link Image
Enzyme 6 GeneCard ID A3FMP9 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 11
Enzyme 6 Locus 11q13
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available