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Human Metabolome Database Version 2.5

 

Showing metabocard for 3,4-Dihydroxyphenylglycol (HMDB00318)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-13 13:51:08
Accession Number HMDB00318
Secondary Accession Numbers HMDB05870
Common Name 3,4-Dihydroxyphenylglycol
Description 3,4-Dihydroxyphenylglycol (DOPEG) is a normal norepinephrine metabolite present in CSF, plasma and urine in humans (PMID 6875564). In healthy individuals there is a tendency for free DOPEG to increase and for conjugated DOPEG to decrease with age; plasmatic DOPEG levels are significantly lower in depressed patients as compared to healthy controls (PMID 6671452).
Synonyms
  1. (3,4-Dihydroxyphenyl)ethylene glycol
  2. 3,4-Dihydroxyphenylethyleneglycol
  3. 1-(3,4-Dihydroxyphenyl)-1,2-ethanediol
  4. 3,4-Dihydroxyphenethyl glycol
  5. 3,4-Dihydroxyphenylethyl glycol
  6. DHPG
  7. DL-3,4-Dihydroxyphenylglycol
  8. DOPEG
  9. 4-(1,2-dihydroxyethyl)-1,2-benzenediol
Chemical IUPAC Name 4-(1,2-dihydroxyethyl)benzene-1,2-diol
Chemical Formula C8H10O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohols and Polyols
  • Polyphenols
Sub Class
  • Phenols
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • phenol or hydroxyhetarene
  • 1,2-diphenol
  • aromatic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 170.163
Monoisotopic Molecular Weight 170.057907
Isomeric SMILES OCC(O)C1=CC(O)=C(O)C=C1
Canonical SMILES OCC(O)C1=CC(O)=C(O)C=C1
KEGG Compound ID C05576 Link Image
BioCyc ID Not Available
BiGG ID 46054 Link Image
Wikipedia Link DHPG Link Image
NuGOwiki Link HMDB00318 Link Image
Metagene Link HMDB00318 Link Image
METLIN ID 5307 Link Image
PubChem Compound 91528 Link Image
PubChem Substance 10224860 Link Image
ChEBI ID Not Available
CAS Registry Number 28822-73-3
InChI Identifier InChI=1/C8H10O4/c9-4-8(12)5-1-2-6(10)7(11)3-5/h1-3,8-12H,4H2
Synthesis Reference Hunter L W; Rorie D K; Yaksh T L; Tyce G M Concurrent separation of catecholamines, dihydroxyphenylglycol, vasoactive intestinal peptide, and neuropeptide Y in superfusate and tissue extract. Analytical biochemistry (1988), 173(2), 340-52.
Melting Point (Experimental) 130-132 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 16.699999 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -1.01 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -0.72 [Predicted by ALOGPS]; -0.14 [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 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
  • Extracellular
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Adrenal Medulla —
Brain —
Nerve Cells —
Concentrations (Normal)
Biofluid Blood
Value 0.008 +/- 0.005 uM
Age Infant:0-1 yr old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Kaler SG, Holmes CS, Goldstein DS, Tang J, Godwin SC, Donsante A, Liew CJ, Sato S, Patronas N: Neonatal diagnosis and treatment of Menkes disease. N Engl J Med. 2008 Feb 7;358(6):605-14. [PubMed Link Image]
Biofluid Blood
Value 0.009 +/- 0.003 uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Kaler SG, Holmes CS, Goldstein DS, Tang J, Godwin SC, Donsante A, Liew CJ, Sato S, Patronas N: Neonatal diagnosis and treatment of Menkes disease. N Engl J Med. 2008 Feb 7;358(6):605-14. [PubMed Link Image]
Biofluid Blood
Value 0.006 +/- 0.0016 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Izzo JL Jr, Greulich D: Radioenzymatic assay for plasma dihydroxyphenylglycol (DHPG), dihydroxymandelic acid (DOMA) and dihydroxyphenylacetic acid (DOPAC). Life Sci. 1983 Aug 1;33(5):483-8. [PubMed Link Image]
Biofluid Urine
Value 0.25 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal)
Biofluid Blood
Value 0.002 +/- 0.001 uM
Age Infant:0-1 yr old
Sex N/A
Condition Menkes disease
Comments Not Available
References
  • Kaler SG, Holmes CS, Goldstein DS, Tang J, Godwin SC, Donsante A, Liew CJ, Sato S, Patronas N: Neonatal diagnosis and treatment of Menkes disease. N Engl J Med. 2008 Feb 7;358(6):605-14. [PubMed Link Image]
Biofluid Blood
Value 0.004 +/- 0.002 uM
Age Newborn:0-30 days old
Sex Both
Condition Menkes disease
Comments Not Available
References
  • Kaler SG, Holmes CS, Goldstein DS, Tang J, Godwin SC, Donsante A, Liew CJ, Sato S, Patronas N: Neonatal diagnosis and treatment of Menkes disease. N Engl J Med. 2008 Feb 7;358(6):605-14. [PubMed Link Image]
Associated Disorders
Condition References
Menkes disease
  • Kaler SG, Holmes CS, Goldstein DS, Tang J, Godwin SC, Donsante A, Liew CJ, Sato S, Patronas N: Neonatal diagnosis and treatment of Menkes disease. N Engl J Med. 2008 Feb 7;358(6):605-14. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
General References
  1. Julien C, Rodriguez C, Sacquet J, Cuisinaud G, Sassard J: Liquid-chromatographic determination of free and total 3,4-dihydroxyphenylglycol and 3-methoxy-4-hydroxyphenylglycol in urine. Clin Chem. 1988 May;34(5):966-9. [PubMed Link Image]
  2. Nakada T, Sasagawa I, Kubota Y, Suzuki H, Ishigooka M, Watanabe M: Dihydroxyphenylglycol in pheochromocytoma: its diagnostic use for norepinephrine dominant tumor. J Urol. 1996 Jan;155(1):14-8. [PubMed Link Image]
  3. Eisenhofer G, Brush JE, Cannon RO 3rd, Stull R, Kopin IJ, Goldstein DS: Plasma dihydroxyphenylalanine and total body and regional noradrenergic activity in humans. J Clin Endocrinol Metab. 1989 Feb;68(2):247-55. [PubMed Link Image]
  4. Divers WA Jr, Wilkes MM, Babaknia A, Yen SS: Maternal smoking and elevation of catecholamines and metabolites in the amniotic fluid. Am J Obstet Gynecol. 1981 Nov 15;141(6):625-8. [PubMed Link Image]
  5. Graham PE, Smythe GA, Edwards GA, Lazarus L: Laboratory diagnosis of phaeochromocytoma: which analytes should we measure? Ann Clin Biochem. 1993 Mar;30 ( Pt 2):129-34. [PubMed Link Image]
  6. Machida M, Sakaguchi A, Kamada S, Fujimoto T, Takechi S, Kakinoki S, Nomura A: Simultaneous analysis of human plasma catecholamines by high-performance liquid chromatography with a reversed-phase triacontylsilyl silica column. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Jan 18;830(2):249-54. Epub 2005 Nov 21. [PubMed Link Image]
  7. Eisenhofer G, Kopin IJ, Goldstein DS: Catecholamine metabolism: a contemporary view with implications for physiology and medicine. Pharmacol Rev. 2004 Sep;56(3):331-49. [PubMed Link Image]
  8. Baskys A, Fang L, Bayazitov I: Activation of neuroprotective pathways by metabotropic group I glutamate receptors: a potential target for drug discovery? Ann N Y Acad Sci. 2005 Aug;1053:55-73. [PubMed Link Image]
  9. Esler MD, Lambert GW, Ferrier C, Kaye DM, Wallin BG, Kalff V, Kelly MJ, Jennings GL: Central nervous system noradrenergic control of sympathetic outflow in normotensive and hypertensive humans. Clin Exp Hypertens. 1995 Jan-Feb;17(1-2):409-23. [PubMed Link Image]
  10. Divers WA, Wilkes MM, Babaknia A, Hill LM, Quilligan EJ, Yen SS: Amniotic fluid catecholamines and metabolites in intrauterine growth retardation. Am J Obstet Gynecol. 1981 Nov 15;141(6):608-10. [PubMed Link Image]
  11. Elsworth JD, Roth RH, Redmond DE Jr: Relative importance of 3-methoxy-4-hydroxyphenylglycol and 3,4-dihydroxyphenylglycol as norepinephrine metabolites in rat, monkey, and humans. J Neurochem. 1983 Sep;41(3):786-93. [PubMed Link Image]
  12. Wikipedia Link Image
Metabolic Enzymes
  1. Catechol O-methyltransferase
  2. Alcohol dehydrogenase class 3
  3. Alcohol dehydrogenase 1B
  4. Alcohol dehydrogenase 1C
  5. cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
  6. cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
  7. Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
  8. cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
Enzyme 1 [top]
Enzyme 1 ID 5504
Enzyme 1 Name Catechol O-methyltransferase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name COMT
Enzyme 1 Protein Sequence >Catechol O-methyltransferase 
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
Enzyme 1 Number of Residues 271
Enzyme 1 Molecular Weight 30037
Enzyme 1 Theoretical pI 5.15
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 Not Available
Enzyme 1 Specific Function Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol
Enzyme 1 Pathways
Enzyme 1 Reactions
  • S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-32
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 180920 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P21964 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name COMT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >816 bp 
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
Enzyme 1 GenBank Gene ID M65212 Link Image
Enzyme 1 GeneCard ID COMT Link Image
Enzyme 1 GenAtlas ID COMT Link Image
Enzyme 1 HGNC ID HGNC:2228 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q11.21-q11.23|22q11.21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Lundstrom K, Salminen M, Jalanko A, Savolainen R, Ulmanen I: Cloning and characterization of human placental catechol-O-methyltransferase cDNA. DNA Cell Biol. 1991 Apr;10(3):181-9. [PubMed Link Image]
  2. Bertocci B, Miggiano V, Da Prada M, Dembic Z, Lahm HW, Malherbe P: Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1416-20. [PubMed Link Image]
  3. Tenhunen J, Salminen M, Lundstrom K, Kiviluoto T, Savolainen R, Ulmanen I: Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters. Eur J Biochem. 1994 Aug 1;223(3):1049-59. [PubMed Link Image]
  4. Tilgmann C, Kalkkinen N: Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme. Biochem Biophys Res Commun. 1991 Jan 31;174(2):995-1002. [PubMed Link Image]
  5. Ulmanen I, Lundstrom K: Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur J Biochem. 1991 Dec 18;202(3):1013-20. [PubMed Link Image]
  6. Lachman HM, Papolos DF, Saito T, Yu YM, Szumlanski CL, Weinshilboum RM: Human catechol-O-methyltransferase pharmacogenetics: description of a functional polymorphism and its potential application to neuropsychiatric disorders. Pharmacogenetics. 1996 Jun;6(3):243-50. [PubMed Link Image]
  7. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6060
Enzyme 2 Name Alcohol dehydrogenase class 3
Enzyme 2 Synonyms
  1. Alcohol dehydrogenase class III
  2. Alcohol dehydrogenase class chi chain
  3. S-
  4. hydroxymethylglutathione dehydrogenase
  5. Glutathione- dependent formaldehyde dehydrogenase
  6. FDH
Enzyme 2 Gene Name ADH5
Enzyme 2 Protein Sequence >Alcohol dehydrogenase class 3 
MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGC
FPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGK
GLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGY
GAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATEC
INPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEE
IATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFE
LMHSGKSIRTVVKI
Enzyme 2 Number of Residues 374
Enzyme 2 Molecular Weight 39725
Enzyme 2 Theoretical pI 7.54
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
—
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione
Enzyme 2 Pathways
Enzyme 2 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + 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 178134 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P11766 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ADHX_HUMAN Link Image
Enzyme 2 PDB ID 1MC5 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1125 bp 
ATGGCGAACGAGGTTATCAAGTGCAAGGCTGCAGTTGCTTGGGAGGCTGGAAAGCCTCTC
TCCATAGAGGAGATAGAGGTGGCACCCCCAAAGGCTCATGAAGTTCGAATCAAGATCATT
GCCACTGCGGTTTGCCACACCGATGCCTATACCCTGAGTGGAGCTGATCCTGAGGGTTGT
TTTCCAGTGATCTTGGGACATGAAGGTGCTGGAATTGTGGAAAGTGTTGGTGAGGGAGTT
ACTAAGCTGAAGGCGGGTGACACTGTCATCCCACTTTACATCCCACAGTGTGGAGAATGC
AAATTTTGTCTAAATCCTAAAACTAACCTTTGCCAGAAGATAAGAGTCACTCAAGGGAAA
GGATTAATGCCAGATGGTACCAGCAGATTTACTTGCAAAGGAAAGACAATTTTGCATTAC
ATGGGAACCAGCACATTTTCTGAATACACAGTTGTGGCTGATATCTCTGTTGCTAAAATA
GATCCTTTAGCACCTTTGGATAAAGTCTGCCTTCTAGGTTGTGGCATTTCAACCGGTTAT
GGTGCTGCTGTGAACACTGCCAAGTTGGAGCCTGGCTCTGTTTGTGCCGTCTTTGGTCTG
GGAGGAGTCGGATTGGCAGTTATCATGGGCTGTAAAGTGGCTGGTGCTTCCCGGATCATT
GGTGTGGACATCAATAAAGATAAATTTGCAAGGGCCAAAGAGTTTGGAGCCACTGAATGT
ATTAACCCTCAGGATTTTAGTAAACCCATCCAGGAAGTGCTCATTGAGATGACCGATGGA
GGAGTGGACTATTCCTTTGAATGTATTGGTAATGTGAAGGTCATGAGAGCAGCACTTGAG
GCATGTCACAAGGGCTGGGGCGTCAGCGTCGTGGTTGGAGTAGCTGCTTCAGGTGAAGAA
ATTGCCACTCGTCCATTCCAGCTGGTAACAGGTCGCACATGGAAAGGCACTGCCTTTGGA
GGATGGAAGAGTGTAGAAAGTGTCCCAAAGTTGGTGTCTGAATATATGTCCAAAAAGATA
AAAGTTGATGAATTTGTGACTCACAATCTGTCTTTTGATGAAATCAACAAAGCCTTTGAA
CTGATGCATTCTGGAAAGAGCATTCGAACTGTTGTAAAGATTTAA
Enzyme 2 GenBank Gene ID M30471 Link Image
Enzyme 2 GeneCard ID ADH5 Link Image
Enzyme 2 GenAtlas ID ADH5 Link Image
Enzyme 2 HGNC ID HGNC:253 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q21-q25
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Sharma CP, Fox EA, Holmquist B, Jornvall H, Vallee BL: cDNA sequence of human class III alcohol dehydrogenase. Biochem Biophys Res Commun. 1989 Oct 31;164(2):631-7. [PubMed Link Image]
  2. Giri PR, Krug JF, Kozak C, Moretti T, O'Brien SJ, Seuanez HN, Goldman D: Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA. Biochem Biophys Res Commun. 1989 Oct 16;164(1):453-60. [PubMed Link Image]
  3. Hur MW, Edenberg HJ: Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase. Gene. 1992 Nov 16;121(2):305-11. [PubMed Link Image]
  4. Kaiser R, Holmquist B, Hempel J, Vallee BL, Jornvall H: Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes. Biochemistry. 1988 Feb 23;27(4):1132-40. [PubMed Link Image]
  5. Holmquist B, Moulis JM, Engeland K, Vallee BL: Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Biochemistry. 1993 May 18;32(19):5139-44. [PubMed Link Image]
  6. Engeland K, Hoog JO, Holmquist B, Estonius M, Jornvall H, Vallee BL: Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2491-4. [PubMed Link Image]
  7. Yang ZN, Bosron WF, Hurley TD: Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J Mol Biol. 1997 Jan 24;265(3):330-43. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6062
Enzyme 3 Name Alcohol dehydrogenase 1B
Enzyme 3 Synonyms
  1. Alcohol dehydrogenase beta subunit
Enzyme 3 Gene Name ADH1B
Enzyme 3 Protein Sequence >Alcohol dehydrogenase 1B 
MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNP
RGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQ
NLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTVLTF
Enzyme 3 Number of Residues 375
Enzyme 3 Molecular Weight 39855
Enzyme 3 Theoretical pI 8.38
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
—
Component
—
Enzyme 3 General Function Energy production and conversion
Enzyme 3 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 3 Pathways
Enzyme 3 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + 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 178098 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P00325 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ADH1B_HUMAN Link Image
Enzyme 3 PDB ID 1HSZ Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1128 bp 
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGGTAAAGAAA
CCCTTTTCCATTGAGGATGTGGAGGTTGCACCTCCTAAGGCTTATGAAGTTCGCATTAAG
ATGGTGGCTGTAGGAATCTGTCGCACAGATGACCACGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAGTTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGGGGGAAGCCCATTCACCAC
TTCCTTGGCACCAGCACCTTCTCCCAGTACACGGTGGTGGATGAGAATGCAGTGGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTCTCGACTGGT
TATGGGTCTGCAGTTAACGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAAAAAGCAAAGGCCAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATCCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGCGTCATCGTAGGGGTACCTCCTGCTTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACCTGGAAGGGGGCTGTTTAT
GGTGGCTTTAAGAGTAAAGAAGGTATCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCACTGGATGCGTTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCGTCCTGACGTTTTGA
Enzyme 3 GenBank Gene ID M24317 Link Image
Enzyme 3 GeneCard ID ADH1B Link Image
Enzyme 3 GenAtlas ID ADH1B Link Image
Enzyme 3 HGNC ID HGNC:250 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q21-q23
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Heden LO, Hoog JO, Larsson K, Lake M, Lagerholm E, Holmgren A, Vallee BL, Jornvall H, von Bahr-Lindstrom H: cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions. FEBS Lett. 1986 Jan 6;194(2):327-32. [PubMed Link Image]
  2. Duester G, Smith M, Bilanchone V, Hatfield GW: Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. J Biol Chem. 1986 Feb 15;261(5):2027-33. [PubMed Link Image]
  3. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed Link Image]
  4. Carr LG, Xu Y, Ho WH, Edenberg HJ: Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit. Alcohol Clin Exp Res. 1989 Aug;13(4):594-6. [PubMed Link Image]
  5. Matsuo Y, Yokoyama R, Yokoyama S: The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide. Eur J Biochem. 1989 Aug 1;183(2):317-20. [PubMed Link Image]
  6. Hempel J, Buhler R, Kaiser R, Holmquist B, de Zalenski C, von Wartburg JP, Vallee B, Jornvall H: Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme. Eur J Biochem. 1984 Dec 17;145(3):437-45. [PubMed Link Image]
  7. Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ: Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification. Genomics. 1988 Apr;2(3):209-14. [PubMed Link Image]
  8. Jornvall H, Hempel J, Vallee BL, Bosron WF, Li TK: Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme. Proc Natl Acad Sci U S A. 1984 May;81(10):3024-8. [PubMed Link Image]
  9. Burnell JC, Carr LG, Dwulet FE, Edenberg HJ, Li TK, Bosron WF: The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding. Biochem Biophys Res Commun. 1987 Aug 14;146(3):1127-33. [PubMed Link Image]
  10. Hurley TD, Bosron WF, Hamilton JA, Amzel LM: Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. [PubMed Link Image]
  11. Hurley TD, Bosron WF, Stone CL, Amzel LM: Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. J Mol Biol. 1994 Jun 10;239(3):415-29. [PubMed Link Image]
  12. Davis GJ, Bosron WF, Stone CL, Owusu-Dekyi K, Hurley TD: X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J Biol Chem. 1996 Jul 19;271(29):17057-61. [PubMed Link Image]
  13. Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 2001 Apr;10(4):697-706. [PubMed Link Image]
  14. Borras E, Coutelle C, Rosell A, Fernandez-Muixi F, Broch M, Crosas B, Hjelmqvist L, Lorenzo A, Gutierrez C, Santos M, Szczepanek M, Heilig M, Quattrocchi P, Farres J, Vidal F, Richart C, Mach T, Bogdal J, Jornvall H, Seitz HK, Couzigou P, Pares X: Genetic polymorphism of alcohol dehydrogenase in europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1. Hepatology. 2000 Apr;31(4):984-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6066
Enzyme 4 Name Alcohol dehydrogenase 1C
Enzyme 4 Synonyms
  1. Alcohol dehydrogenase gamma subunit
Enzyme 4 Gene Name ADH1C
Enzyme 4 Protein Sequence >Alcohol dehydrogenase 1C 
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNP
RGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGF
DLLRSGKSIRTVLTF
Enzyme 4 Number of Residues 375
Enzyme 4 Molecular Weight 39868
Enzyme 4 Theoretical pI 8.38
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
—
Component
—
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 4 Pathways
Enzyme 4 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + 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 28404 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P00326 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ADH1G_HUMAN Link Image
Enzyme 4 PDB ID 1HT0 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1128 bp 
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTAGAGGTTGCACCTCCTAAGGCTCATGAAGTTCGCATTAAG
ATGGTGGCTGCAGGAATCTGTCGTTCAGATGAGCATGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAAAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAATTTGCAAAAACCCAGAAAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGCGGGAAGCCCATCCACCAC
TTCGTCGGCGTCAGCACCTTCTCCCAGTACACAGTGGTGGATGAGAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTTTCGACTGGT
TATGGGTCTGCAGTCAAAGTTGCCAAGGTCACCCCAGGGTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGTTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCTGTGGACATCAACAAGGACAAATTTGCAAAGGCTAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATTCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCAGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATTGTAGGGGTACCTCCTGATTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACGTGGAAAGGAGCTATTTTT
GGAGGCTTTAAGAGTAAAGAATCTGTCCCCAAACTTGTGGCTGACTTTATGGCTAAGAAG
TTTTCACTGGATGCATTAATAACAAATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCGCTCTGGAAAGAGTATCCGTACCGTCCTGACGTTTTGA
Enzyme 4 GenBank Gene ID X04299 Link Image
Enzyme 4 GeneCard ID ADH1C Link Image
Enzyme 4 GenAtlas ID ADH1C Link Image
Enzyme 4 HGNC ID HGNC:251 Link Image
Enzyme 4 Chromosome Location 4
Enzyme 4 Locus 4q21-q23
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Hoog JO, Heden LO, Larsson K, Jornvall H, von Bahr-Lindstrom H: The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties. Eur J Biochem. 1986 Sep 1;159(2):215-8. [PubMed Link Image]
  2. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed Link Image]
  3. Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R: Molecular structure of the human alcohol dehydrogenase 3 gene. Jpn J Genet. 1992 Apr;67(2):167-71. [PubMed Link Image]
  4. Buhler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jornvall H: Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain. Eur J Biochem. 1984 Dec 17;145(3):447-53. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13004
Enzyme 5 Name cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
Enzyme 5 Synonyms
  1. ADH1alpha subunit mRNA
  2. Alcohol dehydrogenase 1A
  3. Class I, alpha polypeptide, isoform CRA_b
Enzyme 5 Gene Name ADH1A
Enzyme 5 Protein Sequence >cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase 
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNP
QGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTILMF
Enzyme 5 Number of Residues 375
Enzyme 5 Molecular Weight 39859
Enzyme 5 Theoretical pI 8.02
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158254548 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A8K3E3 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8K3E3_HUMAN Link Image
Enzyme 5 PDB ID 1HSO Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK290558 Link Image
Enzyme 5 GeneCard ID A8K3E3 Link Image
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 Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15205
Enzyme 6 Name cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name Not Available
Enzyme 6 Protein Sequence >cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA 
MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEG
LAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLK
SPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGC
GFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKA
LGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGV
AAGSKGLTIFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDK
ISEAFDLMNQGKSVRTILIF
Enzyme 6 Number of Residues 380
Enzyme 6 Molecular Weight 40222
Enzyme 6 Theoretical pI 8.01
Enzyme 6 GO Classification Not Available
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 Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 158255106 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID A8K470 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A8K470_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1143 bp 
ATGGGCACCAAGGGCAAAGTTATTAAATGCAAAGCAGCCATCGCCTGGGAAGCAGGCAAG
CCCCTTTGCATTGAAGAGGTTGAAGTAGCTCCCCCCAAGGCTCATGAAGTTCGCATTCAG
ATCATTGCTACCTCCCTGTGCCATACTGATGCCACTGTTATCGATTCTAAATTTGAGGGC
CTAGCTTTCCCAGTGATCGTTGGCCATGAGGCTGCAGGTATTGTGGAAAGTATTGGGCCA
GGAGTGACCAACGTCAAACCAGGTGACAAAGTAATTCCACTTTATGCACCTCTATGTAGA
AAATGCAAGTTTTGTCTGAGTCCACTCACAAATTTGTGTGGGAAAATCAGTAATCTCAAA
AGTCCTGCTAGTGATCAACAACTAATGGAAGACAAAACCAGCAGGTTTACCTGCAAAGGA
AAACCAGTTTACCATTTCTTTGGAACCAGTACATTCTCTCAGTACACTGTGGTGTCAGAT
ATCAATCTTGCCAAAATAGATGATGATGCAAATTTAGAGAGAGTTTGTCTGCTTGGATGT
GGGTTTTCAACTGGCTATGGGGCTGCAATCAACAATGCCAAGGTCACCCCTGGTTCGACT
TGTGCTGTCTTTGGCCTAGGAGGTGTGGGTCTTTCTGCTGTAATGGGTTGTAAAGCAGCA
GGAGCTTCCAGAATCATAGGTATTGACATCAACAGTGAGAAGTTTGTGAAGGCTAAAGCC
CTGGGAGCCACTGACTGCCTCAATCCTAGAGACTTACATAAACCAATCCAGGAAGTTATC
ATTGAATTGACCAAGGGAGGTGTGGATTTTGCCCTTGACTGTGCAGGTGGATCTGAAACC
ATGAAAGCAGCCCTGGACTGTACAACCGCAGGCTGGGGATCATGTACTTTCATTGGAGTA
GCTGCTGGTAGCAAAGGATTGACTATTTTTCCAGAGGAGCTAATAATCGGCCGTACTATA
AATGGAACATTCTTTGGTGGTTGGAAAAGTGTAGATTCTATCCCAAAGCTGGTCACTGAC
TATAAGAATAAGAAATTCAATCTGGATGCATTGGTGACCCATACCCTGCCTTTTGACAAA
ATCAGTGAGGCATTTGACCTAATGAACCAAGGAAAAAGCGTCCGAACAATCCTCATCTTT
TGA
Enzyme 6 GenBank Gene ID AK290835 Link Image
Enzyme 6 GeneCard ID A8K470 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs Not Available
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15206
Enzyme 7 Name Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name ADH7
Enzyme 7 Protein Sequence >Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide 
MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICR
TDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPD
GNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEK
VCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDK
FEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGT
SVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITH
VLPFKKISEGFELLNSGQSIRTVLTF
Enzyme 7 Number of Residues 386
Enzyme 7 Molecular Weight 41482
Enzyme 7 Theoretical pI 7.94
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
—
Component
—
Enzyme 7 General Function Energy production and conversion
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 124297943 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID A2RRB6 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name A2RRB6_HUMAN Link Image
Enzyme 7 PDB ID 1D1S Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1161 bp 
ATGTTTGCAGAAATACAGATCCAAGACAAAGACAGGATGGGCACTGCTGGAAAAGTTATT
AAATGCAAAGCAGCTGTGCTTTGGGAGCAGAAGCAACCCTTCTCCATTGAGGAAATAGAA
GTTGCCCCACCAAAGACTAAAGAAGTTCGCATTAAGATTTTGGCCACAGGAATCTGTCGC
ACAGATGACCATGTGATAAAAGGAACAATGGTGTCCAAGTTTCCAGTGATTGTGGGACAT
GAGGCAACTGGGATTGTAGAGAGCATTGGAGAAGGAGTGACTACAGTGAAACCAGGTGAC
AAAGTCATCCCTCTCTTTCTGCCACAATGTAGAGAATGCAATGCTTGTCGCAACCCAGAT
GGCAACCTTTGCATTAGGAGCGATATTACTGGTCGTGGAGTACTGGCTGATGGCACCACC
AGATTTACATGCAAGGGCAAACCAGTCCACCACTTCATGAACACCAGTACATTTACCGAG
TACACAGTGGTGGATGAATCTTCTGTTGCTAAGATTGATGATGCAGCTCCTCCTGAGAAA
GTCTGTTTAATTGGCTGTGGGTTTTCCACTGGATATGGCGCTGCTGTTAAAACTGGCAAG
GTCAAACCTGGTTCCACTTGCGTCGTCTTTGGCCTGGGAGGAGTTGGCCTGTCAGTCATC
ATGGGCTGTAAGTCAGCTGGTGCATCTAGGATCATTGGGATTGACCTCAACAAAGACAAA
TTTGAGAAGGCCATGGCTGTAGGTGCCACTGAGTGTATCAGTCCCAAGGACTCTACCAAA
CCCATCAGTGAGGTGCTGTCAGAAATGACAGGCAACAACGTGGGATACACCTTTGAAGTT
ATTGGGCATCTTGAAACCATGATTGATGCCCTGGCATCCTGCCACATGAACTATGGGACC
AGCGTGGTTGTAGGAGTTCCTCCATCAGCCAAGATGCTCACCTATGACCCGATGTTGCTC
TTCACTGGACGCACATGGAAGGGATGTGTCTTTGGAGGTTTGAAAAGCAGAGATGATGTC
CCAAAACTAGTGACTGAGTTCCTGGCAAAGAAATTTGACCTGGACCAGTTGATAACTCAT
GTTTTACCATTTAAAAAAATCAGTGAAGGATTTGAGCTGCTCAATTCAGGACAAAGCATT
CGAACGGTCCTGACGTTTTGA
Enzyme 7 GenBank Gene ID BC131512 Link Image
Enzyme 7 GeneCard ID A2RRB6 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16485
Enzyme 8 Name cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name Not Available
Enzyme 8 Protein Sequence >cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1) 
MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLD
LLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK
TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTG
FGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE
CLNPQDLKKPIQEVLFDMTDAGIDFRFEAIGNLDVLAAALASCNESYGVCVVVGVLPASV
QLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAV
ELMKTGKCIRCILLL
Enzyme 8 Number of Residues 375
Enzyme 8 Molecular Weight 39868
Enzyme 8 Theoretical pI 8.09
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
—
Component
—
Enzyme 8 General Function Energy production and conversion
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326 R07327] ALL_REAC R07326 > R00623 R00754 R01036 R04805 R04880 R06917 R06927
  • R07327 > R00624
  • (other) R01041 R05233 R05234 R07105
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID B3KS45 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B3KS45_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK092768 Link Image
Enzyme 8 GeneCard ID B3KS45 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs Not Available
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available