ADH1A

ADH1A
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesADH1A, ADH1, alcohol dehydrogenase 1A (class I), alpha polypeptide
External IDsHomoloGene: 88335 GeneCards: ADH1A
EC number1.1.1.1
Gene location (Human)
Chr.Chromosome 4 (human)[1]
Band4q23Start99,276,367 bp[1]
End99,291,028 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

124

n/a

Ensembl

ENSG00000187758

n/a

UniProt

P07327

n/a

RefSeq (mRNA)

NM_000667

n/a

RefSeq (protein)

NP_000658

n/a

Location (UCSC)Chr 4: 99.28 – 99.29 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Alcohol dehydrogenase 1A is an enzyme that in humans is encoded by the ADH1A gene.[3][4]

This gene encodes class I alcohol dehydrogenase, alpha subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster. This gene is monomorphic and predominant in fetal and infant livers, whereas the genes encoding beta and gamma subunits are polymorphic and strongly expressed in adult livers.[4]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000187758 - Ensembl, May 2017
  2. ↑ "Human PubMed Reference:".
  3. ↑ Smith M (Mar 1986). "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet. 15: 249–90. doi:10.1007/978-1-4615-8356-1_5. ISBN 978-1-4615-8358-5. PMID 3006456.
  4. 1 2 "Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide".

Further reading

  • Lange LG, Sytkowski AJ, Vallee BL (1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features". Biochemistry. 15 (21): 4687–93. doi:10.1021/bi00666a023. PMID 9982.
  • van Ooij C, Snyder RC, Paeper BW, Duester G (1992). "Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein". Mol. Cell. Biol. 12 (7): 3023–31. PMC 364516. PMID 1620113.
  • Stewart MJ, McBride MS, Winter LA, Duester G (1990). "Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box". Gene. 90 (2): 271–9. doi:10.1016/0378-1119(90)90190-3. PMID 2169444.
  • Yasunami M, Kikuchi I, Sarapata D, Yoshida A (1990). "The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome". Genomics. 7 (2): 152–8. doi:10.1016/0888-7543(90)90535-3. PMID 2347582.
  • Tsukahara M, Yoshida A (1989). "Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization". Genomics. 4 (2): 218–20. doi:10.1016/0888-7543(89)90304-2. PMID 2737681.
  • Matsuo Y, Yokoyama S (1989). "Molecular structure of the human alcohol dehydrogenase 1 gene". FEBS Lett. 243 (1): 57–60. doi:10.1016/0014-5793(89)81217-7. PMID 2920825.
  • Ikuta T, Szeto S, Yoshida A (1986). "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence". Proc. Natl. Acad. Sci. U.S.A. 83 (3): 634–8. doi:10.1073/pnas.83.3.634. PMC 322918. PMID 2935875.
  • von Bahr-Lindström H, Höög JO, Hedén LO, et al. (1986). "cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase". Biochemistry. 25 (9): 2465–70. doi:10.1021/bi00357a026. PMID 3013304.
  • Duester G, Farrés J, Felder MR, et al. (1999). "Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family". Biochem. Pharmacol. 58 (3): 389–95. doi:10.1016/S0006-2952(99)00065-9. PMID 10424757.
  • Rodriguez-Zavala JS, Weiner H (2002). "Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation". Biochemistry. 41 (26): 8229–37. doi:10.1021/bi012081x. PMID 12081471.
  • Sandberg M, Yasar U, Strömberg P, et al. (2003). "Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase". British Journal of Clinical Pharmacology. 54 (4): 423–9. doi:10.1046/j.1365-2125.2002.01660.x. PMC 1874434. PMID 12392591.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Dannenberg LO, Chen HJ, Edenberg HJ (2006). "GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene". DNA Cell Biol. 24 (9): 543–52. doi:10.1089/dna.2005.24.543. PMID 16153155.
  • Jelski W, Chrostek L, Szmitkowski M (2007). "The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer". Pancreas. 35 (2): 142–6. doi:10.1097/MPA.0b013e318053eae2. PMID 17632320.


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