ADH1A

Alcohol dehydrogenase 1A (class I), alpha polypeptide, also known as ADH1A, is a human gene.cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Smith M |title=Genetics of human alcohol and aldehyde dehydrogenases. |journal=Adv. Hum. Genet. |volume=15 |issue= |pages= 249–90 |year= 1986 |pmid= 3006456 |doi=
*cite journal | author=Lange LG, Sytkowski AJ, Vallee BL |title=Human liver alcohol dehydrogenase: purification, composition, and catalytic features. |journal=Biochemistry |volume=15 |issue= 21 |pages= 4687–93 |year= 1976 |pmid= 9982 |doi=
*cite journal | author=van Ooij C, Snyder RC, Paeper BW, Duester G |title=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. |journal=Mol. Cell. Biol. |volume=12 |issue= 7 |pages= 3023–31 |year= 1992 |pmid= 1620113 |doi=
*cite journal | author=Stewart MJ, McBride MS, Winter LA, Duester G |title=Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box. |journal=Gene |volume=90 |issue= 2 |pages= 271–9 |year= 1990 |pmid= 2169444 |doi=
*cite journal | author=Yasunami M, Kikuchi I, Sarapata D, Yoshida A |title=The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome. |journal=Genomics |volume=7 |issue= 2 |pages= 152–8 |year= 1990 |pmid= 2347582 |doi=
*cite journal | author=Tsukahara M, Yoshida A |title=Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization. |journal=Genomics |volume=4 |issue= 2 |pages= 218–20 |year= 1989 |pmid= 2737681 |doi=
*cite journal | author=Matsuo Y, Yokoyama S |title=Molecular structure of the human alcohol dehydrogenase 1 gene. |journal=FEBS Lett. |volume=243 |issue= 1 |pages= 57–60 |year= 1989 |pmid= 2920825 |doi=
*cite journal | author=Ikuta T, Szeto S, Yoshida A |title=Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 3 |pages= 634–8 |year= 1986 |pmid= 2935875 |doi=
*cite journal | author=von Bahr-Lindström H, Höög JO, Hedén LO, "et al." |title=cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase. |journal=Biochemistry |volume=25 |issue= 9 |pages= 2465–70 |year= 1986 |pmid= 3013304 |doi=
*cite journal | author=Duester G, Farrés J, Felder MR, "et al." |title=Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family. |journal=Biochem. Pharmacol. |volume=58 |issue= 3 |pages= 389–95 |year= 1999 |pmid= 10424757 |doi=
*cite journal | author=Rodriguez-Zavala JS, Weiner H |title=Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation. |journal=Biochemistry |volume=41 |issue= 26 |pages= 8229–37 |year= 2002 |pmid= 12081471 |doi=
*cite journal | author=Sandberg M, Yasar U, Strömberg P, "et al." |title=Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase. |journal=British journal of clinical pharmacology |volume=54 |issue= 4 |pages= 423–9 |year= 2003 |pmid= 12392591 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Dannenberg LO, Chen HJ, Edenberg HJ |title=GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene. |journal=DNA Cell Biol. |volume=24 |issue= 9 |pages= 543–52 |year= 2006 |pmid= 16153155 |doi= 10.1089/dna.2005.24.543
*cite journal | author=Jelski W, Chrostek L, Szmitkowski M |title=The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer. |journal=Pancreas |volume=35 |issue= 2 |pages= 142–6 |year= 2007 |pmid= 17632320 |doi= 10.1097/MPA.0b013e318053eae2

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