Alcohol dehydrogenase 1B is an enzyme that in humans is encoded by the ADH1Bgene.
The protein encoded by this gene 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. This encoded protein, 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.
A single nucleotide polymorphism (SNP) in ADH1B is rs1229984, that changes arginine to histidine at residue 47. The 'typical' variant of this has been referred to as ADH2(1) or ADH2*1 while the 'atypical' has been referred to as, e.g., ADH2(2), ADH2*2, ADH1B*47his, or ADH1B arg47-to-his. This SNP may be related to alcohol consumption with the atypical genotype having reduced risk of alcoholism.
Harada S (2001). "[Classification of alcohol metabolizing enzymes and polymorphisms--specificity in Japanese]". Nihon Arukōru Yakubutsu Igakkai zasshi (Japanese journal of alcohol studies & drug dependence)36 (2): 85–106. PMID11398342.
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.". Gene90 (2): 271–9. doi:10.1016/0378-1119(90)90190-3. PMID2169444.
Winter LA, Stewart MJ, Shean ML; et al. (1990). "A hormone response element upstream from the human alcohol dehydrogenase gene ADH2 consists of three tandem glucocorticoid receptor binding sites.". Gene91 (2): 233–40. doi:10.1016/0378-1119(90)90093-7. PMID2210383.
Carr LG, Edenberg HJ (1990). "cis-acting sequences involved in protein binding and in vitro transcription of the human alcohol dehydrogenase gene ADH2.". J. Biol. Chem.265 (3): 1658–64. PMID2295648.
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.". Genomics7 (2): 152–8. doi:10.1016/0888-7543(90)90535-3. PMID2347582.
Hurley TD, Edenberg HJ, Bosron WF (1990). "Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47.". J. Biol. Chem.265 (27): 16366–72. PMID2398055.
Tsukahara M, Yoshida A (1989). "Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization.". Genomics4 (2): 218–20. doi:10.1016/0888-7543(89)90304-2. PMID2737681.
Duester G, Smith M, Bilanchone V, Hatfield GW (1986). "Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit.". J. Biol. Chem.261 (5): 2027–33. PMID2935533.
Hedén LO, Höög JO, Larsson K; et al. (1986). "cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions.". FEBS Lett.194 (2): 327–32. doi:10.1016/0014-5793(86)80111-9. PMID3000832.
Xu YL, Carr LG, Bosron WF; et al. (1988). "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification.". Genomics2 (3): 209–14. doi:10.1016/0888-7543(88)90004-3. PMID3397059.