Alcohol Dehydrogenase 2 (ADH2)

ADH1B; Alcohol dehydrogenase subunit beta

SPN	R951
HGNC	250
PubMed	17963305
UniProt	P00325
Wiki	ADH1B

ADH2 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. Previously ADH1B was called ADH2. There are more genes in the family of alcohol and aldehyde dehydrogenase genes. These genes are now referred to as ADH1A, ADH1C, and ADH4, ADH5, ADH6 and ADH7.

Reference

"Molecular cloning of a full-length cDNA for human alcohol dehydrogenase."
Proc. Natl. Acad. Sci. U.S.A. 82:2703-2707(1985) [PubMed] [Europe PMC] [Abstract]

Erratum
Proc. Natl. Acad. Sci. U.S.A. 82:5578-5578(1985)

"cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions."
FEBS Lett. 194:327-332(1986) [PubMed] [Europe PMC] [Abstract]

"Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit."
J. Biol. Chem. 261:2027-2033(1986) [PubMed] [Europe PMC] [Abstract]

"Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence."
Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986) [PubMed] [Europe PMC] [Abstract]

"Molecular characterization of cDNA clones encoding the human alcohol dehydrogenase beta 1 and the evolutionary relationship to the other class I subunits alpha and gamma."
Jpn. J. Genet. 62:241-256(1987)

"Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit."
Alcohol. Clin. Exp. Res. 13:594-596(1989) [PubMed] [Europe PMC] [Abstract]

"The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide."
Eur. J. Biochem. 183:317-320(1989) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme."
Eur. J. Biochem. 145:437-445(1984) [PubMed] [Europe PMC] [Abstract]

"Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification."
Genomics 2:209-214(1988) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"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. 81:3024-3028(1984) [PubMed] [Europe PMC] [Abstract]

"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. 146:1127-1133(1987) [PubMed] [Europe PMC] [Abstract]

"Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions."
Proc. Natl. Acad. Sci. U.S.A. 88:8149-8153(1991) [PubMed] [Europe PMC] [Abstract]

"Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences."
J. Mol. Biol. 239:415-429(1994) [PubMed] [Europe PMC] [Abstract]

"X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding."
J. Biol. Chem. 271:17057-17061(1996) [PubMed] [Europe PMC] [Abstract]

"Three-dimensional structures of the three human class I alcohol dehydrogenases."
Protein Sci. 10:697-706(2001) [PubMed] [Europe PMC] [Abstract]

"Genetic polymorphism of alcohol dehydrogenase in Europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1."
Hepatology 31:984-989(2000) [PubMed] [Europe PMC] [Abstract]