ADH1B
Alcohol dehydrogenase IB (class I), beta polypeptide | |||||||||||||
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PDB rendering based on 1deh. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | ADH1B ; ADH2 | ||||||||||||
External IDs | Template:OMIM5 HomoloGene: 88336 | ||||||||||||
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Orthologs | |||||||||||||
Template:GNF Ortholog box | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | n/a | n/a | |||||||||||
Ensembl | n/a | n/a | |||||||||||
UniProt | n/a | n/a | |||||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||||
RefSeq (protein) | n/a | n/a | |||||||||||
Location (UCSC) | n/a | n/a | |||||||||||
PubMed search | n/a | n/a |
Alcohol dehydrogenase IB (class I), beta polypeptide, also known as ADH1B, is a human gene.
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.[1]
References
Further reading
- Smith M (1986). "Genetics of human alcohol and aldehyde dehydrogenases". Adv. Hum. Genet. 15: 249–90. PMID 3006456.
- 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. PMID 11398342.
- Green RF, Stoler JM (2007). "Alcohol dehydrogenase 1B genotype and fetal alcohol syndrome: a HuGE minireview". Am. J. Obstet. Gynecol. 197 (1): 12–25. doi:10.1016/j.ajog.2007.02.028. PMID 17618743.
- Lange LG, Sytkowski AJ, Vallee BL (1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features". Biochemistry. 15 (21): 4687–93. PMID 9982.
- Hurley TD, Bosron WF, Hamilton JA, Amzel LM (1991). "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions". Proc. Natl. Acad. Sci. U.S.A. 88 (18): 8149–53. PMID 1896463.
- 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. PMID 2169444.
- 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". Gene. 91 (2): 233–40. PMID 2210383.
- 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. PMID 2295648.
- 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. PMID 2347582.
- 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. PMID 2398055.
- Matsuo Y, Yokoyama R, Yokoyama S (1989). "The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide". Eur. J. Biochem. 183 (2): 317–20. PMID 2547609.
- Carr LG, Xu Y, Ho WH, Edenberg HJ (1989). "Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit". Alcohol. Clin. Exp. Res. 13 (4): 594–6. PMID 2679216.
- 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. PMID 2737681.
- 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. PMID 2935533.
- 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. PMID 2935875.
- Ikuta T, Fujiyoshi T, Kurachi K, Yoshida A (1985). "Molecular cloning of a full-length cDNA for human alcohol dehydrogenase". Proc. Natl. Acad. Sci. U.S.A. 82 (9): 2703–7. PMID 2986130.
- 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. PMID 3000832.
- Xu YL, Carr LG, Bosron WF; et al. (1988). "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification". Genomics. 2 (3): 209–14. PMID 3397059.
- Burnell JC, Carr LG, Dwulet FE; et al. (1987). "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 (3): 1127–33. PMID 3619918.
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