ADH1B

From Wikipedia, the free encyclopedia

Alcohol dehydrogenase IB (class I), beta polypeptide

PDB rendering based on 1deh.

Available structures: 1deh, 1hdx, 1hdy, 1hdz, 1hso, 1hsz, 1ht0, 1htb, 1u3t, 1u3u, 1u3v, 1u3w, 3hud

Identifiers

Symbol(s)

ADH1B; ADH2

External IDs

OMIM: 103720 HomoloGene: 88336

Gene ontology
Molecular Function:	• alcohol dehydrogenase activity, zinc-dependent • zinc ion binding • electron carrier activity • metal ion binding
Biological Process:	• ethanol oxidation

Orthologs

Human

Mouse

Entrez

125

n/a

Refseq

NM_000668 (mRNA)
NP_000659 (protein)

n/a (mRNA)
n/a (protein)

Pubmed search

[1]

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]

[edit] References

^ Entrez Gene: ADH1B alcohol dehydrogenase IB (class I), beta polypeptide.

[edit] 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.