ADH1B

Alcohol dehydrogenase IB (class I), beta polypeptide, also known as ADH1B, is a human gene.

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ADH1B alcohol dehydrogenase IB (class I), beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=125| accessdate = ]

The human gene is located on chromosome 4 in 4q22.

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".Cite web
author = Sandra Porter
title = A gene by many other names and thoughts on teaching bioinformatics
publisher = ScienceBlogs
date = 2008-08-21
url = http://scienceblogs.com/digitalbio/2008/08/a_gene_by_any_other_name_and_t_1.php
accessdate = 2008-09-03]

Variants

A single nucleotide polymorphism (SNP) in "ADH1B" is rs1229984, that changes arginine to histidine at residue 47. [Cite journal
author = Y. Matsuo, R. Yokoyama & S. Yokoyama
title = The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide
journal = European Journal of Biochemistry
volume = 183
issue = 2
pages = 317–310
year = 1989
month = August
pmid = 2547609] 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. [Cite journal
author = T. Muramatsu, Z. C. Wang, Y. R. Fang, K. B. Hu, H. Yan, K. Yamada, S. Higuchi, S. Harada & H. Kono
title = Alcohol and aldehyde dehydrogenase genotypes and drinking behavior of Chinese living in Shanghai
journal = Human Genetics
volume = 96
issue = 2
pages = 151–154
year = 1995
month = August
pmid = 7635462]

Another SNP is Arg369Cys. [Cite journal
author = J. C. Burnell, L. G. Carr, F. E. Dwulet, H. J. Edenberg, T. K. Li & W. F. Bosron
title = The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding
journal = Biochemical and Biophysical Research Communications
volume = 146
issue = 3
pages = 1127–1123
year = 1987
month = August
pmid = 3619918]

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=Harada S |title= [Classification of alcohol metabolizing enzymes and polymorphisms--specificity in Japanese] |journal=Nihon Arukōru Yakubutsu Igakkai zasshi = Japanese journal of alcohol studies & drug dependence |volume=36 |issue= 2 |pages= 85–106 |year= 2001 |pmid= 11398342 |doi=
*cite journal | author=Green RF, Stoler JM |title=Alcohol dehydrogenase 1B genotype and fetal alcohol syndrome: a HuGE minireview. |journal=Am. J. Obstet. Gynecol. |volume=197 |issue= 1 |pages= 12–25 |year= 2007 |pmid= 17618743 |doi= 10.1016/j.ajog.2007.02.028
*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=Hurley TD, Bosron WF, Hamilton JA, Amzel LM |title=Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 18 |pages= 8149–53 |year= 1991 |pmid= 1896463 |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=Winter LA, Stewart MJ, Shean ML, "et al." |title=A hormone response element upstream from the human alcohol dehydrogenase gene ADH2 consists of three tandem glucocorticoid receptor binding sites. |journal=Gene |volume=91 |issue= 2 |pages= 233–40 |year= 1990 |pmid= 2210383 |doi=
*cite journal | author=Carr LG, Edenberg HJ |title=cis-acting sequences involved in protein binding and in vitro transcription of the human alcohol dehydrogenase gene ADH2. |journal=J. Biol. Chem. |volume=265 |issue= 3 |pages= 1658–64 |year= 1990 |pmid= 2295648 |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=Hurley TD, Edenberg HJ, Bosron WF |title=Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47. |journal=J. Biol. Chem. |volume=265 |issue= 27 |pages= 16366–72 |year= 1990 |pmid= 2398055 |doi=
*cite journal | author=Carr LG, Xu Y, Ho WH, Edenberg HJ |title=Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit. |journal=Alcohol. Clin. Exp. Res. |volume=13 |issue= 4 |pages= 594–6 |year= 1989 |pmid= 2679216 |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=Duester G, Smith M, Bilanchone V, Hatfield GW |title=Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. |journal=J. Biol. Chem. |volume=261 |issue= 5 |pages= 2027–33 |year= 1986 |pmid= 2935533 |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=Ikuta T, Fujiyoshi T, Kurachi K, Yoshida A |title=Molecular cloning of a full-length cDNA for human alcohol dehydrogenase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 9 |pages= 2703–7 |year= 1985 |pmid= 2986130 |doi=
*cite journal | author=Hedén LO, Höög JO, Larsson K, "et al." |title=cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions. |journal=FEBS Lett. |volume=194 |issue= 2 |pages= 327–32 |year= 1986 |pmid= 3000832 |doi=
*cite journal | author=Xu YL, Carr LG, Bosron WF, "et al." |title=Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification. |journal=Genomics |volume=2 |issue= 3 |pages= 209–14 |year= 1988 |pmid= 3397059 |doi=

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes