ADH1B

ADH1B
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1DEH, 1HDX, 1HDY, 1HDZ, 1HSZ, 1HTB, 1U3U, 1U3V, 3HUD
Identifiers
Aliases	ADH1B, ADH2, HEL-S-117, alcohol dehydrogenase 1B (class I), beta polypeptide
External IDs	HomoloGene: 133563 GeneCards: ADH1B
Genetically Related Diseases
alcohol abuse, esophageal cancer[1]
Gene ontology Molecular function • oxidoreductase activity • zinc ion binding • alcohol dehydrogenase (NAD) activity • metal ion binding • alcohol dehydrogenase activity, zinc-dependent Cellular component • cytoplasm • cytosol Biological process • oxidation-reduction process • ethanol oxidation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	125	n/a
Ensembl	ENSG00000196616	n/a
UniProt	P00325	n/a
RefSeq (mRNA)	NM_001286650 NM_000668	n/a
RefSeq (protein)	NP_000659.2 NP_001273579.1	n/a
Location (UCSC)	Chr 4: 99.3 – 99.32 Mb	n/a
PubMed search	[2]	n/a
Wikidata

View/Edit Human

Alcohol dehydrogenase 1B is an enzyme that in humans is encoded by the ADH1B gene.^[3]

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.^[4]

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.^[5]

Variants

A single nucleotide polymorphism (SNP) in ADH1B is rs1229984, that changes arginine to histidine at residue 47.^[6] 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.^[7]

Another SNP is Arg369Cys.^[8]

Role in pathology

A marked decrease of ADH1B mRNA was detected in corneal fibroblasts taken from persons suffering from keratoconus.^[9]

See also

• Alcohol dehydrogenase
• Aldehyde dehydrogenase

References

1. "Diseases that are genetically associated with ADH1B view/edit references on wikidata".
2. "Human PubMed Reference:".
3. Smith M (Mar 1986). "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet. 15: 249–90. doi:10.1007/978-1-4615-8356-1_5. PMID 3006456.
4. "Entrez Gene: ADH1B alcohol dehydrogenase IB (class I), beta polypeptide".
5. Sandra Porter (2008-08-21). "A gene by many other names and thoughts on teaching bioinformatics". ScienceBlogs. Retrieved 2008-09-03.
6. Y. Matsuo; R. Yokoyama & S. Yokoyama (August 1989). "The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide". European Journal of Biochemistry. 183 (2): 317–310. doi:10.1111/j.1432-1033.1989.tb14931.x. PMID 2547609.
7. T. Muramatsu; Z. C. Wang; Y. R. Fang; K. B. Hu; H. Yan; K. Yamada; S. Higuchi; S. Harada & H. Kono (August 1995). "Alcohol and aldehyde dehydrogenase genotypes and drinking behavior of Chinese living in Shanghai". Human Genetics. 96 (2): 151–154. doi:10.1007/BF00207371. PMID 7635462.
8. J. C. Burnell; L. G. Carr; F. E. Dwulet; H. J. Edenberg; T. K. Li & W. F. Bosron (August 1987). "The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding". Biochemical and Biophysical Research Communications. 146 (3): 1127–1123. PMID 3619918.
9. Mootha VV, Kanoff JM, Shankardas J, Dimitrijevich S (2009). "Marked reduction of alcohol dehydrogenase in keratoconus corneal fibroblasts". Mol. Vis. 15: 706–12. PMC 2666775. PMID 19365573.

External links

• Human ADH1B genome location and ADH1B gene details page in the UCSC Genome Browser.

Further reading

• 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. doi:10.1021/bi00666a023. 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. doi:10.1073/pnas.88.18.8149. PMC 52464. 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. doi:10.1016/0378-1119(90)90190-3. 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. doi:10.1016/0378-1119(90)90093-7. 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. doi:10.1016/0888-7543(90)90535-3. 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.
• 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. doi:10.1111/j.1530-0277.1989.tb00383.x. 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. doi:10.1016/0888-7543(89)90304-2. 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. doi:10.1073/pnas.83.3.634. PMC 322918. 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. doi:10.1073/pnas.82.9.2703. PMC 397633. 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. doi:10.1016/0014-5793(86)80111-9. 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. doi:10.1016/0888-7543(88)90004-3. PMID 3397059.