Literature DB >> 10424757

Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family.

G Duester1, J Farrés, M R Felder, R S Holmes, J O Höög, X Parés, B V Plapp, S J Yin, H Jörnvall.   

Abstract

The alcohol dehydrogenase (ADH) gene family encodes enzymes that metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Studies on 19 vertebrate animals have identified ADH orthologs across several species, and this has now led to questions of how best to name ADH proteins and genes. Seven distinct classes of vertebrate ADH encoded by non-orthologous genes have been defined based upon sequence homology as well as unique catalytic properties or gene expression patterns. Each class of vertebrate ADH shares <70% sequence identity with other classes of ADH in the same species. Classes may be further divided into multiple closely related isoenzymes sharing >80% sequence identity such as the case for class I ADH where humans have three class I ADH genes, horses have two, and mice have only one. Presented here is a nomenclature that uses the widely accepted vertebrate ADH class system as its basis. It follows the guidelines of human and mouse gene nomenclature committees, which recommend coordinating names across species boundaries and eliminating Roman numerals and Greek symbols. We recommend that enzyme subunits be referred to by the symbol "ADH" (alcohol dehydrogenase) followed by an Arabic number denoting the class; i.e. ADH1 for class I ADH. For genes we recommend the italicized root symbol "ADH" for human and "Adh" for mouse, followed by the appropriate Arabic number for the class; i.e. ADH1 or Adh1 for class I ADH genes. For organisms where multiple species-specific isoenzymes exist within a class, we recommend adding a capital letter after the Arabic number; i.e. ADH1A, ADH1B, and ADH1C for human alpha, beta, and gamma class I ADHs, respectively. This nomenclature will accommodate newly discovered members of the vertebrate ADH family, and will facilitate functional and evolutionary studies.

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Year:  1999        PMID: 10424757     DOI: 10.1016/s0006-2952(99)00065-9

Source DB:  PubMed          Journal:  Biochem Pharmacol        ISSN: 0006-2952            Impact factor:   5.858


  44 in total

1.  Three-dimensional structures of the three human class I alcohol dehydrogenases.

Authors:  M S Niederhut; B J Gibbons; S Perez-Miller; T D Hurley
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

2.  Changes in the activity of alcohol dehydrogenase isoenzymes during the estrus cycle in the vagina of the rat.

Authors:  C Nowak; I P Maly; D Sasse
Journal:  Histochem J       Date:  2000-08

3.  Contribution of liver alcohol dehydrogenase to metabolism of alcohols in rats.

Authors:  Bryce V Plapp; Kevin G Leidal; Bruce P Murch; David W Green
Journal:  Chem Biol Interact       Date:  2015-01-29       Impact factor: 5.192

Review 4.  Xenobiotica-metabolizing enzymes in the skin of rat, mouse, pig, guinea pig, man, and in human skin models.

Authors:  F Oesch; E Fabian; Robert Landsiedel
Journal:  Arch Toxicol       Date:  2018-06-18       Impact factor: 5.153

5.  The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.

Authors:  Yaroslav Tsybovsky; Yuryi Malakhau; Kyle C Strickland; Sergey A Krupenko
Journal:  Chem Biol Interact       Date:  2013-01-05       Impact factor: 5.192

Review 6.  Role of alcohol in the development and progression of hepatocellular carcinoma.

Authors:  Iain H McKillop; Laura W Schrum; Kyle J Thompson
Journal:  Hepat Oncol       Date:  2015-11-30

Review 7.  Genetic risk markers for hepatocellular carcinoma in patients with alcoholic liver disease.

Authors:  Pierre Nahon; Angela Sutton; Marianne Ziol; Jessica Zucman-Rossi; Jean-Claude Trinchet; Nathalie Ganne-Carrié
Journal:  Hepat Oncol       Date:  2015-01-12

8.  Contribution of NADH increases to ethanol's inhibition of retinol oxidation by human ADH isoforms.

Authors:  Jennifer R Chase; Mark G Poolman; David A Fell
Journal:  Alcohol Clin Exp Res       Date:  2009-01-16       Impact factor: 3.455

Review 9.  A new view of alcohol metabolism and alcoholism--role of the high-Km Class III alcohol dehydrogenase (ADH3).

Authors:  Takeshi Haseba; Youkichi Ohno
Journal:  Int J Environ Res Public Health       Date:  2010-03-15       Impact factor: 3.390

10.  Medium- and short-chain dehydrogenase/reductase gene and protein families : MDR and SDR gene and protein superfamilies.

Authors:  H Jörnvall
Journal:  Cell Mol Life Sci       Date:  2008-12       Impact factor: 9.261

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