RESEARCH ARTICLE y p a

Barcelona, E-08193, Bellaterra, Barcelona, Spain Full list of author information is available at the end of the articleBackground Vertebrate alcohol dehydrogenases (ADH, EC1.1.1.1) are dimeric zinc-containing enzymes with a 40-kDa subunit and 373–383 amino acid residues. Structurally, they belong to the medium-chain dehydrogenase/reductase (MDR) superfamily [1]. ADHs catalyze the reversible oxidation of a wide range of alcohol substrates to the corresponding aldehydes or ketones, and can be grouped in eight enzyme classes (ADH1-8, class I to VIII) [2], according to their pri-mary structure and function. The human ADH gene nomenclature used throughout the text is the enzyme class-based nomenclature currently used for vertebrate ADH [2] and differs from that approved by the Human Genome Organization (HUGO) Gene Nomenclature Committee [3], as the former facilitates comparisons with ADHs from other mammals and lower vertebrate * Correspondence