Zinc-containing alcohol dehydrogenases are found in bacteria, mammals, plants, and in fungi. They are dimeric or tetrameric enzymes that bind two atoms of zinc per subunit [1]. A number of other zinc-dependent dehydrogenases are closely related to zinc ADH such as sorbitol dehydrogenase, L-threonine 3-dehydrogenase, glutathione-dependent formaldehyde dehydrogenase, mannitol dehydrogenase, and NADP-dependent quinone oxidoreductase.
The allergen Cand a 1 from Candida albicans is an alcohol dehydrogenase [2].
Family-defining Pfam domains (at least one of these domains is present in each family member):
Pfam domain | Pfam clan | ||
PF00107 | Zinc-binding dehydrogenase | CL0063 | FAD/NAD(P)-binding Rossmann fold Superfamily |
PF08240 | Alcohol dehydrogenase GroES-like domain | CL0296 | GroES-like superfamily |
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