Conserved Site

Alcohol dehydrogenase, zinc-type, conserved site (IPR002328)

Short name: ADH_Zn_CS


Alcohol dehydrogenase (EC: (ADH) catalyzes the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD: Ethanol + NAD = Acetaldehyde + NADH Currently three structurally and catalytically different types of alcohol dehydrogenases are known:

  1. Zinc-containing 'long-chain' alcohol dehydrogenases.
  2. Insect-type, or 'short-chain' alcohol dehydrogenases.
  3. Iron-containing alcohol dehydrogenases.
Zinc-containing ADH's [PMID: 3622514, PMID: 1593644] are dimeric or tetrameric enzymes that bind two atoms of zinc per subunit. One of the zinc atom is essential for catalytic activity while the other is not. Both zinc atoms are coordinated by either cysteine or histidine residues; the catalytic zinc is coordinated by two cysteines and one histidine. Zinc-containing ADH's are found in bacteria, mammals, plants, and in fungi. In most species there are more than one isozyme (for example, human have at least six isozymes, yeast have three, etc.).

A number of other zinc-dependent dehydrogenases are closely related to zinc ADH [PMID: 8504864] and are included in this family, including xylitol dehydrogenase (EC:; sorbitol dehydrogenase (EC:; aryl-alcohol dehydrogenase (EC:; threonine 3-dehydrogenase (EC:; cinnamyl-alcohol dehydrogenase (EC: (CAD); galactitol-1-phosphate dehydrogenase (EC:; and Pseudomonas putida 5-exo-alcohol dehydrogenase (EC:1.1.1).

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0016491 oxidoreductase activity
GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns