InterPro: IPR016163 Aldehyde dehydrogenase, C-terminal

This entry represents a structural domain found at the C-terminal of aldehyde dehydrogenases [1]. These proteins contain two similar domains, each with a 3-layer alpha/beta/alpha structure, which probably arose from a duplication; this entry covers the C-terminal a/b/a domain. These enzymes bind NAD differently from other NAD(P)-dependent oxidoreductases.

Aldehyde dehydrogenases (EC:1.2.1.3 and EC:1.2.1.5) are enzymes that oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor. In mammals at least four different forms of the enzyme are known [2]: class-1 (or Ald C) a tetrameric cytosolic enzyme, class-2 (or Ald M) a tetrameric mitochondrial enzyme, class- 3 (or Ald D) a dimeric cytosolic enzyme, and class IV a microsomal enzyme. Aldehyde dehydrogenases have also been sequenced from fungal and bacterial species. A number of enzymes are known to be evolutionary related to aldehyde dehydrogenases. A glutamic acid and a cysteine residue have been implicated in the catalytic activity of mammalian aldehyde dehydrogenase.