Pathways & interactions
Aldehyde dehydrogenase, C-terminal (IPR016163)
Short name: Ald_DH_C
This entry represents a structural domain found at the C-terminal of aldehyde dehydrogenases [PMID: 12795606]. 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:22.214.171.124 and EC:126.96.36.199) 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 [PMID: 2713359]: 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.
No terms assigned in this category.
- G3DSA:3.40.309.10 (G3DSA:3.40.309.10)