Pathways & interactions
Aldehyde dehydrogenase, C-terminal (IPR016163)
Short name: Ald_DH_C
- Aldehyde dehydrogenase (IPR011408)
- Phenylacetic acid degradation protein PaaN (IPR011966)
- Aldehyde dehydrogenase NAD(P)-dependent (IPR012394)
- Acetaldehyde dehydrogenase, acetylating (IPR013357)
- Aldehyde dehydrogenase domain (IPR015590)
- Aldehyde dehydrogenase, cysteine active site (IPR016160)
- Aldehyde/histidinol dehydrogenase (IPR016161)
- Aldehyde dehydrogenase, N-terminal (IPR016162)
- Gamma-glutamyl phosphate reductase GPR, conserved site (IPR020593)
This superfamily 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:18.104.22.168 and EC:22.214.171.124) 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.
- G3DSA:3.40.309.10 (G3DSA:3.40.309.10)