| Type: | Domain | Name: | Aldehyde dehydrogenase, C-terminal |
| Description: | This entry represents a structural domain found at the C-terminal of aldehyde dehydrogenases []. 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 (and ) 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 []: 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. | Short Name: | Ald_DH_C |
| DB identifier | Type | Name |
|---|---|---|
| IPR020593 | Conserved_site | Gamma-glutamyl phosphate reductase GPR, conserved site |
| GO Term | Gene Name |
|---|---|
| GO:0016491 | IPR016163 |
| GO:0016620 | IPR016163 |
| GO:0008152 | IPR016163 |
| GO:0055114 | IPR016163 |
| GO Term | Gene Name |
|---|---|
| GO:0016491 | IPR016163 |
| GO:0016620 | IPR016163 |
| GO:0008152 | IPR016163 |
| GO:0055114 | IPR016163 |
