Retinal dehydrogenase
| retinal dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 retinal dehydrogenase inhibited by Yb | |||||||||
| Identifiers | |||||||||
| EC no. | 1.2.1.36 | ||||||||
| CAS no. | 37250-99-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a retinal dehydrogenase (EC 1.2.1.36) is an enzyme that catalyzes the chemical reaction
- retinal + NAD+ + H2O retinoic acid + NADH + H+
The 3 substrates of this enzyme are retinal, NAD+, and H2O, whereas its 3 products are retinoic acid, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is retinal:NAD+ oxidoreductase. This enzyme is also called cytosolic retinal dehydrogenase. This enzyme participates in retinol metabolism. It has 2 cofactors: FAD, and Metal.
References
- Moffa DJ, Lotspeich FJ, Krause RF (1970). "Preparation and properties of retinal-oxidizing enzyme from rat intestinal mucosa". J. Biol. Chem. 245 (2): 439–47. PMID 4312676.
{{cite journal}}: CS1 maint: multiple names: authors list (link)