In enzymology, a 1,2-dihydrovomilenine reductase (EC 1.3.1.73) is an enzyme that catalyzes the chemical reaction
| 1,2-dihydrovomilenine reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.73 | ||||||||
| 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 | ||||||||
| |||||||||
- 17-O-acetylnorajmaline + NADP+ 1,2-dihydrovomilenine + NADPH + H+
Thus, the two substrates of this enzyme are 17-O-acetylnorajmaline and NADP+, whereas its 3 products are 1,2-dihydrovomilenine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 17-O-acetylnorajmaline:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
edit- Gao S, von Schumann G, Stockigt J (2002). "A newly-detected reductase from Rauvolfia closes a gap in the biosynthesis of the antiarrhythmic alkaloid ajmaline". Planta Medica. 68 (10): 906–11. doi:10.1055/s-2002-34935. PMID 12391554.
