In enzymology, a vomilenine reductase (EC 1.5.1.32) is an enzyme that catalyzes the chemical reaction
| vomilenine reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.32 | ||||||||
| CAS no. | 462127-03-3 | ||||||||
| 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 | ||||||||
| |||||||||
- 1,2-dihydrovomilenine + NADP+ vomilenine + NADPH + H+
Thus, the two substrates of this enzyme are 1,2-dihydrovomilenine and NADP+, whereas its 3 products are vomilenine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrovomilenine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
edit- von Schumann G, Gao S, Stockigt J (2002). "Vomilenine reductase--a novel enzyme catalyzing a crucial step in the biosynthesis of the therapeutically applied antiarrhythmic alkaloid ajmaline". Bioorg. Med. Chem. 10 (6): 1913–8. doi:10.1016/S0968-0896(01)00435-7. PMID 11937349.
