Vinorine hydroxylase (EC 1.14.14.104, Formerly EC 1.14.13.75) is an enzyme that catalyzes the chemical reaction
| Vinorine hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.14.104 | ||||||||
| CAS no. | 162875-03-8 | ||||||||
| 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 | ||||||||
| |||||||||
Vinorine hydroxylase is a cytochrome P450 protein containing heme, isolated from Rauwolfia serpentina. It requires a partner cytochrome P450 reductase for functional expression. This uses nicotinamide adenine dinucleotide phosphate. The systematic name of this enzyme class is vinorine,NADPH:oxygen oxidoreductase (21alpha-hydroxylating). This enzyme is part of the biosynthetic pathway to the indole alkaloid, ajmaline.[1][2][3]
References
edit- ↑ Enzyme 1.14.14.104 at KEGG Pathway Database.
- ↑ Falkenhagen H, Stockligt J (1995). "Enzymatic biosynthesis of vomilenine, a key intermediate of the ajmaline pathway, catalysed by a novel cytochrome P-450-dependent enzyme from plant cell cultures of Rauwolfia serpentina". Z. Naturforsch. C: Biosci. 50 (1–2): 45–53. doi:10.1515/znc-1995-1-208.
- ↑ Wu F, Kerčmar P, Zhang C, Stöckigt J (2015). "Sarpagan-Ajmalan-Type Indoles: Biosynthesis, Structural Biology, and Chemo-Enzymatic Significance". The Alkaloids. Chemistry and Biology. 76: 1–61. doi:10.1016/bs.alkal.2015.10.001. PMID 26827882.
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