Vinorine Hydroxylase
From Handwiki | Vinorine hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.14.104 | ||||||||
| CAS number | 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 (EC 1.14.14.104, Formerly EC 1.14.13.75) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
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
- ↑ Enzyme 1.14.14.104 at KEGG Pathway Database.
- ↑ "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. 1995. doi:10.1515/znc-1995-1-208.
- ↑ "Sarpagan-Ajmalan-Type Indoles: Biosynthesis, Structural Biology, and Chemo-Enzymatic Significance". The Alkaloids. Chemistry and Biology 76: 1–61. 2015. doi:10.1016/bs.alkal.2015.10.001. PMID 26827882.
 |  |
Categories: [EC 1.14.14] [NADPH-dependent enzymes] [Enzymes of unknown structure]
↧ Download as ZWI file | Last modified: 08/08/2026 01:15:58 | 4 views
☰ Source: https://handwiki.org/wiki/Biology:Vinorine_hydroxylase | License: CC BY-SA 3.0
✘
ZWI is not signed. [what is this?]
ZWI viewer
by the 
KSF
KSF