KEGG   ENZYME: 1.14.14.104
Entry
EC 1.14.14.104              Enzyme                                 

Name
vinorine hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
vinorine,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (21alpha-hydroxylating)
Reaction(IUBMB)
vinorine + [reduced NADPH---hemoprotein reductase] + O2 = vomilenine + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R05877]
Reaction(KEGG)
R05877
Substrate
vinorine [CPD:C11807];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
vomilenine [CPD:C01761];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
A cytochrome P-450 (heme-thiolate) protein from the plant Rauvolfia serpentina. Forms a stage in the biosynthesis of the indole alkaloid ajmaline.
History
EC 1.14.14.104 created 2002 as EC 1.14.13.75, transferred 2018 to EC 1.14.14.104
Pathway
ec00901  Indole alkaloid biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K22326  vinorine hydroxylase
Reference
1
  Authors
Falkenhagen, H. and Stockligt, J.
  Title
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.
  Journal
Z Naturforsch C: Biosci 50:45-53 (1995)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.104
IUBMB Enzyme Nomenclature: 1.14.14.104
ExPASy - ENZYME nomenclature database: 1.14.14.104
BRENDA, the Enzyme Database: 1.14.14.104
CAS: 162875-03-8

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