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Vinorine hydroxylase

From Wikipedia, the free encyclopedia
vinorine hydroxylase
Identifiers
EC no.1.14.14.104
CAS no.162875-03-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a vinorine hydroxylase (EC 1.14.14.104, Formerly EC 1.14.13.75) is an enzyme that catalyzes the chemical reaction

vinorine + NADPH + H+ + O2 vomilenine + NADP+ + H2O

The 4 substrates of this enzyme are vinorine, NADPH, H+, and O2, whereas its 3 products are vomilenine, NADP+, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is vinorine,NADPH:oxygen oxidoreductase (21alpha-hydroxylating). This enzyme participates in indole and ipecac alkaloid biosynthesis.

References

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  • 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: 45–53.