Vinorine hydroxylase

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

vinorine + NADPH + H⁺ + O₂ $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 1.14.13.75
BRENDA references for 1.14.13.75 (Recommended.)
PubMed references for 1.14.13.75
PubMed Central references for 1.14.13.75
Google Scholar references for 1.14.13.75
Falkenhagen H and 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.