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 Failed to parse (MathML with SVG or PNG fallback (recommended for modern browsers and accessibility tools): Invalid response ("Math extension cannot connect to Restbase.") from server "https://en.wikipedia.org/api/rest_v1/":): \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.

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&ndash, 53.

External links

The CAS registry number for this enzyme class is 162875-03-8.

Gene Ontology (GO) codes

Template:1.14.13-enzyme-stub


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