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Information on EC 1.14.13.75 - vinorine hydroxylase for references in articles please use BRENDA:EC1.14.13.75Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Rauvolfia serpentina
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Indole alkaloid biosynthesis
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Biosynthesis of secondary metabolites
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UniProt
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metabolism
in plant-derived ajmalan alkaloid pathways, the biosynthetic intermediate vomilenine can be transformed into the anti-arrhythmic compound ajmaline, or alternatively, can isomerize to form perakine, an alkaloid with a structurally distinct scaffold. Enzyme vinorine hydroxylase, a cytochrome P450 enzyme, hydroxylates vinorine to form vomilenine, which exists as a mixture of rapidly interconverting epimers (with 21-epi-vomilenine). The cytochrome P450 also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine. Alkaloid network in Rauwolfia serpentina from strictosidine, overview
physiological function
the unusual dual catalytic activity of vinorine hydroxylase provides a control mechanism for the bifurcation of the alkaloid pathway branches
additional information
proposed reaction mechanism for the isomerization of vomilenine to perakine, the introduction of a hydroxy group at C-21 allows opening of the ring via the newly formed hemiaminal. The resulting amine can then undergo a Michael addition to form perakine, overview. The conversion of vomilenine into perakine is enzymatically catalyzed by vinorine hydroxylase
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vinorine + NADPH + H+ + O2
vomilenine + NADP+ + H2O
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vomilenine
perakrine
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
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additional information
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product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated
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vinorine + NADPH + H+ + O2
vomilenine + NADP+ + H2O
A0A218NGS0
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vomilenine
perakrine
A0A218NGS0
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
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0.0068
vinorine
pH 6.5, 30°C, recombinant enzyme
additional information
additional information
Michaelis-Menten-type reaction kinetics
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6.5
hydroxylation reaction
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brenda
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gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression
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Dang, T.T.; Franke, J.; Tatsis, E.; O'Connor, S.E.
Dual catalytic activity of a cytochrome P450 controls bifurcation at a metabolic branch point of alkaloid biosynthesis in Rauwolfia serpentina
Angew. Chem. Int. Ed. Engl.
56
9440-9444
2017
Rauvolfia serpentina (A0A218NGS0)
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