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IUBMB Comments A cytochrome P -450 (heme-thiolate) protein from the plant Rauvolfia serpentina . Forms a stage in the biosynthesis of the indole alkaloid ajmaline.
Synonyms
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EC 1.14.13.75
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vinorine + [reduced NADPH-hemoprotein reductase] + O2 = vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
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MetaCyc
ajmaline and sarpagine biosynthesis
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vinorine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (21alpha-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein from the plant Rauvolfia serpentina. Forms a stage in the biosynthesis of the indole alkaloid ajmaline.
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vinorine + [reduced NADPH-hemoprotein reductase] + O2
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
additional information
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vinorine + [reduced NADPH-hemoprotein reductase] + O2
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
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Substrates: -
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vinorine + [reduced NADPH-hemoprotein reductase] + O2
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
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vinorine + [reduced NADPH-hemoprotein reductase] + O2
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
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Substrates: enzyme is involved in the biosynthesis of the alkaloid ajmaline
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additional information
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Substrates: 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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Substrates: 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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Substrates: product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated
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additional information
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Substrates: product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated
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additional information
additional information
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Substrates: the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
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additional information
additional information
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Substrates: the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
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vinorine + [reduced NADPH-hemoprotein reductase] + O2
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
additional information
additional information
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vinorine + [reduced NADPH-hemoprotein reductase] + O2
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
?
vinorine + [reduced NADPH-hemoprotein reductase] + O2
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
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Substrates: enzyme is involved in the biosynthesis of the alkaloid ajmaline
?
additional information
additional information
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Substrates: the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
?
additional information
additional information
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Substrates: the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
?
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NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
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cytochrome P-450
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additional information
additional information
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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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additional information
additional information
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Michaelis-Menten-type reaction kinetics
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6.5
hydroxylation reaction
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UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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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
additional information
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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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A0A218NGS0_RAUSE
480
0
54063
TrEMBL
Mitochondrion (Reliability: 5 )
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-28°C, 20% sucrose, no loss of activity
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gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression
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Falkenhagen, H.; Stoeckigt, J.
Enzymic biosynthesis of vomilenine, a key intermediate of the ajmaline pathway, catalyzed by a novel cytochrome P450-dependent enzyme from plant cell cultures of Rauwolfia serpentina
Z. Naturforsch. C
50
45-53
1995
Rauvolfia serpentina
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brenda
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), Rauvolfia serpentina
brenda
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