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Literature summary for 1.14.14.104 extracted from

  • 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 (2017), Angew. Chem. Int. Ed. Engl., 56, 9440-9444 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression Rauvolfia serpentina

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten-type reaction kinetics Rauvolfia serpentina
0.0068
-
vinorine pH 6.5, 30°C, recombinant enzyme Rauvolfia serpentina

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Rauvolfia serpentina
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rauvolfia serpentina the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine additional information
-
?
vinorine + [reduced NADPH-hemoprotein reductase] + O2 Rauvolfia serpentina
-
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Organism

Organism UniProt Comment Textmining
Rauvolfia serpentina A0A218NGS0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine Rauvolfia serpentina ?
-
?
additional information product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated Rauvolfia serpentina ?
-
?
additional information the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine Rauvolfia serpentina additional information
-
?
vinorine + [reduced NADPH-hemoprotein reductase] + O2
-
Rauvolfia serpentina vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Synonyms

Synonyms Comment Organism
CYP5437
-
Rauvolfia serpentina
CYP82S18
-
Rauvolfia serpentina
cytochrome P450_5437
-
Rauvolfia serpentina
vinorine hydroxylase
-
Rauvolfia serpentina

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Rauvolfia serpentina

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
hydroxylation reaction Rauvolfia serpentina

Cofactor

Cofactor Comment Organism Structure
cytochrome P-450
-
Rauvolfia serpentina
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._ Rauvolfia serpentina

General Information

General Information Comment Organism
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 Rauvolfia serpentina
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 Rauvolfia serpentina
physiological function the unusual dual catalytic activity of vinorine hydroxylase provides a control mechanism for the bifurcation of the alkaloid pathway branches Rauvolfia serpentina