Any feedback?
Literature summary extracted from
- 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 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.104 | gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression | Rauvolfia serpentina |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.104 | additional information | - |
additional information | Michaelis-Menten-type reaction kinetics | Rauvolfia serpentina | |
| 1.14.14.104 | 0.0068 | - |
vinorine | pH 6.5, 30°C, recombinant enzyme | Rauvolfia serpentina |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.14.104 | microsome | - |
Rauvolfia serpentina | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.104 | additional information | Rauvolfia serpentina | the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine | additional information | - |
? | |
| 1.14.14.104 | vinorine + [reduced NADPH-hemoprotein reductase] + O2 | Rauvolfia serpentina | - |
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.104 | Rauvolfia serpentina | A0A218NGS0 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.104 | additional information | the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine | Rauvolfia serpentina | ? | - |
? | |
| 1.14.14.104 | additional information | product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated | Rauvolfia serpentina | ? | - |
? | |
| 1.14.14.104 | additional information | the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine | Rauvolfia serpentina | additional information | - |
? | |
| 1.14.14.104 | vinorine + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rauvolfia serpentina | vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.104 | CYP5437 | - |
Rauvolfia serpentina |
| 1.14.14.104 | CYP82S18 | - |
Rauvolfia serpentina |
| 1.14.14.104 | cytochrome P450_5437 | - |
Rauvolfia serpentina |
| 1.14.14.104 | vinorine hydroxylase | - |
Rauvolfia serpentina |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.104 | 30 | - |
- |
Rauvolfia serpentina |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.104 | 6.5 | - |
hydroxylation reaction | Rauvolfia serpentina |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.104 | cytochrome P-450 | - |
Rauvolfia serpentina | |
| 1.14.14.104 | 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
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.14.104 | 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 |
| 1.14.14.104 | 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 |
| 1.14.14.104 | physiological function | the unusual dual catalytic activity of vinorine hydroxylase provides a control mechanism for the bifurcation of the alkaloid pathway branches | Rauvolfia serpentina |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
