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show all sequences of 1.14.14.104

Dual catalytic activity of a cytochrome P450 controls bifurcation at a metabolic branch point of alkaloid biosynthesis in Rauwolfia serpentina

Dang, T.T.; Franke, J.; Tatsis, E.; O'Connor, S.E.; Angew. Chem. Int. Ed. Engl. 56, 9440-9444 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression
Rauvolfia serpentina
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Rauvolfia serpentina
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Rauvolfia serpentina
A0A218NGS0
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
744036
Rauvolfia serpentina
?
-
-
-
?
additional information
product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated
744036
Rauvolfia serpentina
?
-
-
-
-
additional information
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
744036
Rauvolfia serpentina
additional information
-
-
-
?
vinorine + [reduced NADPH-hemoprotein reductase] + O2
-
744036
Rauvolfia serpentina
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Rauvolfia serpentina
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
hydroxylation reaction
Rauvolfia serpentina
Cofactor
Cofactor
Commentary
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
Cloned(Commentary) (protein specific)
Commentary
Organism
gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression
Rauvolfia serpentina
Cofactor (protein specific)
Cofactor
Commentary
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
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Rauvolfia serpentina
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
744036
Rauvolfia serpentina
?
-
-
-
?
additional information
product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated
744036
Rauvolfia serpentina
?
-
-
-
-
additional information
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
744036
Rauvolfia serpentina
additional information
-
-
-
?
vinorine + [reduced NADPH-hemoprotein reductase] + O2
-
744036
Rauvolfia serpentina
vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Rauvolfia serpentina
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
hydroxylation reaction
Rauvolfia serpentina
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 1.14.14.104
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744036
Dang
Dual catalytic activity of a ...
Rauvolfia serpentina
Angew. Chem. Int. Ed. Engl.
56
9440-9444
2017
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1
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1
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4
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1
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1
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3
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440250
Falkenhagen
-
Enzymic biosynthesis of vomile ...
Rauvolfia serpentina
Z. Naturforsch. C
50
45-53
1995
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3
1
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1
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1
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1
2
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1
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1
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1
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1
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3
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1
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1
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1
2
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1
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1
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