Information on EC 1.14.13.75 - vinorine hydroxylase

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The expected taxonomic range for this enzyme is: Rauvolfia serpentina

EC NUMBER
COMMENTARY hide
1.14.13.75
transferred to EC 1.14.14.104
RECOMMENDED NAME
GeneOntology No.
vinorine hydroxylase
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Indole alkaloid biosynthesis
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-
Biosynthesis of secondary metabolites
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
vinorine + NADPH + H+ + O2
vomilenine + NADP+ + H2O
show the reaction diagram
-
-
-
?
vomilenine
perakrine
show the reaction diagram
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
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-
?
additional information
?
-
product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated
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-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
vinorine + NADPH + H+ + O2
vomilenine + NADP+ + H2O
show the reaction diagram
A0A218NGS0
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-
-
?
vomilenine
perakrine
show the reaction diagram
A0A218NGS0
the enzyme also catalyzes the non-oxidative isomerization of the ajmaline precursor vomilenine to perakine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0068
vinorine
pH 6.5, 30°C, recombinant enzyme
additional information
additional information
Michaelis-Menten-type reaction kinetics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
hydroxylation reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression