Information on EC 1.14.13.75 - vinorine hydroxylase

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The expected taxonomic range for this enzyme is: Rauvolfia serpentina

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EC NUMBER
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1.14.13.75
transferred to EC 1.14.14.104
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RECOMMENDED NAME
GeneOntology No.
vinorine hydroxylase
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Indole alkaloid biosynthesis
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Biosynthesis of secondary metabolites
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-
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ORGANISM
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LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
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LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
vinorine + NADPH + H+ + O2
vomilenine + NADP+ + H2O
show the reaction diagram
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-
?
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
?
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product analysis by NMR spectroscopy. The stereoselectivity of the enzyme cannot be determined, since the vomilenine isomers cannot be separated
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
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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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-
?
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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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
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LITERATURE
6.5
hydroxylation reaction
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
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GeneOntology No.
LITERATURE
SOURCE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene CYP5437, unrooted neighbor-joining phylogenetic tree, recombinant expression
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.75)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)