Information on EC 2.1.1.99 - 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase

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The expected taxonomic range for this enzyme is: Catharanthus roseus

EC NUMBER
COMMENTARY hide
2.1.1.99
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RECOMMENDED NAME
GeneOntology No.
3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3-hydroxy-16-methoxy-2,3-dihydrotabersonine = S-adenosyl-L-homocysteine + deacetoxyvindoline
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vindoline and vinblastine biosynthesis
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-
Indole alkaloid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase
Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle Catharanthus roseus.
CAS REGISTRY NUMBER
COMMENTARY hide
113478-40-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
S-adenosyl-L-homocysteine + deacetoxyvindoline
show the reaction diagram
additional information
?
-
-
hydrogenation of 2,3 double bond of tabersonine instead of hydration results in a 75% decrease in N-methylation, double bound present: no N-methylation, the presence of 6,7 double bound is a necessary structural requirement for N-methylation with membrane-bound enzyme, whereas the detergent-solubilized enzyme is also able to N-methylate the 6,7 anhydro analogue
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-
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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
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
S-adenosyl-L-homocysteine + deacetoxyvindoline
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lysolecithin
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completely elimination of activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CHAPS
-
highest activity with 3 mg/ml
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
associated with thylakoids
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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gel chromatography
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
reducing agent, e.g. DTT, necessary for the retention of activity after breakage of thylakoid membranes of chloroplasts
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
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0.1% Triton X-100 90% of activity
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
labile to O2, DTT or 2-mercaptoethanol stabilizes
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485690
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in absence of CHAPS, 4 days, 50% loss of activity
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-20°C, in absence of detergent by adding 25% glycerol, one week, 9% loss of activity
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-20°C, in presence of 0.6% CHAPS, 7 days, 50% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE