BRENDA - Enzyme Database

Partial purification of an N-methyltransferase involved in vindoline biosynthesis in Catharanthus roseus

Dethier, M.; De Luca, V.; Phytochemistry 32, 673-678 (1993)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
2.1.1.99
CHAPS
highest activity with 3 mg/ml
Catharanthus roseus
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
2.1.1.99
lysolecithin
completely elimination of activity
Catharanthus roseus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.99
chloroplast
associated with thylakoids
Catharanthus roseus
9507
-
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.1.99
60000
-
gel chromatography
Catharanthus roseus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2.1.1.99
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
Catharanthus roseus
enzyme is involved in the biosynthesis of vindoline from tabersonine
S-adenosyl-L-homocysteine + deacetoxyvindoline
-
-
-
Organic Solvent Stability
EC Number
Organic Solvent
Commentary
Organism
2.1.1.99
additional information
CHAPS: 232% activity is solubilized; octyl-beta-D-glucoside: 0.15% solution 100% of activity
Catharanthus roseus
2.1.1.99
Triton X-100
0.1% Triton X-100 90% of activity
Catharanthus roseus
Organism
EC Number
Organism
UniProt
Commentary
Textmining
2.1.1.99
Catharanthus roseus
-
-
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
2.1.1.99
partially
Catharanthus roseus
Reaction
EC Number
Reaction
Commentary
Organism
Reaction ID
2.1.1.99
S-adenosyl-L-methionine + 3-hydroxy-16-methoxy-2,3-dihydrotabersonine = S-adenosyl-L-homocysteine + deacetoxyvindoline
summerization of biosynthetic pathway of vindoline
Catharanthus roseus
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.1.1.99
additional information
-
-
Catharanthus roseus
Storage Stability
EC Number
Storage Stability
Organism
2.1.1.99
-20°C, in absence of CHAPS, 4 days, 50% loss of activity
Catharanthus roseus
2.1.1.99
-20°C, in absence of detergent by adding 25% glycerol, one week, 9% loss of activity
Catharanthus roseus
2.1.1.99
-20°C, in presence of 0.6% CHAPS, 7 days, 50% loss of activity
Catharanthus roseus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2.1.1.99
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
485692
Catharanthus roseus
?
-
-
-
-
2.1.1.99
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
high degree of specifity for the N-indole of 2,3-dihydro-3-hydroxytabersonine
485692
Catharanthus roseus
S-adenosyl-L-homocysteine + deacetoxyvindoline
-
-
-
?
2.1.1.99
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
enzyme is involved in the biosynthesis of vindoline from tabersonine
485692
Catharanthus roseus
S-adenosyl-L-homocysteine + deacetoxyvindoline
-
-
-
-
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
2.1.1.99
CHAPS
highest activity with 3 mg/ml
Catharanthus roseus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
2.1.1.99
lysolecithin
completely elimination of activity
Catharanthus roseus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.99
chloroplast
associated with thylakoids
Catharanthus roseus
9507
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.1.99
60000
-
gel chromatography
Catharanthus roseus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2.1.1.99
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
Catharanthus roseus
enzyme is involved in the biosynthesis of vindoline from tabersonine
S-adenosyl-L-homocysteine + deacetoxyvindoline
-
-
-
Organic Solvent Stability (protein specific)
EC Number
Organic Solvent
Commentary
Organism
2.1.1.99
additional information
CHAPS: 232% activity is solubilized; octyl-beta-D-glucoside: 0.15% solution 100% of activity
Catharanthus roseus
2.1.1.99
Triton X-100
0.1% Triton X-100 90% of activity
Catharanthus roseus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.1.99
partially
Catharanthus roseus
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.1.1.99
additional information
-
-
Catharanthus roseus
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
2.1.1.99
-20°C, in absence of CHAPS, 4 days, 50% loss of activity
Catharanthus roseus
2.1.1.99
-20°C, in absence of detergent by adding 25% glycerol, one week, 9% loss of activity
Catharanthus roseus
2.1.1.99
-20°C, in presence of 0.6% CHAPS, 7 days, 50% loss of activity
Catharanthus roseus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2.1.1.99
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
485692
Catharanthus roseus
?
-
-
-
-
2.1.1.99
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
high degree of specifity for the N-indole of 2,3-dihydro-3-hydroxytabersonine
485692
Catharanthus roseus
S-adenosyl-L-homocysteine + deacetoxyvindoline
-
-
-
?
2.1.1.99
S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine
enzyme is involved in the biosynthesis of vindoline from tabersonine
485692
Catharanthus roseus
S-adenosyl-L-homocysteine + deacetoxyvindoline
-
-
-
-