Information on EC 2.1.1.153 - vitexin 2''-O-rhamnoside 7-O-methyltransferase

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The expected taxonomic range for this enzyme is: Avena sativa

EC NUMBER
COMMENTARY
2.1.1.153
-
RECOMMENDED NAME
GeneOntology No.
vitexin 2''-O-rhamnoside 7-O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside = S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
show the reaction diagram
the flavonoids vitexin and isovitexin 2’’-O-arabinoside do not act as substrates for the enzyme from oats, Avena sativa, kinetic mechanism, mono-iso Theorell-Chance mechanism
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Flavone and flavonol biosynthesis
-
-
vitexin and derivatives biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:vitexin-2''-O-beta-L-rhamnoside 7-O-methyltransferase
The flavonoids vitexin and isovitexin 2''-O-arabinoside do not act as substrates for the enzyme from oats (Avena sativa).
CAS REGISTRY NUMBER
COMMENTARY
90698-29-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Flämingskrone
-
-
Manually annotated by BRENDA team
Gelbhafer Flämingskrone
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + apigenin
S-adenosyl-L-homocysteine + 7-O-methylapigenin
show the reaction diagram
-
5-10% of the rate with vitexin 2’’-O-rhamnoside as substrate
-
-
?
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
show the reaction diagram
-
flavonoid biosynthesis, final enzyme of the vitexin branch of the pathway
-
-
?
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
show the reaction diagram
-
last step in the biosynthetic pathway to the flavonoid 7-O-methylvitexin 2’’-O-rhamnoside, catalyzes the transfer of the methyl group of S-adenosyl-L-methionine to the A-ring 7-hydroxyl group of vitexin 2’’-O-rhamnoside, very high substrate specificity, mono-iso Theorell-Chance mechanism with the nucleotide substrate binding before the flavonoid
-
-
?
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
show the reaction diagram
-
FMT specifically catalyzes the transfer of a methyl group to the 7-hydroxyl group of vitexin 2’’-O-rhamnoside
-
-
?
additional information
?
-
-
not: caffeic acid, naringenin, vitexin, isovitexin 2’’-O-arabinoside
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
show the reaction diagram
-
flavonoid biosynthesis, final enzyme of the vitexin branch of the pathway
-
-
?
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
show the reaction diagram
-
last step in the biosynthetic pathway to the flavonoid 7-O-methylvitexin 2’’-O-rhamnoside
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphate
-
the highest activity is obtained in 0.1-0.2 M phosphate buffer, at lower ionic strength the activity drops drastically
additional information
-
not activated by Mg2+ or 2-mercaptoethanol
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-O-methylvitexin
-
competitive inhibition
S-adenosyl-L-homocysteine
-
strong product inhibition, kinetics
vitexin
-
competitive inhibition
7-O-methylvitexin 2''-O-beta-L-rhamnoside
-
product inhibition, kinetics
additional information
-
not inhibited by Mg2+ or 2-mercaptoethanol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
S-adenosyl-L-methionine
-
pH 7.5, 30°C
0.015
vitexin 2''-O-beta-L-rhamnoside
-
pH 7.5, 30°C
additional information
additional information
-
kinetic mechanism, mono-iso Theorell-Chance mechanism with the nucleotide substrate binding before the flavonoid
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 8.6
-
50% of the maximum activity at pH 6.4 and 8.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
primary leaves
Manually annotated by BRENDA team
-
primary leaves, tissue-specific activity in different stages of leaf growth, FMT is located in the mesophyll
Manually annotated by BRENDA team
additional information
-
FMT activity profile as a function of plant age
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
-
gel filtration
655395
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes during purification procedures or storage
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, 10 mM 2-mercaptoethanol, 50% glycerol, 1 year, 30-40% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
180fold
-