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IUBMB Comments The flavonoids vitexin and isovitexin 2′′-O -arabinoside do not act as substrates for the enzyme from oats (Avena sativa ).
Synonyms
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AdoMet:vitexin 2''-O-rhamnoside 7-O-methyltransferase
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methyltransferase, vitexin 2''-O-rhamnoside 7-O-
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S-adenosyl-L-methionine:vitexin 2''-O-rhamnoside 7-O-methyltransferase
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside = S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside = S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside = S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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transfer of methyl group
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MetaCyc
vitexin and derivatives biosynthesis
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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).
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S-adenosyl-L-methionine + apigenin
S-adenosyl-L-homocysteine + 7-O-methylapigenin
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Substrates: 5-10% of the rate with vitexin 2-O-rhamnoside as substrate
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
additional information
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Substrates: not: caffeic acid, naringenin, vitexin, isovitexin 2-O-arabinoside
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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Substrates: last step in the biosynthetic pathway to the flavonoid 7-O-methylvitexin 2-O-rhamnoside
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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Substrates: flavonoid biosynthesis, final enzyme of the vitexin branch of the pathway
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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Substrates: 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
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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Substrates: FMT specifically catalyzes the transfer of a methyl group to the 7-hydroxyl group of vitexin 2-O-rhamnoside
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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Substrates: last step in the biosynthetic pathway to the flavonoid 7-O-methylvitexin 2-O-rhamnoside
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S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside
S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside
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Substrates: flavonoid biosynthesis, final enzyme of the vitexin branch of the pathway
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phosphate
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the highest activity is obtained in 0.1-0.2 M phosphate buffer, at lower ionic strength the activity drops drastically
additional information
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not activated by Mg2+ or 2-mercaptoethanol
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7-O-methylvitexin
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competitive inhibition
7-O-methylvitexin 2''-O-beta-L-rhamnoside
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product inhibition, kinetics
S-adenosyl-L-homocysteine
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strong product inhibition, kinetics
vitexin
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competitive inhibition
additional information
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not inhibited by Mg2+ or 2-mercaptoethanol
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0.0016
S-adenosyl-L-methionine
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pH 7.5, 30°C
0.015
vitexin 2''-O-beta-L-rhamnoside
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pH 7.5, 30°C
additional information
additional information
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kinetic mechanism, mono-iso Theorell-Chance mechanism with the nucleotide substrate binding before the flavonoid
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additional information
additional information
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additional information
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6.4 - 8.6
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50% of the maximum activity at pH 6.4 and 8.6
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cv. Flämingskrone
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brenda
Gelbhafer Flämingskrone
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brenda
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additional information
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FMT activity profile as a function of plant age
brenda
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primary leaves
brenda
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primary leaves, tissue-specific activity in different stages of leaf growth, FMT is located in the mesophyll
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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2-mercaptoethanol stabilizes during purification procedures or storage
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-20°C, purified enzyme, 10 mM 2-mercaptoethanol, 50% glycerol, 1 year, 30-40% loss of activity
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Knogge, W.; Weissenboeck, G.
Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine: vitexin 2"-O-rhamnoside 7-O-methyltransferase of Avena sativa L
Eur. J. Biochem.
140
113-118
1984
Avena sativa
brenda
Knogge, W.; Weissenboeck, G.
Tissue-distribution of secondary phenolic biosynthesis in developing primary leaves of Avena sativa L.
Planta
167
196-205
1986
Avena sativa
brenda
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