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2 S-adenosyl-L-methionine + myricetin
2 S-adenosyl-L-homocysteine + syringetin
4 S-adenosyl-L-methionine + quercetin
4 S-adenosyl-L-homocysteine + 3,3',5,7-tetramethoxyquercetin
whole-cell biocatalysis using CdFOMT5 expressed in Escherichia coli cells is performed using quercetin as a substrate, and 3,3',5,7-tetramethylated quercetin is obtained as the final product
-
-
?
eriodictyol + S-adenosyl-L-methionine
homoeriodictyol + S-adenosyl-L-homocysteine
-
11% of the activity with quercetin
-
-
?
laricitrin + S-adenosyl-L-methionine
syringetin + S-adenosyl-L-homocysteine
-
114% of the activity with quercetin
-
-
?
luteolin + S-adenosyl-L-methionine
chrysoeriol + S-adenosyl-L-homocysteine
-
42% of the activity with quercetin
-
-
?
quercetin + S-adenosyl-L-methionine
isorhamnetin + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + 2,3-dihydromyricetin
S-adenosyl-L-homocysteine + 3'-O-methyl-2,3-dihydromyricetin
-
-
-
?
S-adenosyl-L-methionine + 3'-methoxydelphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3',5'-dimethoxydelphinidin 3-O-glucoside
S-adenosyl-L-methionine + 3'-O-methyl-2,3-dihydromyricetin
S-adenosyl-L-homocysteine + 3',5'-di-O-methyl-2,3-dihydromyricetin
-
i.e. syringetin
-
?
S-adenosyl-L-methionine + 3'-O-methyl-2,3-dihydroquercetin
S-adenosyl-L-homocysteine + 3',4'-di-O-methyl-2,3-dihydroquercetin
-
-
-
?
S-adenosyl-L-methionine + 3'-O-methylmyricetin
S-adenosyl-L-homocysteine + 3',5'-di-O-methylmyricetin
-
-
-
?
S-adenosyl-L-methionine + 3'-O-methylquercetin
S-adenosyl-L-homocysteine + 3',4'-di-O-methylquercetin
-
-
-
?
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
S-adenosyl-L-methionine + caffeoyl-coenzyme A
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + cyanidin
S-adenosyl-L-homocysteine + 3'-methoxycyanidin
-
very low activity
-
-
?
S-adenosyl-L-methionine + cyanidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + 3'-methoxycyanidin 3,5-O-diglucoside
S-adenosyl-L-methionine + cyanidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + peonidin 3,5-O-diglucoside
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + peonidin 3-O-beta-D-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + peonidin 3-O-beta-D-glucoside + H+
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxycyanidin 3-O-glucoside
S-adenosyl-L-methionine + cyanidin 3-O-glucoside
S-adenosyl-L-homocysteine + peonidin 3-O-glucoside
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-glucoside-5-O-coumaroylglucoside
S-adenosyl-L-homocysteine + peonidin 3-O-glucoside-5-O-coumaroylglucoside
-
-
-
?
S-adenosyl-L-methionine + delphinidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + petunidin 3,5-O-diglucoside
-
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + petunidin 3-O-beta-D-glucoside
-
high activity
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxydelphinidin 3-O-glucoside
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + petunidin 3-O-beta-D-glucoside
-
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + petunidin 3-O-glucoside
-
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside-5-O-coumaroylglucoside
S-adenosyl-L-homocysteine + petunidin 3-O-glucoside-5-O-coumaroylglucoside
-
-
-
?
S-adenosyl-L-methionine + dihydromyricetin
?
two sequential methylations at the 3'- and 5'-positions of the B-ring in dihydromyricetin
-
-
?
S-adenosyl-L-methionine + dihydromyricetin
S-adenosyl-L-homocysteine + ?
54% of the activity with myricetin
-
-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + 3'-O-methyl-2,3-dihydroquercetin
-
-
-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + ?
22% of the activity with myricetin
-
-
?
S-adenosyl-L-methionine + fisetin
S-adenosyl-L-homocysteine + ?
Halalkalibacterium halodurans
-
analysis of binding constant and docking energy
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + 3'-methoxyluteolin
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + luteolin 7-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxyluteolin 7-O-glucoside
S-adenosyl-L-methionine + myricetin
?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + 3'-O-methylmyricetin
best substrate
-
-
?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + ?
Halalkalibacterium halodurans
-
analysis of binding constant and docking energy
-
-
?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + syringetin
S-adenosyl-L-methionine + myricitin
S-adenosyl-L-homocysteine + laricitrin
-
-
two product isomers
-
?
S-adenosyl-L-methionine + petunidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + malvidin 3,5-O-diglucoside
-
-
-
?
S-adenosyl-L-methionine + petunidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + malvidin 3-O-beta-D-glucoside
-
-
-
?
S-adenosyl-L-methionine + petunidin 3-O-glucoside
S-adenosyl-L-homocysteine + malvidin 3-O-glucoside
-
-
-
?
S-adenosyl-L-methionine + petunidin 3-O-glucoside-5-O-coumaroylglucoside
S-adenosyl-L-homocysteine + malvidin 3-O-glucoside-5-O-coumaroylglucoside
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3'-methoxyquercetin
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3'-O-methylquercetin
low activity
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3-methoxyquercetin
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 5-methoxyquercetin
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 7-methoxyquercetin
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
-
-
-
-
?
S-adenosyl-L-methionine + quercetin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + isorhamnetin 3-O-beta-D-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + quercetin 3-O-beta-D-rutinoside
S-adenosyl-L-homocysteine + isorhamnetin 3-O-beta-D-rutinoside
-
-
-
-
?
S-adenosyl-L-methionine + quercetin 3-O-rutinoside
S-adenosyl-L-homocysteine + 3'-methoxyquercetin 3-O-rutinoside
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + ?
additional information
?
-
2 S-adenosyl-L-methionine + myricetin
2 S-adenosyl-L-homocysteine + syringetin
the enzyme also catalyzes the methylation of luteolin, tricetin and caffeoyl-CoA. ROMT-15 exhibits similar kcat/Km values for the four substrates. ROMT-15 can not utilize naringenin, apigenin, or kaempferol. The 2,3-double bond and the O-dihydroxyl group are both required for catalytic activity
syringetin is the 3',5'-dimethyl ether of myricetin
-
?
2 S-adenosyl-L-methionine + myricetin
2 S-adenosyl-L-homocysteine + syringetin
the enzyme also catalyzes the methylation of luteolin, tricetin and caffeoyl-CoA. ROMT-17 prefers tricetin. ROMT-15 can not utilize naringenin, apigenin, or kaempferol. The 2,3-double bond and the O-dihydroxyl group are both required for catalytic activity
syringetin is the 3',5'-dimethyl ether of myricetin
-
?
S-adenosyl-L-methionine + 3'-methoxydelphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3',5'-dimethoxydelphinidin 3-O-glucoside
very low activity, with delphinidin 3-O-glucoside as substrate, NmAMT6 almost exclusively yields petunidin 3-O-glucoside rather than malvidin 3-O-glucoside. This specificity is consistent with the anthocyanin composition of Nemophila petals
-
-
?
S-adenosyl-L-methionine + 3'-methoxydelphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3',5'-dimethoxydelphinidin 3-O-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + 3'-methoxydelphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3',5'-dimethoxydelphinidin 3-O-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
-
-
-
-
?
S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
-
-
-
-
?
S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-coenzyme A
S-adenosyl-L-homocysteine + ?
isoform ROMT-15, 100% of the activity with myricetin
-
-
?
S-adenosyl-L-methionine + caffeoyl-coenzyme A
S-adenosyl-L-homocysteine + ?
isoform ROMT-17, 100% of the activity with myricetin
-
-
?
S-adenosyl-L-methionine + cyanidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + 3'-methoxycyanidin 3,5-O-diglucoside
-
substrate binding structure, modelling, overview
-
-
?
S-adenosyl-L-methionine + cyanidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + 3'-methoxycyanidin 3,5-O-diglucoside
-
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxycyanidin 3-O-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxycyanidin 3-O-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxydelphinidin 3-O-glucoside
-
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxydelphinidin 3-O-glucoside
with delphinidin 3-O-glucoside as substrate, NmAMT6 almost exclusively yields petunidin 3-O-glucoside rather than malvidin 3-O-glucoside. This specificity is consistent with the anthocyanin composition of Nemophila petals
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxydelphinidin 3-O-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxydelphinidin 3-O-glucoside
-
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + 3'-methoxyluteolin
-
very low activity
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + 3'-methoxyluteolin
-
low activity
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
Halalkalibacterium halodurans
-
analysis of binding constant and docking energy
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
isoform ROMT-15, 92% of the activity with myricetin
isoform ROMT-15, methylation at 3'-hydroxyl group
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
isoform ROMT-17, 92% of the activity with myricetin
isoform ROMT-17, methylation at 3'-hydroxyl group
-
?
S-adenosyl-L-methionine + luteolin 7-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxyluteolin 7-O-glucoside
-
low activity
-
-
?
S-adenosyl-L-methionine + luteolin 7-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxyluteolin 7-O-glucoside
-
low activity
-
-
?
S-adenosyl-L-methionine + myricetin
?
two sequential methylations at the 3'- and 5'-positions of the B-ring in myricetin, activity is strictly confined to flavonols and dihydroflavonols, it requires at least 2 B-ring hydroxyl groups
-
-
?
S-adenosyl-L-methionine + myricetin
?
involvement in biosynthesis of flavonol glycosides and anthocyanins
-
-
?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + syringetin
-
-
-
?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + syringetin
-
isoform ROMT-15, methylation at 3'-hydroxyl group and at the 5' hydroxyl group
-
?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + syringetin
-
isoform ROMT-17, methylation at 3'-hydroxyl group and at the 5' hydroxyl group
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3'-methoxyquercetin
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3'-methoxyquercetin
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3'-methoxyquercetin
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
Halalkalibacterium halodurans
-
analysis of binding constant and docking energy
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
isoform ROMT-15, methylation at 3'-hydroxyl group
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
isoform ROMT-17, methylation at 3'-hydroxyl group
-
?
S-adenosyl-L-methionine + quercetin 3-O-rutinoside
S-adenosyl-L-homocysteine + 3'-methoxyquercetin 3-O-rutinoside
-
-
-
-
?
S-adenosyl-L-methionine + quercetin 3-O-rutinoside
S-adenosyl-L-homocysteine + 3'-methoxyquercetin 3-O-rutinoside
-
-
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + ?
isoform ROMT-15, methylation at 3'-hydroxyl group and at the 5' hydroxyl group. 87% of the activity with myricetin
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + ?
isoform ROMT-17, methylation at 3'-hydroxyl group and at the 5' hydroxyl group. 87% of the activity with myricetin
-
-
?
additional information
?
-
-
CROMT2 is involved in biosynthesis of glycosides and anthocyanins
-
-
?
additional information
?
-
CROMT2 is involved in biosynthesis of glycosides and anthocyanins
-
-
?
additional information
?
-
-
OMT2 performs two sequential methylations at the 3'-and 5'-positions of the B-ring in myricetin (flavonol) and dihydromyricetin (dihydroflavonol)
-
-
?
additional information
?
-
OMT2 performs two sequential methylations at the 3'-and 5'-positions of the B-ring in myricetin (flavonol) and dihydromyricetin (dihydroflavonol)
-
-
?
additional information
?
-
-
no activity with kaempferol, dihydrokaempferol, caffeate and caffeate esters
-
-
?
additional information
?
-
no activity with kaempferol, dihydrokaempferol, caffeate and caffeate esters
-
-
?
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity. Isozyme CdFOMT5 exhibits O-methyltransferase activity for quercetin, naringenin, (-)-epicatechin, and equol using S-adenosyl-L-methionine (SAM) as a methyl donor. The recombinant CdFOMT5 CdFOMT5 can catalyze the O-methylation of at least three hydroxyl groups of quercetin, and di- or tri-O-methylated quercetin products are obtained by this enzymatic reaction. CdFMOT5 prefers flavonol (3-hydroxyflavone) to other flavonoid structures. Thus, substrate structure, especially the C-ring in flavonoids, may strongly affect the substrate preference, including regioselectivity, of CdFOMT5
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity. Isozyme CdFOMT5 exhibits O-methyltransferase activity for quercetin, naringenin, (-)-epicatechin, and equol using S-adenosyl-L-methionine (SAM) as a methyl donor. The recombinant CdFOMT5 CdFOMT5 can catalyze the O-methylation of at least three hydroxyl groups of quercetin, and di- or tri-O-methylated quercetin products are obtained by this enzymatic reaction. CdFMOT5 prefers flavonol (3-hydroxyflavone) to other flavonoid structures. Thus, substrate structure, especially the C-ring in flavonoids, may strongly affect the substrate preference, including regioselectivity, of CdFOMT5
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity. Isozyme CdFOMT5 exhibits O-methyltransferase activity for quercetin, naringenin, (-)-epicatechin, and equol using S-adenosyl-L-methionine (SAM) as a methyl donor. The recombinant CdFOMT5 CdFOMT5 can catalyze the O-methylation of at least three hydroxyl groups of quercetin, and di- or tri-O-methylated quercetin products are obtained by this enzymatic reaction. CdFMOT5 prefers flavonol (3-hydroxyflavone) to other flavonoid structures. Thus, substrate structure, especially the C-ring in flavonoids, may strongly affect the substrate preference, including regioselectivity, of CdFOMT5
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity. Isozyme CdFOMT5 exhibits O-methyltransferase activity for quercetin, naringenin, (-)-epicatechin, and equol using S-adenosyl-L-methionine (SAM) as a methyl donor. The recombinant CdFOMT5 CdFOMT5 can catalyze the O-methylation of at least three hydroxyl groups of quercetin, and di- or tri-O-methylated quercetin products are obtained by this enzymatic reaction. CdFMOT5 prefers flavonol (3-hydroxyflavone) to other flavonoid structures. Thus, substrate structure, especially the C-ring in flavonoids, may strongly affect the substrate preference, including regioselectivity, of CdFOMT5
-
-
-
additional information
?
-
the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity. Isozyme CdFOMT5 exhibits O-methyltransferase activity for quercetin, naringenin, (-)-epicatechin, and equol using S-adenosyl-L-methionine (SAM) as a methyl donor. The recombinant CdFOMT5 CdFOMT5 can catalyze the O-methylation of at least three hydroxyl groups of quercetin, and di- or tri-O-methylated quercetin products are obtained by this enzymatic reaction. CdFMOT5 prefers flavonol (3-hydroxyflavone) to other flavonoid structures. Thus, substrate structure, especially the C-ring in flavonoids, may strongly affect the substrate preference, including regioselectivity, of CdFOMT5
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
isoform ROMT-15, no substrate: naringenin, apigenin, kaempferol
-
-
?
additional information
?
-
isoform ROMT-15, no substrate: naringenin, apigenin, kaempferol
-
-
?
additional information
?
-
-
isoform ROMT-17, no substrate: naringenin, apigenin, kaempferol
-
-
?
additional information
?
-
isoform ROMT-17, no substrate: naringenin, apigenin, kaempferol
-
-
?
additional information
?
-
-
substrate specificity study using a number of potential substrates including anthocyanidins, anthocyanins, flavonols, flavones, flavan-3-ols, and phenolic acid as substrates based on optimized conditions, overview. Enzyme PsAOMT uses anthocyanins as methoxyl accepters, and acts to methylate the 3'-hydroxyl group of the B-ring with high affinity and efficiency. Pelargonidin 3-O-glucoside is the only tested anthocyanin compound that is not a substrate for PsAOMT. With delphinidin 3-O-glucoside, a sequential methylation occurs at the 3'- and 5'-hydroxyl group on the B-ring. In comparison with the substrates delphinidin 3-O-glucoside, quercetin 3-O-rutinoside, and quercetin, PsAOMT has a higher affinity for cyanidin 3-O-glucoside and cyanidin 3,5-O-diglucoside. Cyanidin-derived anthocyanins are high-affinity substrates for PsAOMT. No activity with the antocyanin pelargonidin 3-O-glucoside and the cyanidin delphinin. The enzyme also shows no activity with kaempferol 3-O-glucoside, kaempferol, apigenin, naringenin, epicatechin, and caffeic acid
-
-
-
additional information
?
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substrate specificity study using a number of potential substrates including anthocyanidins, anthocyanins, flavonols, flavones, flavan-3-ols, and phenolic acid as substrates based on optimized conditions, overview. Enzyme PtAOMT uses anthocyanins as methoxyl accepters, and acts to methylate the 3'-hydroxyl group of the B-ring with high affinity and efficiency. Pelargonidin 3-O-glucoside is the only tested anthocyanin compound that is not a substrate for PtAOMT. With delphinidin 3-O-glucoside, a sequential methylation occurs at the 3'- and 5'-hydroxyl group on the B-ring. In comparison with the substrates delphinidin 3-O-glucoside, quercetin 3-O-rutinoside, and quercetin, PtAOMT has a higher affinity for cyanidin 3-O-glucoside and cyanidin 3,5-O-diglucoside. Cyanidin-derived anthocyanins are high-affinity substrates for PtAOMT. No activity with the antocyanin pelargonidin 3-O-glucoside and the cyanidin delphinin. The enzyme also shows no activity with kaempferol 3-O-glucoside, kaempferol, apigenin, naringenin, epicatechin, and caffeic acid
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additional information
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enzyme is a regiospecific flavonoid 3'/5'-O-methyltransferase showing higher binding affinity and catalytic efficiency for quercetin and luteolin than for eriodictyol. No substrates: naringenin, apigenin, tricetin, kaempferol, daidzein, genistein
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additional information
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the enzyme AnthOMT shows a strong affinity for glycosylated anthocyanins, while other flavonoid glycosides and aglycones are much less preferred
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additional information
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the specificity of AnthOMT is mainly directed towards the 3' and 5' positions of the anthocyanin B-ring, to produce petunidin and malvidin glucosides, and is not active at the 4' position, substrate specificity of enzyme AnthOMT, overview. Poor activity with caffeic acid, no activity with pelargonidin-3-glucoside and delphinidin. AnthOMT is able to methylate the more complex substrates, e.g. an an extract of semi-polar compounds from Ros/Del tomato fruits preparation, resulting in a strong increase in malvidin 3-(4-coumaroyl)-rutinoside-5-glucoside
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additional information
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anthocyanin O-methyltransferase methylates anthocyanins of both groups, di- and trihydroxylated anthocyanins, quantitative trait locus analyses for the ratios of tri/di-hydroxylated and methylated/non-methylated anthocyanins using a population from an interspecific hybrid cross, relationship between the genotypes of the markers closest to the major quantitative trait loci and the expression levels of anthocyanin biosynthetic genes, overview
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L87A
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site-directed mutagenesis, the mutant shows highly decreased catalytic efficency, the observed in vitro catalytic efficiency of PtAOMT-L87R mutant is equal to that of Paeonia tenuifolia PtAOMT wild-type
L87R
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site-directed mutagenesis, the mutant shows highly decreased catalytic efficency, the observed in vitro catalytic efficiency of PtAOMT-L87R mutant is equal to that of Paeonia tenuifolia PtAOMT wild-type
G13E
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site-directed mutagenesis, the mutant shows increased activity compared to wild-type
R87L
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site-directed mutagenesis, the mutant shows highly increased catalytic efficency, the observed in vitro catalytic efficiency of PtAOMT-R87L mutant is equal to that of Paeonia suffruticosa PsAOMT wild-type
T205R
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site-directed mutagenesis, the mutant shows increased activity compared to wild-type
T85A
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site-directed mutagenesis, the mutant shows increased activity compared to wild-type
D168L
isoform ROMT-15, complete loss of activity
D168L
mutation abolishes activity (with quercetin as substrate)
D194L
isoform ROMT-15, complete loss of activity
D194L
mutation abolishes activity (with quercetin as substrate)
D209L
isoform ROMT-17, complete loss of activity
D209L
mutation abolishes activity (with quercetin as substrate)
D234L
isoform ROMT-17, complete loss of activity
D234L
mutation abolishes activity (with quercetin as substrate)
E112L
isoform ROMT-17, 14% loss of activity
E112L
mutation results in 40% loss of activity (with quercetin as substrate)
E69L
isoform ROMT-15, 14% loss of activity
E69L
mutation results in 14% loss of activity (with quercetin as substrate)
N195I
isoform ROMT-15, complete loss of activity
N195I
mutation abolishes activity (with quercetin as substrate)
N235I
isoform ROMT-17, complete loss of activity
N235I
mutation abolishes activity (with quercetin as substrate)
additional information
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silencing of AnthOMT in hypocotyl tissue, several hypocotyls of three lines (57, 85 and 87) show an anthocyanin profile that is different to that of the wild-type, and show a strong reduction in malvidin-type anthocyanins, while other lines (64, 66 and 71) show only wild-type anthocyanin profiles
additional information
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construction of a multifunctional flavonoid O-methyltransferase fusing tomato 3'-O-methyltransferase OMT3 and Oryza sativa naringenin 7-O-methyltransferase NOMT. The OMT3/NOMT fusion enzyme possesses both 3'- and 7-OMT activities to diverse flavonoid substrates, which are comparable to those of individual OMT3 and NOMT. The OMT3/OsNOMT enzyme also shows 3'- and 7-OMT activity for 7- or 3'-O-methylflavonoids, respectively. The biotransformation of the flavonoids quercetin, luteolin, eriodictyol, and taxifolin using OMT3/NOMT-transformed Escherichia coli generates corresponding di-O-methylflavonoids, rhamnazin, velutin, 3',7-di-O-methyleriodictyol, and 3',7-di-Omethyltaxifolin, respectively
additional information
construction of a multifunctional flavonoid O-methyltransferase fusing tomato 3'-O-methyltransferase OMT3 and Oryza sativa naringenin 7-O-methyltransferase NOMT. The OMT3/NOMT fusion enzyme possesses both 3'- and 7-OMT activities to diverse flavonoid substrates, which are comparable to those of individual OMT3 and NOMT. The OMT3/OsNOMT enzyme also shows 3'- and 7-OMT activity for 7- or 3'-O-methylflavonoids, respectively. The biotransformation of the flavonoids quercetin, luteolin, eriodictyol, and taxifolin using OMT3/NOMT-transformed Escherichia coli generates corresponding di-O-methylflavonoids, rhamnazin, velutin, 3',7-di-O-methyleriodictyol, and 3',7-di-Omethyltaxifolin, respectively
additional information
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generation of a multifunctional FOMT fusing a 3'-OMT (SlOMT3, EC 2.1.1.267) and a 7-OMT (OsNOMT, EC 2.1.1.82). The SlOMT3/OsNOMT fusion enzyme possesses both 3'- and 7-OMT activities to diverse flavonoid substrates, which are comparable to those of individual SlOMT3 and OsNOMT. The SlOMT3/OsNOMT enzyme also shows 3'- and 7-OMT activity for 7- or 3'-O-methylflavonoids, respectively, suggesting that the fusion enzyme can sequentially methylate flavonoids into di-O-methylflavonoids. The biotransformation of the flavonoids quercetin, luteolin, eriodictyol, and taxifolin using SlOMT3/OsNOMT-transformed Escherichia coli generated corresponding di-O-methylflavonoids, rhamnazin, velutin, 3',7-di-O-methyleriodictyol, and 3',7-di-O-methyltaxifolin, respectively. These results indicate that dimethoxyflavonoids may be efficiently produced from non-methylated flavonoid precursors through a one-step biotransformation using the engineered Escherichia coli harboring the SlOMT3/OsNOMT fusion gene
additional information
generation of a multifunctional FOMT fusing a 3'-OMT (SlOMT3, EC 2.1.1.267) and a 7-OMT (OsNOMT, EC 2.1.1.82). The SlOMT3/OsNOMT fusion enzyme possesses both 3'- and 7-OMT activities to diverse flavonoid substrates, which are comparable to those of individual SlOMT3 and OsNOMT. The SlOMT3/OsNOMT enzyme also shows 3'- and 7-OMT activity for 7- or 3'-O-methylflavonoids, respectively, suggesting that the fusion enzyme can sequentially methylate flavonoids into di-O-methylflavonoids. The biotransformation of the flavonoids quercetin, luteolin, eriodictyol, and taxifolin using SlOMT3/OsNOMT-transformed Escherichia coli generated corresponding di-O-methylflavonoids, rhamnazin, velutin, 3',7-di-O-methyleriodictyol, and 3',7-di-O-methyltaxifolin, respectively. These results indicate that dimethoxyflavonoids may be efficiently produced from non-methylated flavonoid precursors through a one-step biotransformation using the engineered Escherichia coli harboring the SlOMT3/OsNOMT fusion gene
additional information
flower color modification in Rosa hybrida by expressing the S-adenosylmethionine: anthocyanin 3',5'-O-methyltransferase gene from Torenia hybrida, phenotypes of T-DNA insertion transgenic plants, overview
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Cacace, S.; Schrder, G.; Wehinger, E.; Strack, D.; Schmidt, J.; Schrder, J.
A flavonol O-methyltransferase from Catharanthus roseus performing two sequential methylations
Phytochemistry
62
127-137
2003
Catharanthus roseus, Catharanthus roseus (Q8GSN1)
brenda
Jeong, K.; Lee, J.; Kang, D.; Lee, J.; Hwang, Y.; Kim, Y.
Flavonoids as substrates of Bacillus halodurans O-methyltransferase
Bull. Korean Chem. Soc.
29
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Halalkalibacterium halodurans
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Lee, Y.; Kim, B.; Chong, Y.; Lim, Y.; Ahn, J.
Cation dependent O-methyltransferases from rice
Planta
227
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Oryza sativa, Oryza sativa (Q9XGP7)
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Hugueney, P.; Provenzano, S.; Verries, C.; Ferrandino, A.; Meudec, E.; Batelli, G.; Merdinoglu, D.; Cheynier, V.; Schubert, A.; Ageorges, A.
A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine
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Fournier-Level, A.; Hugueney, P.; Verries, C.; This, P.; Ageorges, A.
Genetic mechanisms underlying the methylation level of anthocyanins in grape (Vitis vinifera L.)
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Vitis vinifera (G0YKW8)
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Cho, M.; Park, H.; Park, J.; Lee, S.; Bhoo, S.; Hahn, T.
Characterization of regiospecific flavonoid 3'/5'-O-methyltransferase from tomato and its application in flavonoid biotransformation
J. Korean Soc. Appl. Biol. Chem.
55
749-755
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Solanum lycopersicum
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Gomez Roldan, M.V.; Outchkourov, N.; van Houwelingen, A.; Lammers, M.; Romero de la Fuente, I.; Ziklo, N.; Aharoni, A.; Hall, R.D.; Beekwilder, J.
An O-methyltransferase modifies accumulation of methylated anthocyanins in seedlings of tomato
Plant J.
80
695-708
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Solanum lycopersicum
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Azuma, A.; Ban, Y.; Sato, A.; Kono, A.; Shiraishi, M.; Yakushiji, H.; Kobayashi, S.
MYB diplotypes at the color locus affect the ratios of tri/di-hydroxylated and methylated/non-methylated anthocyanins in grape berry skin
Tree Genet. Genomes
11
31
2015
Vitis vinifera (C7AE94)
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brenda
Itoh, N.; Iwata, C.; Toda, H.
Molecular cloning and characterization of a flavonoid-O-methyltransferase with broad substrate specificity and regioselectivity from Citrus depressa
BMC Plant Biol.
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Citrus depressa (A0A120MXL9), Citrus depressa (A0A120MXM2), Citrus depressa (A0A120MXM3), Citrus depressa (A0A125T1T4), Citrus depressa (A0A125T1T5)
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Du, H.; Wu, J.; Ji, K.X.; Zeng, Q.Y.; Bhuiya, M.W.; Su, S.; Shu, Q.Y.; Ren, H.X.; Liu, Z.A.; Wang, L.S.
Methylation mediated by an anthocyanin, O-methyltransferase, is involved in purple flower coloration in Paeonia
J. Exp. Bot.
66
6563-6577
2015
Paeonia suffruticosa, Paeonia tenuifolia
brenda
Lee, D.; Park, H.L.; Lee, S.W.; Bhoo, S.H.; Cho, M.H.
Biotechnological production of dimethoxyflavonoids using a fusion flavonoid O-methyltransferase possessing both 3- and 7-O-methyltransferase activities
J. Nat. Prod.
80
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2017
Solanum lycopersicum, Solanum lycopersicum (K4D2J5)
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Nakamura, N.; Katsumoto, Y.; Brugliera, F.; Demelis, L.; Nakajima, D.; Suzuki, H.; Tanaka, Y.
Flower color modification in Rosa hybrida by expressing the S-adenosylmethionine anthocyanin 3',5'-O-methyltransferase gene from Torenia hybrida
Plant Biotechnol.
32
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Torenia hybrid cultivar (A0A090BN67)
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Molecular cloning of flavonoid biosynthetic genes and biochemical characterization of anthocyanin O-methyltransferase of Nemophila menziesii Hook. and Arn
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