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Information on EC 2.1.1.267 - flavonoid 3',5'-methyltransferase
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EC Tree
2.1.1.267 flavonoid 3',5'-methyltransferaseIUBMB Comments
Isolated from Vitis vinifera (grape) . Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin .
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Word Map
- 2.1.1.267
- anthocyanins
- flavonols
- petals
- petunia
-
o-methylation
- malvidin
- delphinidin
-
b-ring
- hybrida
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polymethoxylated
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madagascar
- eriodictyol
-
fragrant
- cyclamen
- cyanidin
-
dimethoxylated
-
nonmethylated
- periwinkle
- 3-o-glucoside
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
anthocyanin o-methyltransferase, cromt2, psaomt, anthomt, 3'-omt, nmamt6, ptaomt, myricetin o-methyltransferase, flavonoid 3',5'-methyltransferase, anthocyanin methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anthocyanin O-methyltransferase
AOMT
CrCOMT2
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-
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CrOMT2
EC 2.1.1.149
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formerly
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flavonoid 3',5'-O-dimethyltransferase
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flavonoid O-methyltransferase
flavonoid-O-methyltransferase
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methyltransferase, flavonoid
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Mg2+-independent O-methyltransferase
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S-adenosylmethionine: anthocyanin 3'5'-methyltransferase
UniProt
type II OMT
flavonoid O-methyltransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 3'-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
(1)
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-
-
S-adenosyl-L-methionine + a 5'-hydroxy-3'-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3',5'-dimethoxyflavonoid
(2)
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:flavonoid 3'-O-methyltransferase
Isolated from Vitis vinifera (grape) [2]. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin [1].
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CAS REGISTRY NUMBER
COMMENTARY
118251-36-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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11% of the activity with quercetin
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-
?
laricitrin + S-adenosyl-L-methionine
syringetin + S-adenosyl-L-homocysteine
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114% of the activity with quercetin
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-
?
luteolin + S-adenosyl-L-methionine
chrysoeriol + S-adenosyl-L-homocysteine
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42% of the activity with quercetin
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-
?
quercetin + S-adenosyl-L-methionine
isorhamnetin + S-adenosyl-L-homocysteine
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-
-
-
?
S-adenosyl-L-methionine + 2,3-dihydromyricetin
S-adenosyl-L-homocysteine + 3'-O-methyl-2,3-dihydromyricetin
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-
-
?
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
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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
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-
-
?
S-adenosyl-L-methionine + 3'-O-methylmyricetin
S-adenosyl-L-homocysteine + 3',5'-di-O-methylmyricetin
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-
-
?
S-adenosyl-L-methionine + 3'-O-methylquercetin
S-adenosyl-L-homocysteine + 3',4'-di-O-methylquercetin
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-
-
?
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 + cyanidin
S-adenosyl-L-homocysteine + 3'-methoxycyanidin
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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
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-
-
?
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
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-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-glucoside-5-O-coumaroylglucoside
S-adenosyl-L-homocysteine + peonidin 3-O-glucoside-5-O-coumaroylglucoside
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-
-
?
S-adenosyl-L-methionine + delphinidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + petunidin 3,5-O-diglucoside
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-
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?
S-adenosyl-L-methionine + delphinidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + petunidin 3-O-beta-D-glucoside
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high activity
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-
?
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
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-
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?
S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + petunidin 3-O-glucoside
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-
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?
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
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-
?
S-adenosyl-L-methionine + dihydromyricetin
S-adenosyl-L-homocysteine + ?
54% of the activity with myricetin
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-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + 3'-O-methyl-2,3-dihydroquercetin
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-
-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + ?
22% of the activity with myricetin
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?
S-adenosyl-L-methionine + fisetin
S-adenosyl-L-homocysteine + ?
Halalkalibacterium halodurans
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analysis of binding constant and docking energy
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-
?
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-homocysteine + 3'-O-methylmyricetin
best substrate
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?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + ?
Halalkalibacterium halodurans
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analysis of binding constant and docking energy
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?
S-adenosyl-L-methionine + myricitin
S-adenosyl-L-homocysteine + laricitrin
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two product isomers
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?
S-adenosyl-L-methionine + petunidin 3,5-O-diglucoside
S-adenosyl-L-homocysteine + malvidin 3,5-O-diglucoside
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?
S-adenosyl-L-methionine + petunidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + malvidin 3-O-beta-D-glucoside
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?
S-adenosyl-L-methionine + petunidin 3-O-glucoside
S-adenosyl-L-homocysteine + malvidin 3-O-glucoside
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-
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?
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'-O-methylquercetin
low activity
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-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3-methoxyquercetin
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 5-methoxyquercetin
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-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 7-methoxyquercetin
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
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-
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?
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
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
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very low activity
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + 3'-methoxyluteolin
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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
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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
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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
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additional information
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substrate specificity, overview
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isoform ROMT-15, no substrate: naringenin, apigenin, kaempferol
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additional information
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isoform ROMT-15, no substrate: naringenin, apigenin, kaempferol
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additional information
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isoform ROMT-17, no substrate: naringenin, apigenin, kaempferol
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additional information
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isoform ROMT-17, no substrate: naringenin, apigenin, kaempferol
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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 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
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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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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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the enzyme AnthOMT shows a strong affinity for glycosylated anthocyanins, while other flavonoid glycosides and aglycones are much less preferred
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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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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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
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S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
S-adenosyl-L-methionine + cyanidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + peonidin 3-O-beta-D-glucoside + H+
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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
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S-adenosyl-L-methionine + myricetin
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involvement in biosynthesis of flavonol glycosides and anthocyanins
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S-adenosyl-L-methionine + petunidin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + malvidin 3-O-beta-D-glucoside
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S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
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S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
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S-adenosyl-L-methionine + a 3'-hydroxyflavonoid
S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid
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S-adenosyl-L-methionine + delphinidin 3-O-glucoside
S-adenosyl-L-homocysteine + 3'-methoxydelphinidin 3-O-glucoside
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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
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additional information
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CROMT2 is involved in biosynthesis of glycosides and anthocyanins
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additional information
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CROMT2 is involved in biosynthesis of glycosides and anthocyanins
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additional information
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OMT2 performs two sequential methylations at the 3'-and 5'-positions of the B-ring in myricetin (flavonol) and dihydromyricetin (dihydroflavonol)
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additional information
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OMT2 performs two sequential methylations at the 3'-and 5'-positions of the B-ring in myricetin (flavonol) and dihydromyricetin (dihydroflavonol)
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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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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Zn2+
additional information
Ca2+
Halalkalibacterium halodurans
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interactions between flavonoid and enzyme are enhanced by metal-mediated electrostatic interactions in substrate binding site. Ca2+ and Mg2+ show similar effects
Co2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 41% of the activity with Mg2+ (with quercetin as substrate)
Co2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 82% of the activity with Mg2+ (with quercetin as substrate)
Mg2+
Halalkalibacterium halodurans
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interactions between flavonoid and enzyme are enhanced by metal-mediated electrostatic interactions in substrate binding site. Ca2+ and Mg2+ show similar effects
Mg2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity (with quercetin as substrate)
Mn2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Mn2+ shows 69% of the activity with Mg2+ (with quercetin as substrate)
Mn2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Mn2+ shows 74% of the activity with Mg2+ (with quercetin as substrate)
additional information
the enzyme is an Mg2+-independent O-methyltransferase
additional information
the enzyme is an Mg2+-independent O-methyltransferase
additional information
the enzyme is an Mg2+-independent O-methyltransferase
additional information
the enzyme is an Mg2+-independent O-methyltransferase
additional information
the enzyme is an Mg2+-independent O-methyltransferase
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Iron Deficiencies
Iron deficiency stimulates anthocyanin accumulation in grapevine apical leaves.
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