Information on EC 2.1.1.B75 - flavonoid 7-O-methyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.1.1.B75
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
flavonoid 7-O-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 7-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 7-methoxyflavonoid
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:flavonoid 7-O-methyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + kaempferol
2 S-adenosyl-L-homocysteine + 3,7-O-dimethylkaempferol
show the reaction diagram
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activity only of enzyme mutant POMT7-M1, D257G, not of wild-type POMT7
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-
?
2 S-adenosyl-L-methionine + quercetin
2 S-adenosyl-L-homocysteine + 3,7-O-dimethylquercetin
show the reaction diagram
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activity only of enzyme mutant POMT7-M1, D257G, not of wild-type POMT7, molecular docking of quercetin into the modeled structure of Asp257Gly
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-
?
S-adenosyl-L-methionine + (2S)-5,7,4'-trihydroxyflavanone
S-adenosyl-L-homocysteine + (2S)-5,4'-dihydroxy-7-methoxyflavanone
show the reaction diagram
S-adenosyl-L-methionine + (2S)-naringenin
S-adenosyl-L-homocysteine + (2S)-sakuranetin
show the reaction diagram
S-adenosyl-L-methionine + 3,3',4',5,7-pentahydroxyflavone
S-adenosyl-L-homocysteine + 3,3',4',5-tetrahydroxy-7-methoxyflavone
show the reaction diagram
S-adenosyl-L-methionine + 3,4',5,7-tetrahydroxyflavanone
S-adenosyl-L-homocysteine + 3,4',5-trihydroxy-7-methoxyflavanone
show the reaction diagram
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i.e. kaempferol, active is identical to that with (2S)-naringenin (i.e. (2S)-5,7,4'-trihydroxyflavanone)
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S-adenosyl-L-methionine + 3,5,7,4'-tetrahydroxy-3'-methoxyflavone
S-adenosyl-L-homocysteine + 3,5,4'-trihydroxy-7,3'-dimethoxyflavone
show the reaction diagram
S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone
S-adenosyl-L-homocysteine + 5,4'-dihydroxy-7-methoxyflavone
show the reaction diagram
S-adenosyl-L-methionine + 5,7,4'-trihydroxyisoflavone
S-adenosyl-L-homocysteine + 5,4'-dihydroxy-7-methoxyisoflavone
show the reaction diagram
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i.e. genistein. 59% of the activity with (2S)-naringenin (i.e. (2S)-5,7,4'-trihydroxyflavanone)
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-
?
S-adenosyl-L-methionine + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 4'-hydroxy-7-methoxyisoflavone
show the reaction diagram
S-adenosyl-L-methionine + dihydrokaempferol
S-adenosyl-L-homocysteine + 7-O-methylaromadendrin
show the reaction diagram
S-adenosyl-L-methionine + kaempferol
S-adenosyl-L-homocysteine + 7-O-methylkaempferol
show the reaction diagram
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?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 7-O-methylquercetin
show the reaction diagram
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + kaempferol
S-adenosyl-L-homocysteine + 7-O-methylkaempferol
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 7-O-methylquercetin
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0298 - 0.0324
kaempferol
0.0324 - 0.0378
quercetin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.064 - 0.071
kaempferol
0.064 - 0.07
quercetin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9 - 2.4
kaempferol
408
1.7 - 1.9
quercetin
137
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
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x * 38000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type POMT7 and mutant POMT7-M1 fromEscherichia coli by glutathione affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tag fusion protein
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gene POMT7, error-prone polymerase chain reaction, expression of GST-tagged wild-type POMT7 and mutant POMT7-M1 in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D257G
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random mutagenesis, the mutant of POMT-7, POMT7-M1, has a novel regioselectivity, from large scale mutant screening, mutant D257G methylates the 3-hydroxyl group of flavonols in addition to 7-hydrdoxyl group
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis