Information on EC 2.1.1.231 - flavonoid 4'-O-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.231
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RECOMMENDED NAME
GeneOntology No.
flavonoid 4'-O-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 4'-hydroxyflavanone = S-adenosyl-L-homocysteine + a 4'-methoxyflavanone
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ponciretin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase
The enzyme catalyses the 4'-methylation of naringenin. In vitro it catalyses the 4'-methylation of apigenin, quercetin, daidzein and genistein.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene CrOMT6
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the last step in the biosynthesis of the bioactive flavonoid ponciretin, biosynthetic pathways starting with glucose, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4'-hydroxyflavanone + S-adenosyl-L-methionine
4'-methoxyflavanone + S-adenosyl-L-homocysteine
show the reaction diagram
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-
-
-
?
apigenin + S-adenosyl-L-methionine
acacetin + S-adenosyl-L-homocysteine
show the reaction diagram
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-
-
-
?
genistein + S-adenosyl-L-methionine
biochanin A + S-adenosyl-L-homocysteine
show the reaction diagram
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-
-
-
?
kaempferol + S-adenosyl-L-methionine
kaempferide + S-adenosyl-L-homocysteine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + 3'-O-methyleriodictyol
S-adenosyl-L-homocysteine + 3',4'-O-dimethyleriodictyol
show the reaction diagram
S-adenosyl-L-methionine + apigenin
S-adenosyl-L-homocysteine + acacetin
show the reaction diagram
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36% of the activity relative to naringenin. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
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?
S-adenosyl-L-methionine + chrysoeriol
S-adenosyl-L-homocysteine + 4'-O-methylchrysoeriol
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + daidzein
S-adenosyl-L-homocysteine + formononetin
show the reaction diagram
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90% of the activity relative to naringenin. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
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-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + 4'-O-methyleriodictyol
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + biochanin A
show the reaction diagram
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62% of the activity relative to naringenin. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
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?
S-adenosyl-L-methionine + isorhamnetin
S-adenosyl-L-homocysteine + 4'-O-methylisorhamnetin
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + kaempferol
S-adenosyl-L-homocysteine + 4'-O-methylkaempferol
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + naringenin
S-adenosyl-L-homocysteine + ponciretin
show the reaction diagram
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 4'-methylquercetin
show the reaction diagram
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Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
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?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 4'-O-methylquercetin
show the reaction diagram
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?
additional information
?
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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 + 3'-O-methyleriodictyol
S-adenosyl-L-homocysteine + 3',4'-O-dimethyleriodictyol
show the reaction diagram
Q6VCW3
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-
-
?
S-adenosyl-L-methionine + naringenin
S-adenosyl-L-homocysteine + ponciretin
show the reaction diagram
C6TAY1
i.e. 4',5,7-trihyroxyflavanone, the enzyme transfers a methyl group to 4'-hydroxyl group of naringenin
i.e. 4'-methoxy-5,7-dihydroxyflavanone
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
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1 mM, 40% residual activity
Mn2+
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1 mM, 79% residual activity
phenylmercuric acetate
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1 mM, 20% residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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activity is increased, in both in vitro and in vivo carnation tissues, by the inoculation with Fusarium oxysporum f. sp. dianthi
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
4'-hydroxyflavanone
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pH 7.0, 25C
0.0033
apigenin
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pH 7.0, 25C
0.0735
genistein
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pH 7.0, 25C
0.0017
kaempferol
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pH 7.0, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19590
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pH 7.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000 - 45000
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gel filtration and PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 40000, SDS-PAGE
monomer
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1 * 43000-45000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, two weeks, about 50% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged OMT6 in Escherichia coli by nickel affinity chromatgraphy
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression of Oryza sativa ROMT-9, which methylates specifically at the 3'-hydroxyl group of quercetin and SOMT-2, which methylates at the 4'-hydroxyl group, in Escherichia coli
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DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli, functional coexpression of plant enzymes, e.g. 4-coumaroyl-CoA ligase and chalcone synthase, of different origins catalyzing steps in flavonoid biosynthesis pathways for production of naringenin from p-coumaric acid and synthesis of ponciretin and sakuranetin from naringenin in engineered and transformed Escherichia coli strain BL21(DE3)
expressed in Escherichia coli as a glutathione S-transferase fusion protein. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
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gene CrOMT6, DNA and amino acid sequence determination and analysis, qualitative RT-PCR expression analysis, sequence comparison and phylogenetic tree, expression of His-tagged OMT6 in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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coexpression of Oryza sativa ROMT-9, which methylates specifically at the 3'-hydroxyl group of quercetin and SOMT-2, which methylates at the 4'-hydroxyl group, in Escherichia coli. Reaction products of quercetin with the transformant show two methylation products that correspond to the 3'-methylated and the 3',4'-dimethylated quercetin. More than 90% of quercetin is converted into the 3',4'-dimethylated quercetin after 24 h incubation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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coexpression of Oryza sativa ROMT-9, which methylates specifically at the 3'-hydroxyl group of quercetin and SOMT-2, which methylates at the 4'-hydroxyl group, in Escherichia coli. Reaction products of quercetin with the transformant show two methylation products that correspond to the 3'-methylated and the 3',4'-dimethylated quercetin. More than 90% of quercetin is converted into the 3',4'-dimethylated quercetin after 24 h incubation