Information on EC 2.1.1.155 - kaempferol 4'-O-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.155
-
RECOMMENDED NAME
GeneOntology No.
kaempferol 4'-O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + kaempferol = S-adenosyl-L-homocysteine + kaempferide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transfer of methyl group
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Flavone and flavonol biosynthesis
-
-
kaempferide triglycoside biosynthesis
-
-
polymethylated kaempferol biosynthesis
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-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:kaempferol 4'-O-methyltransferase
The enzyme acts on the hydroxy group in the 4'-position of some flavones, flavanones and isoflavones. Kaempferol, apigenin and kaempferol triglucoside are substrates, as is genistein, which reacts more slowly. Compounds with an hydroxy group in the 3' and 4' positions, such as quercetin and eriodictyol, do not act as substrates. Similar to EC 2.1.1.75, apigenin 4'-O-methyltransferase and EC 2.1.1.83, 3,7-dimethylquercetin 4'-O-methyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
118251-36-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
line CP3a
-
-
Manually annotated by BRENDA team
cv. Novada
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
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 + 4'-hydroxyflavanone
S-adenosyl-L-homocysteine + 4'-methoxyflavanone
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + a flavonoid
S-adenosyl-L-homocysteine + a 4'-methoxyflavonoid
show the reaction diagram
S-adenosyl-L-methionine + apigenin
S-adenosyl-L-homocysteine + acacetin
show the reaction diagram
-
-
4’-methoxyapigenin
-
?
S-adenosyl-L-methionine + chrysoeriol
S-adenosyl-L-homocysteine + 4'-methoxychrysoeriol
show the reaction diagram
-
good substrate
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + 4'-methoxyeriodictyol
show the reaction diagram
-
lower activity than with homoeriodictyol, isorhamnetin or chrysoeriol
-
-
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + biochanin A
show the reaction diagram
-
-
4’-methoxygenistein
-
?
S-adenosyl-L-methionine + homoeriodictyol
S-adenosyl-L-homocysteine + 4'-methoxyhomoeriodictyol
show the reaction diagram
-
best substrate
-
-
?
S-adenosyl-L-methionine + isorhamnetin
S-adenosyl-L-homocysteine + 4'-methoxyisorhamnetin
show the reaction diagram
-
good substrate
-
-
?
S-adenosyl-L-methionine + kaempferol
S-adenosyl-L-homocysteine + kaempferide
show the reaction diagram
S-adenosyl-L-methionine + kaempferol 3-O-beta-D-glucopyranosyl-1,4-O-alpha-L-rhamnopyranosyl-1,2-beta-D-glucopyranoside
S-adenosyl-L-homocysteine + 4'-O-methylkaempferol 3-O-beta-D-glucopyranosyl-1,4-O-alpha-L-rhamnopyranosyl-1,2-beta-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 4'-methoxyquercetin
show the reaction diagram
-
lower activity than with homoeriodictyol, isorhamnetin or chrysoeriol
-
-
?
additional information
?
-
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
additional information
?
-
-
the role of F 4’-OMT is mainly defensive against parasites, rather than structural
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no divalent metal ion requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
10 mM, 19% inhibition
iodoacetamide
-
1 mM, 60% inhibition
Mg2+
-
10 mM, 27% inhibition
Mn2+
-
1 mM: 21% inhibition, 10 mM: 57% inhibition
Phenylmercuriacetate
-
1 mM, 80% inhibition
S-adenosyl-L-homocysteine
-
competitive, inhibition kinetics
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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
-
pH 7, 25°C
0.0033
apigenin
-
pH 7, 25°C
0.0735
genistein
-
pH 7, 25°C
0.0017
kaempferol
-
pH 7, 25°C
additional information
additional information
-
kinetic mechanism
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
S-adenosyl-L-homocysteine
-
pH 7, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70.5
-
pH 7, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
50% of maximum activity at pH 5.5 and 8.5, 4% of maximum activity at pH 5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000 - 45000
-
gel filtration, native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
50% of maximum activity at pH 5.5 and 8.5, 4% of maximum activity at pH 5
655462
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 2 weeks, 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CrOMT6 gene, expression in Escherichia coli, gene structure
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