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Information on EC 2.1.1.42 - flavone 3'-O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.42
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.42 flavone 3'-O-methyltransferase
IUBMB Comments
The enzyme prefers flavones with vicinal 3′,4′-dihydroxyl groups.
The enzyme appears in viruses and cellular organisms
- 2.1.1.42
-
phenylpropanoids
- lignin
- populus
-
bispecific
-
cinnamic
-
guaiacyl
-
5-hydroxylase
- aspen
- tremuloides
Reaction Schemes
showSynonyms
3'-o-methyltransferase, caffeic acid/5-hydroxyferulic acid o-methyltransferase, somt-9, flavone 3'-o-methyltransferase, zmomt1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
luteolin 3'-O-methyltransferase
-
-
-
-
luteolin methyltransferase
-
-
-
-
o-dihydric phenol meta-O-methyltransferase
-
-
-
-
o-dihydric phenol methyltransferase
-
-
-
-
o-diphenol m-O-methyltransferase
-
-
-
-
S-adenosylmethionine:flavone/flavonol 3'-O-methyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3'-hydroxyflavone = S-adenosyl-L-homocysteine + 3'-methoxyflavone
also acts on luteolin 7-O-beta-D-glucoside
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
chrysoeriol biosynthesis, methylquercetin biosynthesis, phenylpropanoids methylation (ice plant), polymethylated quercetin biosynthesis, quercetin sulfate biosynthesis, tricin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3'-hydroxyflavone 3'-O-methyltransferase
The enzyme prefers flavones with vicinal 3',4'-dihydroxyl groups.
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CAS REGISTRY NUMBER
COMMENTARY
37205-55-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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-tetra-O-methyl-quercetin
Substrates: -
Products: -
Products: -
?
luteolin + S-adenosyl-L-methionine
3'-O-methyl luteolin + S-adenosyl-L-homocysteine
-
Substrates: high 3'-O-methyltransferase activity
Products: i.e. chrysoeriol
Products: i.e. chrysoeriol
?
luteolin + S-adenosyl-L-methionine
3'-O-methylluteolin + S-adenosyl-L-homocysteine
-
Substrates: OMT-15 shows 92% activity and OMT-17 shows 84% activity compared to myricetin
Products: -
Products: -
?
S-adenosyl-L-homocysteine + 6,7-dihydroxy-3'-methoxyisoflavone
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + (-)-epicatechin
S-adenosyl-L-homocysteine + ?
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + (2S)-naringenin
S-adenosyl-L-homocysteine + ?
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-2,3-dihydro-4H-chromen-4-one
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3,3',4',5,5',7-hexahydroxyflavone
S-adenosyl-L-homocysteine + 3,4',5,5',7-pentahydroxy-3'-methoxyflavone
Substrates: i.e. mycricetin. 70% of the activity with quercetin
Products: -
Products: -
?
S-adenosyl-L-methionine + 3,3',4',5,7-pentahydroxy flavone
S-adenosyl-L-homocysteine + isorhamnetin
S-adenosyl-L-methionine + 3,3',4',5,7-pentahydroxyflavone
S-adenosyl-L-homocysteine + 3,4',5,7-tetrahydroxy-3'-methoxyflavone
Substrates: i.e. quercetin. Preferred substrate
Products: i.e. isorhamnetin
Products: i.e. isorhamnetin
?
S-adenosyl-L-methionine + 4,5-dihydroxy-3-methoxycinnamate
S-adenosyl-L-homocysteine + 4-hydroxy-3,5-dimethoxycinnamate
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavanone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavanone
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 3'-O-methylluteolin
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
S-adenosyl-L-methionine + 5,7,3'-trihydroxyflavone
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3'-trihydroxyflavone 7-O-glucoside
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone 7-O-glucoside
S-adenosyl-L-methionine + 5-hydroxyferulic acid
?
-
Substrates: OMT-15 shows 25% activity and OMT-17 shows 18% activity compared to myricetin
Products: -
Products: -
?
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
?
-
Substrates: OMT-15 shows 102% activity and OMT-17 shows 143% activity compared to myricetin
Products: -
Products: -
?
S-adenosyl-L-methionine + dihydro-3,3',4',5,7-pentahydroxy flavone
S-adenosyl-L-homocysteine + dihydroisorhamnetin
S-adenosyl-L-methionine + equol
S-adenosyl-L-homocysteine + ?
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + chrysoeriol
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 3'-O-methylquercetin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + quercetin 3-O-glucoside
S-adenosyl-L-homocysteine + ?
-
Substrates: poor substrate
Products: -
Products: -
?
S-adenosyl-L-methionine + rutin
S-adenosyl-L-homocysteine + ?
-
Substrates: poor substrate
Products: -
Products: -
?
taxifolin + S-adenosyl-L-methionine
3'-O-methyl taxifolin + S-adenosyl-L-homocysteine
-
Substrates: 3'-O-methyltransferase activity
Products: -
Products: -
?
quercetin + S-adenosyl-L-methionine
3'-O-methylquercetin + S-adenosyl-L-homocysteine
-
Substrates: SOMT-9 is involved in the biosynthesis of isorhamnetin
Products: -
Products: -
?
quercetin + S-adenosyl-L-methionine
3'-O-methylquercetin + S-adenosyl-L-homocysteine
-
Substrates: a flavone, 3'-O-methyltransferase activity, best substrate
Products: i.e. isorhamnetin
Products: i.e. isorhamnetin
?
S-adenosyl-L-methionine + 3,3',4',5,7-pentahydroxy flavone
S-adenosyl-L-homocysteine + isorhamnetin
-
Substrates: quercetin
Products: -
Products: -
?
S-adenosyl-L-methionine + 3,3',4',5,7-pentahydroxy flavone
S-adenosyl-L-homocysteine + isorhamnetin
-
Substrates: quercetin
Products: -
Products: -
?
S-adenosyl-L-methionine + 4,5-dihydroxy-3-methoxycinnamate
S-adenosyl-L-homocysteine + 4-hydroxy-3,5-dimethoxycinnamate
-
Substrates: 5-hydroxy ferulic acid
Products: -
Products: -
?
S-adenosyl-L-methionine + 4,5-dihydroxy-3-methoxycinnamate
S-adenosyl-L-homocysteine + 4-hydroxy-3,5-dimethoxycinnamate
-
Substrates: 5-hydroxy ferulic acid
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavanone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavanone
-
Substrates: eriodictyol
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavanone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavanone
-
Substrates: eriodictyol
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 3'-O-methylluteolin
-
Substrates: i.e. luteolin, the enzyme also catalyzes the methylation of tricetin and the methylation of quercetin, prefers tricetin over luteolin
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 3'-O-methylluteolin
-
Substrates: i.e. lutepolin, the enzyme also catalyzes the methylation of tricetin and the methylation of 5-hydroxyferulic acid and quercetin, prefers tricetin over luteolin
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
Substrates: i.e. luteolin. 15% of the activity with quercetin
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
-
Substrates: luteolin
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
-
Substrates: luteolin
Products: chrysoeriol
Products: chrysoeriol
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
-
Substrates: luteolin
Products: -
Products: -
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
-
Substrates: luteolin, enzyme directly related to flavone glycoside biosynthesis, biosynthesis of 3'-methoxyflavonoids
Products: chrysoeriol
Products: chrysoeriol
?
S-adenosyl-L-methionine + 5,7,3'-trihydroxyflavone 7-O-glucoside
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone 7-O-glucoside
-
Substrates: -
Products: chrysoeriol-7-O-glucoside
Products: chrysoeriol-7-O-glucoside
?
S-adenosyl-L-methionine + 5,7,3'-trihydroxyflavone 7-O-glucoside
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone 7-O-glucoside
-
Substrates: -
Products: chrysoeriol-7-O-glucoside
Products: chrysoeriol-7-O-glucoside
?
S-adenosyl-L-methionine + 5,7,3'-trihydroxyflavone 7-O-glucoside
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone 7-O-glucoside
-
Substrates: luteolin 7-O-glucoside
Products: chrysoeriol-7-O-glucoside
Products: chrysoeriol-7-O-glucoside
?
S-adenosyl-L-methionine + dihydro-3,3',4',5,7-pentahydroxy flavone
S-adenosyl-L-homocysteine + dihydroisorhamnetin
-
Substrates: dihydroquercetin
Products: -
Products: -
?
S-adenosyl-L-methionine + dihydro-3,3',4',5,7-pentahydroxy flavone
S-adenosyl-L-homocysteine + dihydroisorhamnetin
-
Substrates: dihydroquercetin
Products: -
Products: -
?
additional information
?
-
Substrates: only flavonols with vicinal B-ring hydroxyl groups, such as quercetin and myricetin are good methyl acceptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: only flavonols with vicinal B-ring hydroxyl groups, such as quercetin and myricetin are good methyl acceptor
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme additionally shows N-acetylserotonin methyltransferase activity, reaction of EC 2.1.1.4, and caffeic acid methyltransferase activity, reaction of EC 2.1.1.68. The catalytic efficiency for N-acetylserotonin methyltransferase activity is 709fold lower than for caffeic acid methyltransferase. In vitro, N-acetylserotonin methyltransferase activity is dramatically decreased by the addition of caffeic acid in a dose-dependent manner, but the activity of caffeic acid methyltransferase is not altered by N-acetylserotonin
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows methylation activity for the 3-, 5-, 6-, and 7-hydroxyl groups of flavones. The highest activity is observed for 3-hydroxyflavone (flavonol), followed by 7-hydroxyflavone with a relative activity of 15.6% of that of 3-hydroxyflavone and 5-hydroxyflavone with that of 13.5%. Very weak activity is observed for 6-hydroxyflavone and no activity for 3'- or 4'-hydroxyflavone and 7-methoxy-8-hydroxyflavone. FOMT5 does not exhibit a sequential methylation order for 3-, 5-, and 7-hydroxyl groups of quercetin. No detection of polymethylated products from naringenin, (-)-epicatechin, and equol, and cyanidin is not a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: methylation proceedes only in the meta-position, enzyme is unable to catalyze the methylation of p-coumaric acid, m-coumaric acid, ferulic acid, isoferulic acid, sinapic acid, apigenin and naringenin
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoflavones biochanin A and daidzein do not serve as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: SOMT-9 transfers a methyl group to the 3'-OH group of substrates having ortho-hydroxyl groups and uses a flavonoids as a substrates, no activity with 3,3'-dihydroxyflavone, 5,3'-dihydroxyflavone, 6,3'-dihydroxyflavone, 3'-hydroxyflavone, and 3'-hydroxyflavanone
Products: -
Products: -
?
additional information
?
-
-
Substrates: rutin is no substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: OMT-15 and -17 cannot utilize naringenin, apigenin, or kaempferol as substrates, taxifolin and eriodictyol do not serve as methyl acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: isomeric substances isoferulic acid and diosmetin, chrysoeriol, apigenin p-cumaric acid and ferulic acid are not substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: only ortho-dihydric phenols can function as substrates and only the meta-hydroxyl group is methylated, no reaction takes place if one of the two phenolic hydroxyls is methylated or if only one hydroxyl group is present
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
quercetin + S-adenosyl-L-methionine
3'-O-methylquercetin + S-adenosyl-L-homocysteine
-
Substrates: SOMT-9 is involved in the biosynthesis of isorhamnetin
Products: -
Products: -
?
S-adenosyl-L-methionine + 3,3',4',5,7-pentahydroxyflavone
S-adenosyl-L-homocysteine + 3,4',5,7-tetrahydroxy-3'-methoxyflavone
Substrates: i.e. quercetin. Preferred substrate
Products: i.e. isorhamnetin
Products: i.e. isorhamnetin
?
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone
S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
-
Substrates: luteolin, enzyme directly related to flavone glycoside biosynthesis, biosynthesis of 3'-methoxyflavonoids
Products: chrysoeriol
Products: chrysoeriol
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
Co2+ results in recovery of 82% of OMT-15 and 41% of OMT-17 activity compared to the addition of Mg2+
Mg2+
Mn2+
-
the addition of Mn2+ restores 74% of OMT-15 activity and 69% of OMT-17 compared to the addition of Mg2+
Zn2+
-
Zn2+ results in recovery of less than 10% of OMT-15 and OMT-17 activity compared to the addition of Mg2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
-
inhibits the methylation of luteolin by S-adenosylmethionine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
extractable activity drastically increases by illuminating cells with white light
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Mycoses
The effects of infection by Phytophthora infestans on the control of phenylpropanoid metabolism in wounded potato tissue.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-2,3-dihydro-4H-chromen-4-one
-
-
0.00338
3,3',4',5,5',7-hexahydroxyflavone
i.e. mycricetin, 30°C, pH not specified in the publication
0.00176
3,3',4',5,7-pentahydroxyflavone
i.e. quercetin, 30°C, pH not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
3,3',4',5,5',7-hexahydroxyflavone
i.e. mycricetin, 30°C, pH not specified in the publication
16
3,3',4',5,7-pentahydroxyflavone
i.e. quercetin, 30°C, pH not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
9.6 - 9.8
-
glycine-NaOH buffer with caffeic acid and luteolin as substrates
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
OMT-15 is expressed higher in stem and roots than in other tissues
brenda
-
OMT-17 is expressed in stems only, OMT-15 is expressed higher in stem and roots than in other tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
caffeic acid O-methyltransferase likely evolved from N-acetylserotonin methyltransferase by gene duplication and subsequent divergence. Caffeic acid O-methyltransferase gained a significantly higher N-acetylserotonin methyltransferase activity to produce greater amounts of melatonin for immobile plants to acclimate to the land environments. The caffeic acid O-methyltransferase genes possess more conserved substrate-binding sites at the amino acid level and more open protein conformation compared to N-acetylserotonin methyltransferase genes
physiological function
physiological function
an Arabidopsis thaliana knockout mutant exhibits less production of melatonin than the wild type when leaves are infiltrated with 1 mM N-acetylserotonin
physiological function
COMT is involved in melatonin biosynthesis and significantly delays leaf senescence at the grain filling stage by inhibiting degradation of chlorophyll and chloroplast. Number and size of vascular bundles in the culms and leaves are significantly increased in COMT-overexpressing plants. COMT is a positive regulator of grain yield, and overexpression of COMT increases grain yield per plant even in a high-yield variety background
physiological function
-
COMT1 overexpression improves tomato seed germination under salt stress and significantly increases both melatonin content and salt tolerance. In the stressed overexpression seeds, higher amylase activity is observed than in wild-type
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OMT2_CHRAE
343
0
37868
Swiss-Prot
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
recombinant fusion protein containing a 3 kDa His tail, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
1 * 45000, recombinant fusion protein containing a 3 kDa His tail, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E69L
-
the mutation results in about 14% loss of enzyme activity in OMT-15 and 40% loss of activity in OMT-17
L34Q
mutant shows improved production of chrysoeriol from luteolin due to a higher enzyme expression level
W284A
mutant shows improved production of chrysoeriol from luteolin due to higher efficiency in substrate binding and catalysis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1-3 mg protein/ml in 0.02 M Tris-HCl buffer loses about 30% of its activity after 1 month
-
-20°C, stored in 10% glycerol for 2 months, no singnificant loss in enzyme activity
-
4°C, acetone powder of fresh cells as source of the enzyme can be kept without significant loss of enzyme activity
-
4°C, highly unstable, stored with Triton X-100, bovine serum albumin, ethylene glycol, dimethyl sulfoxide, 2-mercaptoethanol, dithiothreitol or ethylene glycol monoethylether, loses over 90% of its activity within 94 h
-
4°C, stable when stored in buffer containing 10% (v/v) glycerol for 34 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
OMT-15 and OMT-17 are expressed in Escherichia coli BL21(DE3) cells as glutathione S-transferase fusion proteins
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SOMT-9, DNA and amino acid sequence determination, expression of GST-tagged SOMT-9 in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ebel, J.; Hahlbrock, K.; Grisebach, H.
Purification and properties of an o-dihydricphenol meta-O-methyltransferase from cell suspension cultures of parsley and its relation to flavonoid biosynthesis
Biochim. Biophys. Acta
269
313-326
1972
Petroselinum crispum
-
brenda
Ebel, J.; Hahlbrock, K.
Enzymes of flavone and flavonol-glycoside biosynthesis. Coordinated and selective induction in cell-suspension cultures of Petroselinum hortense
Eur. J. Biochem.
75
201-209
1977
Petroselinum crispum
brenda
Poulton, J.E.; Hahlbrock, K.; Grisebach, H.
O-Methylation of flavonoid substrates by a partially purified enzyme from soybean cell suspension cultures
Arch. Biochem. Biophys.
180
543-549
1977
Glycine max, Petroselinum crispum
brenda
Legrand, M.; Fritig, B.; Hirth, L.
O-Diphenol O-methyltransferases of healthy and tobacco-mosaic-virus-infected hypersensitive tobacco
Planta
144
101-108
1978
Nicotiana tabacum
brenda
Muzac, I.; Wang, J.; Anzellotti, D.; Zhang, H.; Ibrahim, R.K.
Functional expression of an Arabidopsis cDNA clone encoding a flavonol 3'-O-methyltransferase and characterization of the gene product
Arch. Biochem. Biophys.
375
385-388
2000
Arabidopsis thaliana (Q9FK25), Arabidopsis thaliana
brenda
Kim, B.G.; Lee, H.J.; Park, Y.; Lim, Y.; Ahn, J.H.
Characterization of an O-methyltransferase from soybean
Plant Physiol. Biochem.
44
236-241
2006
Glycine max
brenda
Lee, Y.; Kim, B.; Chong, Y.; Lim, Y.; Ahn, J.
Cation dependent O-methyltransferases from rice
Planta
227
641-647
2008
Oryza sativa
brenda
Zhou, J.-M.; Fukushi, Y.; Wollenweber, E.; Ibrahim, R.K.
Characterization of two O-methyltransferase-like genes in barley and maize
Pharm. Biol.
46
26-34
2008
Hordeum vulgare, Zea mays
-
brenda
Byeon, Y.; Lee, H.Y.; Lee, K.; Back, K.
Caffeic acid O-methyltransferase is involved in the synthesis of melatonin by methylating N-acetylserotonin in Arabidopsis
J. Pineal Res.
57
219-227
2014
Arabidopsis thaliana (Q9FK25)
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.
16
180
2016
Citrus depressa (A0A125T1T5)
brenda
Wu, X.; Yuwen, M.; Pu, Z.; Zhao, Z.; Yu, H.; Zha, J.
Engineering of flavonoid 3-O-methyltransferase for improved biosynthesis of chrysoeriol in Escherichia coli
Appl. Microbiol. Biotechnol.
107
1663-1672
2023
Oryza sativa Japonica Group (Q6ZD89)
brenda
Ge, L.; Yang, X.; Liu, Y.; Tang, H.; Wang, Q.; Chu, S.; Hu, J.; Zhang, N.; Shi, Q.
Improvement of seed germination under salt stress via overexpressing caffeic acid O-methyltransferase 1 (SlCOMT1) in Solanum lycopersicum L
Int. J. Mol. Sci.
24
734
2023
Solanum lycopersicum
brenda
Zhao, D.; Yao, Z.; Zhang, J.; Zhang, R.; Mou, Z.; Zhang, X.; Li, Z.; Feng, X.; Chen, S.; Reiter, R.J.
Melatonin synthesis genes N-acetylserotonin methyltransferases evolved into caffeic acid O-methyltransferases and both assisted in plant terrestrialization
J. Pineal Res.
71
e12737
2021
Arabidopsis thaliana (Q9FK25)
brenda
Huangfu, L.; Chen, R.; Lu, Y.; Zhang, E.; Miao, J.; Zuo, Z.; Zhao, Y.; Zhu, M.; Zhang, Z.; Li, P.; Xu, Y.; Yao, Y.; Liang, G.; Xu, C.; Zhou, Y.; Yang, Z.
OsCOMT, encoding a caffeic acid O-methyltransferase in melatonin biosynthesis, increases rice grain yield through dual regulation of leaf senescence and vascular development
Plant Biotechnol. J.
20
1122-1139
2022
Oryza sativa Japonica Group (Q6ZD89)
brenda
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