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EC Tree
IUBMB Comments 3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but more slowly.
The taxonomic range for the selected organisms is: Arabidopsis thaliana The enzyme appears in selected viruses and cellular organisms
Synonyms
caffeic acid o-methyltransferase, bmr12, atomt1, caffeate o-methyltransferase, oscomt1, caffeic acid o-methyltransferase 1, caffeate 3-o-methyltransferase, caffeic acid/5-hydroxyferulic acid 3/5-o-methyltransferase, fgcomt1, o-methytransferase,
more
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caffeic acid O-methyltransferase
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caffeate 3-O-methyltransferase
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caffeate methyltransferase
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caffeic acid O-methyl-transferase
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S-adenosyl-L-methionine:caffeic acid-O-methyltransferase
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methyl group transfer
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S-adenosyl-L-methionine:3,4-dihydroxy-trans-cinnamate 3-O-methyltransferase
3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but more slowly.
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S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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?
S-adenosyl-L-methionine + 5-hydroxyconiferyl alcohol
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S-adenosyl-L-methionine + 5-hydroxyconiferyl aldehyde
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S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
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?
S-adenosyl-L-methionine + caffeic acid
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S-adenosyl-L-methionine + caffeoyl alcohol
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S-adenosyl-L-methionine + caffeoyl aldehyde
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?
S-adenosyl-L-methionine + quercetin
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additional information
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additional information
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enzyme additionally shows flavone 3'-O-methyltransferase activity, reaction of EC 2.1.1.42, and N-acetylserotonin methyltransferase activity, reaction of EC 2.1.1.4. 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
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additional information
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enzyme additionally shows flavone 3'-O-methyltransferase activity, reaction of EC 2.1.1.42, and N-acetylserotonin methyltransferase activity, reaction of EC 2.1.1.4. 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
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0.26 - 0.74
N-acetylserotonin
0.0316
5-hydroxyconiferyl alcohol
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pH 7.5, temperature not specified in the publication
0.0179
5-hydroxyconiferyl aldehyde
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pH 7.5, temperature not specified in the publication
0.032
5-hydroxyferulic acid
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pH 7.5, temperature not specified in the publication
0.0242
caffeic acid
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pH 7.5, temperature not specified in the publication
0.0515
caffeoyl alcohol
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pH 7.5, temperature not specified in the publication
0.0197
caffeoyl aldehyde
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pH 7.5, temperature not specified in the publication
0.0237
quercetin
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pH 7.5, temperature not specified in the publication
0.26
N-acetylserotonin
mutant enzyme C296F/Q310L/V314T, at pH 7.8 and 37°C
0.36
N-acetylserotonin
mutant enzyme Q310L, at pH 7.8 and 37°C
0.58
N-acetylserotonin
mutant enzyme C296F, at pH 7.8 and 37°C
0.58
N-acetylserotonin
mutant enzyme V314T, at pH 7.8 and 37°C
0.74
N-acetylserotonin
wild type enzyme, at pH 7.8 and 37°C
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2.94 - 43.79
N-acetylserotonin
2.23
5-hydroxyconiferyl alcohol
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pH 7.5, temperature not specified in the publication
2.85
5-hydroxyconiferyl aldehyde
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pH 7.5, temperature not specified in the publication
1.3
5-hydroxyferulic acid
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pH 7.5, temperature not specified in the publication
0.62
caffeic acid
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pH 7.5, temperature not specified in the publication
1.52
caffeoyl alcohol
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pH 7.5, temperature not specified in the publication
1.55
caffeoyl aldehyde
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pH 7.5, temperature not specified in the publication
0.16
quercetin
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pH 7.5, temperature not specified in the publication
2.94
N-acetylserotonin
wild type enzyme, at pH 7.8 and 37°C
4.76
N-acetylserotonin
mutant enzyme Q310L, at pH 7.8 and 37°C
5.41
N-acetylserotonin
mutant enzyme C296F, at pH 7.8 and 37°C
11.32
N-acetylserotonin
mutant enzyme V314T, at pH 7.8 and 37°C
43.79
N-acetylserotonin
mutant enzyme C296F/Q310L/V314T, at pH 7.8 and 37°C
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3990 - 171060
N-acetylserotonin
3990
N-acetylserotonin
wild type enzyme, at pH 7.8 and 37°C
9370
N-acetylserotonin
mutant enzyme C296F, at pH 7.8 and 37°C
13110
N-acetylserotonin
mutant enzyme Q310L, at pH 7.8 and 37°C
19530
N-acetylserotonin
mutant enzyme V314T, at pH 7.8 and 37°C
171060
N-acetylserotonin
mutant enzyme C296F/Q310L/V314T, at pH 7.8 and 37°C
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0.00609
wild type enzyme, at pH 7.8 and 37°C
0.00945
mutant enzyme V314N, at pH 7.8 and 37°C
0.00982
mutant enzyme C296F, at pH 7.8 and 37°C
0.01109
mutant enzyme C296Y, at pH 7.8 and 37°C
0.01131
mutant enzyme Q310L, at pH 7.8 and 37°C
0.01697
mutant enzyme V314T, at pH 7.8 and 37°C
0.01985
mutant enzyme C296H, at pH 7.8 and 37°C
0.02186
mutant enzyme C296H/Q310L, at pH 7.8 and 37°C
0.02701
mutant enzyme C296F/Q310L, at pH 7.8 and 37°C
0.03342
mutant enzyme Q310L/V314T, at pH 7.8 and 37°C
0.03462
mutant enzyme C296A/V314T, at pH 7.8 and 37°C
0.03913
mutant enzyme C296H/Q310L/V314T, at pH 7.8 and 37°C
0.04694
mutant enzyme C296Y/Q310L/V314T, at pH 7.8 and 37°C
0.05787
mutant enzyme C296F/Q310L/V314T, at pH 7.8 and 37°C
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SwissProt
brenda
additionally shows flavone 3'-O-methyltransferase activity, reaction of EC 2.1.1.42, and N-acetylserotonin methyltransferase activity, reaction of EC 2.1.1.4
SwissProt
brenda
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is induced in wounded vascular tissues
brenda
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COMT1 is not localized in the tapetum, but in two directly adjacent cells layers, the endothecium and the epidermal layer of stamens
brenda
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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
malfunction
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Arabidopsis COMT1 knockout mutant line Atomt1 lignin differs from native lignin in wild type plants, in terms of sinapyl (S) alcohol-derived substructures in fiber cell walls being substituted by 5-hydroxyconiferyl alcohol (5OHG)-derived moieties
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OMT1_ARATH
363
0
39618
Swiss-Prot
other Location (Reliability: 3 )
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C296F
the mutant shows slight activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296F/Q310L
the mutant shows about 4.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296F/Q310L/V314T
the mutant shows 9.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296H
the mutant shows about 3fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296H/Q310L
the mutant shows about 3.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296H/Q310L/V314T
the mutant shows about 6.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296Y
the mutant shows about 2fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296Y/Q310L/V314T
the mutant shows about 8fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296Y/V314T
the mutant shows about 5.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
Q310L
the mutant shows about 2fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
Q310L/V314T
the mutant shows about 5.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
V314N
the mutant shows slight activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
V314T
the mutant shows about 2.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
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HisTrap column chromatography
using affinity chromatography
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using Ni-NTA chromatography
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli
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recombinantly expressed as a His-tagged fusion protein
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additional information
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transgenic Arabidopsis thaliana plants over-expressing the maize R2R3-MYB transcription factors ZmMYB31 and ZmMYB42 down-regulate both the Arabidopsis thaliana and the maize COMT genes, associated with lignin biosynthesis repression
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Fornale, S.; Sonbol, F.M.; Maes, T.; Capellades, M.; Puigdomenech, P.; Rigau, J.; Caparros-Ruiz, D.
Down-regulation of the maize and Arabidopsis thaliana caffeic acid O-methyl-transferase genes by two new maize R2R3-MYB transcription factors
Plant Mol. Biol.
62
809-823
2006
Arabidopsis thaliana, Zea mays
brenda
Moinuddin, S.G.; Jourdes, M.; Laskar, D.D.; Ki, C.; Cardenas, C.L.; Kim, K.W.; Zhang, D.; Davin, L.B.; Lewis, N.G.
Insights into lignin primary structure and deconstruction from Arabidopsis thaliana COMT (caffeic acid O-methyl transferase) mutant Atomt1
Org. Biomol. Chem.
8
3928-3946
2010
Arabidopsis thaliana
brenda
Fellenberg, C.; van Ohlen, M.; Handrick, V.; Vogt, T.
The role of CCoAOMT1 and COMT1 in Arabidopsis anthers
Planta
236
51-61
2012
Arabidopsis thaliana
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), Arabidopsis thaliana
brenda
Wang, W.; Su, S.; Wang, S.; Ye, L.; Yu, H.
Significantly improved catalytic efficiency of caffeic acid O-methyltransferase towards N-acetylserotonin by strengthening its interactions with the unnatural substrates terminal structure
Enzyme Microb. Technol.
125
1-5
2019
Arabidopsis thaliana (Q9FK25), Arabidopsis thaliana
brenda