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Information on EC 2.1.1.68 - caffeate O-methyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FK25

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.68 caffeate O-methyltransferase
IUBMB Comments
3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but more slowly.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9FK25
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Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
caffeic acid O-methyltransferase
-
caffeate 3-O-methyltransferase
-
-
-
-
caffeate methyltransferase
-
-
-
-
caffeic acid O-methyl-transferase
-
-
S-adenosyl-L-methionine:caffeic acid-O-methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3,4-dihydroxy-trans-cinnamate 3-O-methyltransferase
3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
50936-45-3
-
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 + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferyl alcohol
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferyl aldehyde
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26 - 0.74
N-acetylserotonin
0.0316
5-hydroxyconiferyl alcohol
-
pH 7.5, temperature not specified in the publication
0.0179
5-hydroxyconiferyl aldehyde
-
pH 7.5, temperature not specified in the publication
0.032
5-hydroxyferulic acid
-
pH 7.5, temperature not specified in the publication
0.0242
caffeic acid
-
pH 7.5, temperature not specified in the publication
0.0515
caffeoyl alcohol
-
pH 7.5, temperature not specified in the publication
0.0197
caffeoyl aldehyde
-
pH 7.5, temperature not specified in the publication
0.0237
quercetin
-
pH 7.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.94 - 43.79
N-acetylserotonin
2.23
5-hydroxyconiferyl alcohol
-
pH 7.5, temperature not specified in the publication
2.85
5-hydroxyconiferyl aldehyde
-
pH 7.5, temperature not specified in the publication
1.3
5-hydroxyferulic acid
-
pH 7.5, temperature not specified in the publication
0.62
caffeic acid
-
pH 7.5, temperature not specified in the publication
1.52
caffeoyl alcohol
-
pH 7.5, temperature not specified in the publication
1.55
caffeoyl aldehyde
-
pH 7.5, temperature not specified in the publication
0.16
quercetin
-
pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3990 - 171060
N-acetylserotonin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
is induced in wounded vascular tissues
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OMT1_ARATH
363
0
39618
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
Western blot
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
using affinity chromatography
-
using Ni-NTA chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team