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Information on EC 2.1.1.104 - caffeoyl-CoA O-methyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession O49499
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EC Tree
2.1.1.104 caffeoyl-CoA O-methyltransferaseSpecify your search results
Word Map
- 2.1.1.104
- lignin
- flavonoid
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o-methylation
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phenylpropanoids
- polyketide
- xylem
- monolignols
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ferulic
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lignification
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syringyl
- poplar
-
guaiacyl
-
ammonia-lyase
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sam-dependent
- s-adenosyl-l-homocysteine
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s-adenosyl-l-methionine-dependent
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cinnamyl
-
coniferyl
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5-hydroxylase
- allata
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d-aspartyl
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s-adenosylmethionine-dependent
- 4-coumarate
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l-isoaspartyl
-
feruloyl
- feruloyl-coa
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sinapyl
- aspen
- orcinol
-
4-coumarate:coa
-
2.1.1.6
- cinnamoyl-coa
-
hydroxycinnamoyl
- medicine
- agriculture
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
o-methyltransferase, ccoaomt, ccoaomt1, caffeic acid 3-o-methyltransferase, caffeoyl-coa o-methyltransferase, ccomt, ccoaomt2, ccoaomt-like, caffeoyl coa 3-o-methyltransferase, caffeoyl-coa 3-o-methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
caffeoyl coenzyme A methyltransferase
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-
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caffeoyl-CoA 3-O-methyltransferase
CCoAOMT
trans-caffeoyl-CoA 3-O-methyltransferase
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-
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caffeoyl-CoA 3-O-methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:caffeoyl-CoA 3-O-methyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
120433-42-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
10% of the activity with luteolin
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl CoA
33% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + ?
2.5% of the activity with luteolin
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-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + eriodictoyl-3'-O-methylether + eriodictoyl-4'-O-methylether
15% of the activity with luteolin
80% para product versus 20% meta in the wild type
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
20% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
60% of the activity with luteolin
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme predicted to catalyze first methylation step during biosynthesis of monolignols
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-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme responsible for the first methylation step during biosynthesis of monolignols
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-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
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-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
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-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
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-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
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synthesis of a single meta-methylated product
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?
additional information
?
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enzyme shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta-position
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?
additional information
?
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enzyme shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta-position
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?
additional information
?
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enzyme CCoAOMT7 binds to S-adenosyl-L-homocysteine hydrolase (SAHH) and S-adenosyl-L-methionine synthases (SAMSs) in vivo
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additional information
?
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CCoAOMT7 in Arabidopsis thaliana shows a strong preference to methylate para-position of flavanones and dihydroflavonols, and also a relatively lower activity on caffeoyl-CoA using S-adenosyl-L-methionine (SAM or AdoMet) as methyl donor to produce feruloyl-CoA. CCoAOMT7 also shows methyltransferase activity on caffeoyl CoA, although it shows the highest activity on luteolin, a kind of flavonoids
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme predicted to catalyze first methylation step during biosynthesis of monolignols
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-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
-
-
?
additional information
?
-
enzyme CCoAOMT7 binds to S-adenosyl-L-homocysteine hydrolase (SAHH) and S-adenosyl-L-methionine synthases (SAMSs) in vivo
-
-
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S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
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-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
T-DNA null mutant indicates collapsed xylem elements under short-day conditions, lignin composition of p-hydroxyphenyl units and inability of sinapoyl malate synthesis in double mutants impaired in caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), C3 methylation of the phenolic ring of monolignols in Arabidopsis mediated by both, caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), both enzymes also involved in formation of sinapoyl malate and isorhamnetin
additional information
-
T-DNA null mutant indicates collapsed xylem elements under short-day conditions, lignin composition of p-hydroxyphenyl units and inability of sinapoyl malate synthesis in double mutants impaired in caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), C3 methylation of the phenolic ring of monolignols in Arabidopsis mediated by both, caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1), both enzymes also involved in formation of sinapoyl malate and isorhamnetin
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
At4g34050; ecotypes Columbia (Col-0) and Wassilewskija (WS)
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is highly expressed in stem, especially in the top portion of 6-week-old stem where lignification is occurring
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
ferulate is methylated from caffeoyl-CoA using S-adenosyl-L-methionine (SAM) as methyl donor catalyzed by caffeoyl CoA methyltransferase (CCoAOMT). Arabidopsis thaliana CCoAOMT7 contributes to ferulate content in the stem cell wall. CCoAOMT7 further binds to S-adenosyl-L-homocysteine hydrolase (SAHH), a critical step in SAM synthesis to release feedback suppression on CCoAOMT. CCoAOMT7 also binds S-adenosyl-L-methionine synthases (SAMSs) in vivo, which is mediated by SAHH1. Enzyme CCoAOMT7 is required for cell wall-bound ferulic esters
malfunction
interruptions of endogenous SAHH1 by artificial miRNA or SAMSs by T-DNA insertion significantly reduce ferulate contents in the stem cell wall
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). CAMT4_ARATH
259
0
29155
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G46Y
mutation is sufficient for a reversal of the unusual para- back to meta-O-methylation of flavanones and dihydroflavonols
G46Y/W193F/R194M/I195K
methylation in meta-position is preferred, mutations reduce the affinity for eriodictyol due to almost no interactions of the side chains with the substrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, pGEM-T easy vector, pCAMBIA1391xb vector, transgenic plants produced, promoter-GUS fusion constructs, T-DNA null mutant of GABI T-DNA insertion collection identified and characterized, double mutants lacking caffeoyl CoA 3-O-methyltransferase (CCoAOMT 1) and caffeic acid O-methyltransferase (COMT 1)
gene At4g26220, recombinant expression of the enzyme in yeast cells, coexpression with enzymes S-adenosyl-L-methionine synthase (SAMS)1, SAMS2, SAMS3, SAMS4, methionine synthase (MS)1, MS2, S-adenosyl-L-homocysteine hydrolase (SAHH)1, and SAHH2 for the yeast two-hybrid interaction analysis, overview. Quantitative real-time reverse transcript-PCR expression analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Do, C.T.; Pollet, B.; Thevenin, J.; Sibout, R.; Denoue, D.; Barriere, Y.; Lapierre, C.; Jouanin, L.
Both caffeoyl Coenzyme A 3-O-methyltransferase 1 and caffeic acid O-methyltransferase 1 are involved in redundant functions for lignin, flavonoids and sinapoyl malate biosynthesis in Arabidopsis
Planta
226
1117-1129
2007
Arabidopsis thaliana (O49499), Arabidopsis thaliana
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 (O49499)
Wils, C.R.; Brandt, W.; Manke, K.; Vogt, T.
A single amino acid determines position specificity of an Arabidopsis thaliana CCoAOMT-like O-methyltransferase
FEBS Lett.
587
683-689
2013
Arabidopsis thaliana (Q9C5D7), Arabidopsis thaliana
Yang, S.; Wu, T.; Ding, C.; Zhou, P.; Chen, Z.; Gou, J.
SAHH and SAMS form a methyl donor complex with CCoAOMT7 for methylation of phenolic compounds
Biochem. Biophys. Res. Commun.
520
122-127
2019
Arabidopsis thaliana (Q9C5D7), Arabidopsis thaliana Col-0 (Q9C5D7)
Xie, H.; Engle, N.L.; Venketachalam, S.; Yoo, C.G.; Barros, J.; Lecoultre, M.; Howard, N.; Li, G.; Sun, L.; Srivastava, A.C.; Pattathil, S.; Pu, Y.; Hahn, M.G.; Ragauskas, A.J.; Nelson, R.S.; Dixon, R.A.; Tschaplinski, T.J.; Blancaflor, E.B.; Tang, Y.
Combining loss of function of folylpolyglutamate synthetase1 and caffeoyl-CoA 3-O-methyltransferase1 for lignin reduction and improved saccharification efficiency in Arabidopsis thaliana
Biotechnol. Biofuels
12
108
2019
Arabidopsis thaliana
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