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Information on EC 2.1.1.68 - caffeate O-methyltransferase and Organism(s) Medicago sativa and UniProt Accession P28002
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2.1.1.68 caffeate O-methyltransferaseIUBMB Comments
3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but more slowly.
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Word Map
- 2.1.1.68
-
phenylpropanoids
- monolignols
-
syringyl
-
cinnamyl
-
guaiacyl
-
lignification
-
coniferyl
- ccoaomts
- caffeoyl-coa
-
5-hydroxylase
-
5-hydroxyconiferyl
- n-acetylserotonin
-
sinapyl
-
s-lignin
-
brown-midrib
- 5-hydroxyconiferaldehyde
-
caffeoyl-coenzyme
-
sclerenchyma
- synthesis
The taxonomic range for the selected organisms is: Medicago sativa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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, rsomt1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
caffeate 3-O-methyltransferase
-
-
-
-
caffeate methyltransferase
-
-
-
-
S-adenosyl-L-methionine:caffeic acid-O-methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
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
50936-45-3
-
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 + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferyl alcohol
S-adenosyl-L-homocysteine + 5-hydroxy-3-methoxyconiferyl alcohol
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
-
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + 4-[(1E)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + coniferyl aldehyde
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-methoxy-benzaldehyde
S-adenosyl-L-homocysteine + 4-hydroxy-3,5-dimethoxybenzaldehyde
-
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-hydrocinnamic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxyhydrocinnamic acid
-
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + 5-methoxyconiferaldehyde
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferyl alcohol
S-adenosyl-L-homocysteine + 5-hydroxy-3-methoxyconiferyl alcohol
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-trans-cinnamic acid
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
?
-
alternative pathway to monolignols involving methylation of caffeoyl aldehyde and/or caffeoyl alcohol
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + 4-[(1E)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
?
-
alternative pathway to monolignols involving methylation of caffeoyl aldehyde and/or caffeoyl alcohol
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + coniferyl aldehyde
-
-
-
-
?
S-adenosyl-L-methionine + protocatechuic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxybenzoate
-
poor substrate
-
-
?
S-adenosyl-L-methionine + protocatechuic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxybenzoic acid
-
-
-
-
?
S-adenosyl-L-methionine + protocatechuic aldehyde
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxybenzaldehyde
-
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
i.e. caffeic acid, involved in the biosynthesis of lignin
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
-
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
-
-
i.e. ferulate
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
-
-
i.e. ferulate
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
-
-
i.e. ferulate
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
-
i.e. caffeic acid, involved in the biosynthesis of lignin
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
-
at 70% the rate of caffeic acid methylation
-
-
?
additional information
?
-
in silico studies suggest that alcoholic and aldehydic substrates are preferred to those of caffeic, sinapic, and ferulic acid by both caffeic acid-O-methyltransferase, and caffeoyl-coenzyme A-O-methyltransferase, EC 2.1.1.104, with a marked preference for CoA ester substrates over free acids, aldehydes, and alcohols
-
-
?
additional information
?
-
-
bifunctional enzyme, methylation of 3-hydroxy and 5-hydroxy positions on the aromatic ring
-
-
?
additional information
?
-
-
no activity with 3-hydroxybenzaldehyde, 4-hydroxybenzaldehyde, vanillin and syringaldehyde
-
-
?
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 + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
i.e. caffeic acid, involved in the biosynthesis of lignin
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
-
i.e. caffeic acid, involved in the biosynthesis of lignin
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
?
-
alternative pathway to monolignols involving methylation of caffeoyl aldehyde and/or caffeoyl alcohol
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
?
-
alternative pathway to monolignols involving methylation of caffeoyl aldehyde and/or caffeoyl alcohol
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.4
-
37% of maximal activity at pH 7.0, 75% of maximal activity at pH 7.4
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). COMT1_MEDSA
365
0
39946
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization from polyethylene glycol solution, 2.2 A resolution, complex with S-adenosyl-L-homocysteine and ferulic acid
crystallization from polyethylene glycol solution, 2.4 A resolution, complex with S-adenosyl-L-homocysteine and 5-hydroxyconiferaldehyde
molecular docking of 16 putative substrates (intermediates of monolignol biosynthesis pathway). Both caffeic acid-O-methyltransferase and caffeoyl-coenzyme A-O-methyltransferase, EC 2.1.1.104, interact with all 16 substrates in a similar manner, with thiol esters being the most potent and binding of these putative substrates to caffeoyl-coenzyme A-O-methyltransferase being more efficient
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F172Y
no reaction with caffeic acid, with other substrates same reactivity as wild type
H183K
no reaction with caffeic acid, with other substrates same reactivity as wild type
M130L
no reaction with caffeic acid and 5-hydroxyferulic acid, with other substrates same reactivity as wild type
N324Y
no reaction with caffeic acid, with other substrates same reactivity as wild type
A162T
-
2fold increase in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.9fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 1.8fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 2.8fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity against protocatechuic acid
F172Y
-
3fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 34fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 2.3fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity with caffeic acid and protocatechuic acid
H183K
-
19fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 1.8fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, no activity with protocatechuic aldehyde, 3,4-dihydroxy-5-methoxybenzaldehyde and protocatechuic acid
L136Y
-
1.5 fold increase in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 4.8fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 1.7fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 3.9fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, 176fold decrease in ratio of Vmax to Km-value for protocatechuic acid compared to wild-type enzyme
M130L
-
3.1fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 51fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 5.8fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme,no activity with caffeic acid and protocatechuic acid
N131D
-
9.5fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.4fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, no activity with protocatechuic aldehyde, 3,4-dihydroxy-5-methoxybenzaldehyde and protocatechuic acid
N131E
-
475fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 1.7fold increase in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, no activity with protocatechuic aldehyde, 3,4-dihydroxy-5-methoxybenzaldehyde and protocatechuic acid
N131K
-
3.2 fold increase in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.9fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 1.7fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 2.8fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, 3.3fold decrease in ratio of Vmax to Km-value for protocatechuic acid compared to wild-type enzyme
N131L
-
23.8fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.5fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 5.7fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 1.5fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity with protocatechuic acid
N324H/M130L
-
2.4fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 4.2fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 2.8fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 3.1fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, 6.7fold decrease in ratio of Vmax to Km-value for protocatechuic acid compared to wild-type enzyme
N324Y
-
31.7fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.4fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 10.2fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 1.7fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity with protocatechuic acid
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
engineered COMT enzymes can be useful for metabolic engineering of both lignin and benzaldehyde-derived flavors and fragances
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Parvathi, K.; Chen, F.; Guo, D.; Blount, J.W.; Dixon, R.A.
Substrate preferences of O-methyltransferases in alfalfa suggest new pathways for 3-O-methylation of monolignols
Plant J.
25
193-202
2001
Medicago sativa
Eckardt, N.A.
Probing the mysteries of lignin biosynthesis: The crystal structure of caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase provides new insights
Plant Cell
14
1185-1189
2002
Medicago sativa
Zubieta, C.; Kota, P.; Ferrer, J.L.; Dixon, R.A.; Noel, J.P.
Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase
Plant Cell
14
1265-1277
2002
Medicago sativa (P28002), Medicago sativa
Edwards, R.; Dixon, R.A.
Purification and characterization of S-adenosyl-L-methionine: caffeic acid 3-O-methyltransferase from suspension cultures of alfalfa (Medicago sativa L.)
Arch. Biochem. Biophys.
287
372-379
1991
Medicago sativa
Vance, C.P.; Bryan, J.W.
Purification and properties of caffeic acid O-methyltransferase from alfalfa root nodules
Phytochemistry
20
41-43
1981
Medicago sativa, Medicago sativa Saranac
-
Kota, P.; Guo, D.; Zubieta, C.; Noel, J.; Dixon, R.A.
O-Methylation of benzaldehyde derivatives by "lignin specific" caffeic acid 3-O-methyltransferase
Phytochemistry
65
837-846
2004
Medicago sativa
Naaz, H.; Pandey, V.P.; Singh, S.; Dwivedi, U.N.
Structure-function analyses and molecular modeling of caffeic acid-O-methyltransferase and caffeoyl-CoA-O-methyltransferase: revisiting the basis of alternate methylation pathways during monolignol biosynthesis
Biotechnol. Appl. Biochem.
60
170-189
2013
Medicago sativa (P28002)
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