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Information on EC 2.1.1.104 - caffeoyl-CoA O-methyltransferase
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EC Tree
2.1.1.104 caffeoyl-CoA O-methyltransferaseSpecify your search results
Word Map
- 2.1.1.104
- lignin
-
o-methylation
- flavonoid
-
phenylpropanoids
- monolignols
- polyketide
-
ferulic
- xylem
-
syringyl
-
lignification
-
sam-dependent
- poplar
-
guaiacyl
- s-adenosyl-l-homocysteine
-
2.1.1.6
-
cinnamyl
-
coniferyl
-
s-adenosyl-l-methionine-dependent
- orcinol
-
l-isoaspartyl
- aspen
-
d-aspartyl
-
4-coumarate:coa
- allata
- cinnamoyl-coa
-
sinapyl
- feruloyl-coa
-
hydroxycinnamoyl
-
feruloyl
- 4-coumarate
-
s-adenosylmethionine-dependent
- agriculture
- analysis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
ASCCoAOMT, At4g26220, caffeic acid 3-O-methyltransferase, caffeoyl CoA 3-O-methyltransferase, caffeoyl CoA methyltransferase, caffeoyl CoA methyltransferase 7, caffeoyl CoA O-methyltransferase, caffeoyl CoA-O-methyltransferase, caffeoyl coenzyme A 3-O-methyltransferase, caffeoyl coenzyme A methyltransferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
caffeic acid 3-O-methyltransferase
caffeoyl CoA 3-O-methyltransferase
caffeoyl CoA methyltransferase
caffeoyl CoA methyltransferase 7
caffeoyl coenzyme A 3-O-methyltransferase
caffeoyl coenzyme A O-methyltransferase
caffeoyl-CoA 3-O-methyltransferase
caffeoyl-coenzyme A O-methyltransferase
CCoAOMT
CCoAOMT1
CCoAOMT2
CCoAOMT7
CCOMT
COMT
OMT1
additional information
the enzyme belongs to the O-methyltransferase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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 + 3,4-dihydroxybenzaldehyde
?
moderate activity
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxybenzoic acid
S-adenosyl-L-homocysteine + ?
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + 4-coumaroyl-CoA
S-adenosyl-L-homocysteine + ?
-
very low activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-ferulic acid
S-adenosyl-L-homocysteine + ?
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid ethyl ester
?
high activity
-
-
?
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
?
-
OMT-15 shows 102% activity and OMT-17 shows 143% activity compared to myricetin
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + coniferyl alcohol
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + coniferaldehyde
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + ?
-
OMT-15 shows 100% activity and OMT-17 shows 58% activity compared to myricetin
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl CoA
33% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + caffeoyl-D-glucose
S-adenosyl-L-homocysteine + feruloyl-D-glucose
-
-
-
-
?
S-adenosyl-L-methionine + caffeoylaldehyde
?
low activity
-
-
?
S-adenosyl-L-methionine + coniferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
?
S-adenosyl-L-methionine + coniferyl alcohol
S-adenosyl-L-homocysteine + sinapyl alcohol
-
-
-
?
S-adenosyl-L-methionine + cyanidin 3-O-glucoside
S-adenosyl-L-homocysteine + peonidin 3-O-glucoside
-
-
-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + ?
2.5% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + epigallocatechin-3-O-gallate
S-adenosyl-L-homocysteine + ?
-
-
methylation occurs in 3'-, 3''- and 4''-position
-
?
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 + eriodictyol
S-adenosyl-L-homocysteine + homoeriodictyol
-
single product
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + homoeriodictyol + hesperetin
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + scopoletin
-
-
-
?
S-adenosyl-L-methionine + ferulic acid
S-adenosyl-L-homocysteine + sinapic acid
-
-
-
?
S-adenosyl-L-methionine + feruloyl-CoA
S-adenosyl-L-homocysteine + ?
-
very low activity
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + chrysoeriol
-
-
-
?
S-adenosyl-L-methionine + quercetagetin
S-adenosyl-L-homocysteine + ?
-
no activity in presence of Co2+, low activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + quercetagetin
S-adenosyl-L-homocysteine + quercetagetin 6,3'-di-O-methylether
-
-
-
?
S-adenosyl-L-methionine + sinapoyl-CoA
S-adenosyl-L-homocysteine + ?
-
low activity
-
-
?
S-adenosyl-L-methionine + trans-caffeic acid esters
S-adenosyl-L-homocysteine + ?
-
such as methyl caffeate, chlorogenic acid, trans-5-O-caffeoylshikimate, rosmarinic acid, poor substrates
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
highest activity
tricin, also identified as product
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
3' methylating activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
56% activity compared to caffeoyl-CoA
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
low activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
moderate activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
?
-
OMT-15 shows 25% activity and OMT-17 shows 18% activity compared to myricetin
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
?
high activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + baicalein
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
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 + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
-
-
?
S-adenosyl-L-methionine + caffeic acid ethyl ester
?
low activity
-
-
?
S-adenosyl-L-methionine + caffeic acid ethyl ester
?
moderate activity
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeic alcohol
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme predicted to catalyze first methylation step during biosynthesis of monolignols
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme responsible for the first methylation step during biosynthesis of monolignols
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
possibly involved in biosynthesis of oat avenanthramide phytoalexins
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
preferred substrate, 3' methylating activity
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
bi-functional enzyme, involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
the enzyme is involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
trans-caffeoyl-CoA preferred
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
inducible
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
bi-functional enzyme, involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
reaction of the overall disease resistance response of plants
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
enzyme plays a pivotal role in cell wall reinforcement during the induced disease resistance response
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
if CCoAOMT and cinnamoyl co-enzyme A reductase are coupled together, they can convert caffeoyl-CoA to coniferaldehyde if pH changes from 7.5 to 6.0
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
best substrate
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
moderate activity
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
Zinnia sp.
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
Zinnia sp.
-
essential role in the synthesis of guaiacyl lignin units as well as in the supply of substrates for the synthesis of syringyl lignin units
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
20% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
-
-
?
S-adenosyl-L-methionine + quercetin
?
moderate activity
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
-
-
-
?
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 + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
best substrate
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + scutellarein
S-adenosyl-L-homocysteine + ?
-
-
-
?
additional information
?
-
enzyme shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta-position
-
-
?
additional information
?
-
-
enzyme shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta-position
-
-
?
additional information
?
-
enzyme CCoAOMT7 binds to S-adenosyl-L-homocysteine hydrolase (SAHH) and S-adenosyl-L-methionine synthases (SAMSs) in vivo
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
enzyme CCoAOMT7 binds to S-adenosyl-L-homocysteine hydrolase (SAHH) and S-adenosyl-L-methionine synthases (SAMSs) in vivo
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
the enzyme is not able to methylate caffeic acid, 5-hydroxyferulic acid, 5-hydroxyconiferyl alcohol, kaempferol and naringenin
-
-
-
additional information
?
-
-
the enzyme is not able to methylate caffeic acid, 5-hydroxyferulic acid, 5-hydroxyconiferyl alcohol, kaempferol and naringenin
-
-
-
additional information
?
-
-
no activity with catechol, kaempferol, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
CoA and caffeoyl CoA are binding with high affinity to the enzymes in the presence and absence of S-adenosyl-L-methionine, thereby with higher affinity to isozyme CCoAOMT2 than CCoAOMT1, molecular dynamics, simulations, and docking analysis, overview. Conserved active site residues Met58, Thr60, Val63, Glu82, Gly84, Ser90, Asp160, Asp162, Thr169, Asn191 and Arg203 in CCoAOMT1 and CCoAOMT2 enzymes create the positive charge to balance the negatively charged caffeoyl CoA and play an important role in maintaining a functional conformation and are directly involved in donor substrate binding
-
-
?
additional information
?
-
CoA and caffeoyl CoA are binding with high affinity to the enzymes in the presence and absence of S-adenosyl-L-methionine, thereby with higher affinity to isozyme CCoAOMT2 than CCoAOMT1, molecular dynamics, simulations, and docking analysis, overview. Conserved active site residues Met58, Thr60, Val63, Glu82, Gly84, Ser90, Asp160, Asp162, Thr169, Asn191 and Arg203 in CCoAOMT1 and CCoAOMT2 enzymes create the positive charge to balance the negatively charged caffeoyl CoA and play an important role in maintaining a functional conformation and are directly involved in donor substrate binding
-
-
?
additional information
?
-
CCoAOMT down-regulation induces changes in xylem cell-wall structure and the lignin fractions
-
-
?
additional information
?
-
-
CCoAOMT down-regulation induces changes in xylem cell-wall structure and the lignin fractions
-
-
?
additional information
?
-
flax CCoAOMT possesses a small, but probably significant 5' methylating activity, in addition to a more usual 3' methylating activity
-
-
?
additional information
?
-
-
flax CCoAOMT possesses a small, but probably significant 5' methylating activity, in addition to a more usual 3' methylating activity
-
-
?
additional information
?
-
-
no activity with catechol, kaempferol, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
-
no activity with catechol, kaempferol, coniferyl aldehyde, and coniferyl alcohol
-
-
-
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, EC 2.1.1.68, and caffeoyl-coenzyme A-O-methyltransferase with a marked preference for CoA ester substrates over free acids, aldehydes, and alcohols
-
-
?
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, EC 2.1.1.68, and caffeoyl-coenzyme A-O-methyltransferase with a marked preference for CoA ester substrates over free acids, aldehydes, and alcohols
-
-
?
additional information
?
-
a catalytic triad, consisting of Lys157-Asn181-Asp228 residues is required for complete methyl transfer in case of a cation-dependent phenylpropanoid and flavonoid O-methyl transferase. This triad appears essential for efficient methyl transfer to catechol-like hydroxyl group in phenolics. The triad is conserved among all characterized plant caffeoyl coenzyme A O-methyltransferase-like enzymes
-
-
?
additional information
?
-
-
caffeoyl-CoA preferred to 5-hydroxyferuoyl-CoA
-
-
?
additional information
?
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
OMT-15 and -17 cannot utilize naringenin, apigenin, or kaempferol as substrates, taxifolin and eriodictyol do not serve as methyl acceptors
-
-
?
additional information
?
-
-
no substrates are caffeic acid, bergaptol, xanthotoxol, luteolin, esculetin
-
-
?
additional information
?
-
-
no activity with caffeic acid or 5-hydroxyferulic acid
-
-
-
additional information
?
-
no activity with catechol, kaempferol, caffeoyl aldehyde, caffeoyl acid, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
-
no activity with catechol, kaempferol, caffeoyl aldehyde, caffeoyl acid, coniferyl aldehyde, and coniferyl alcohol
-
-
-
additional information
?
-
no activity with kaempferol and dihydrokaempferol
-
-
-
additional information
?
-
-
no activity with kaempferol and dihydrokaempferol
-
-
-
additional information
?
-
CCoAOMT2 possesses more affinity toward caffeoyl CoA, feruloyl CoA, 5-hydroxy feruloyl CoA and sinapoyl CoA than CCoAOMT1
-
-
?
additional information
?
-
CCoAOMT2 possesses more affinity toward caffeoyl CoA, feruloyl CoA, 5-hydroxy feruloyl CoA and sinapoyl CoA than CCoAOMT1
-
-
?
additional information
?
-
no activity with caffeic acid, 5-hydroxyferuloyl-CoA, feruloyl-CoA, 4-coumaroyl-CoA, and 5-hydroxyferuloyl-CoA
-
-
-
additional information
?
-
-
no activity with caffeic acid, 5-hydroxyferuloyl-CoA, feruloyl-CoA, 4-coumaroyl-CoA, and 5-hydroxyferuloyl-CoA
-
-
-
additional information
?
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
the enzyme is capable of 3'- and 5'-methylating not only acid, aldehyde and alcohol precursors, but also ester precursors, broad substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is capable of 3'- and 5'-methylating not only acid, aldehyde and alcohol precursors, but also ester precursors, broad substrate specificity, overview
-
-
?
additional information
?
-
-
very poor substrates: 4-coumarate, caffeate, ferulate, 5-hydroxyferulate and sinapate, coumarylaldehyde, caffeoyaldehyde, coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaryl alcohol, caffeoyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol and sinapyl alcohol
-
-
?
additional information
?
-
-
recombinant TaCCoAOMT1 protein can only use caffeoyl-CoA and 5-hydroxyferuloyl-CoA as effective substrates and caffeoyl-CoA as the best substrate. No activity with p-coumarate, caffeate, ferulate, 5-hydroxyferulate, sinapate, coumarylaldehyde, caffeoyaldehyde, coniferaldehyde, 5-hydroxyconiferaldehyde, and sinapaldehyde, 4-coumaryl alcohol, caffeoyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
-
-
-
additional information
?
-
enzyme prefers as a substrate the flavone tricetin. Enzyme shows a lower activity with vanillin precursor, 3,4-dihydroxybenzaldehyde, than with tricetin
-
-
?
additional information
?
-
enzyme prefers as a substrate the flavone tricetin. Enzyme shows a lower activity with vanillin precursor, 3,4-dihydroxybenzaldehyde, than with tricetin
-
-
?
additional information
?
-
-
enzyme prefers as a substrate the flavone tricetin. Enzyme shows a lower activity with vanillin precursor, 3,4-dihydroxybenzaldehyde, than with tricetin
-
-
?
additional information
?
-
-
caffeoyl-CoA preferred to 5-hydroxyferuoyl-CoA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
enzyme predicted to catalyze first methylation step during biosynthesis of monolignols
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
possibly involved in biosynthesis of oat avenanthramide phytoalexins
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
bi-functional enzyme, involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
the enzyme is involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
inducible
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
bi-functional enzyme, involved in lignin biosynthesis
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
reaction of the overall disease resistance response of plants
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
enzyme plays a pivotal role in cell wall reinforcement during the induced disease resistance response
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
Zinnia sp.
-
essential role in the synthesis of guaiacyl lignin units as well as in the supply of substrates for the synthesis of syringyl lignin units
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
-
-
-
?
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
-
-
-
additional information
?
-
enzyme CCoAOMT7 binds to S-adenosyl-L-homocysteine hydrolase (SAHH) and S-adenosyl-L-methionine synthases (SAMSs) in vivo
-
-
-
additional information
?
-
CCoAOMT down-regulation induces changes in xylem cell-wall structure and the lignin fractions
-
-
?
additional information
?
-
-
CCoAOMT down-regulation induces changes in xylem cell-wall structure and the lignin fractions
-
-
?
additional information
?
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
additional information
?
-
-
COMT catalyzes the multi-step methylation reactions of hydroxylated monomeric lignin precursors, and plays a pivotal position in the lignin biosynthetic pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Zn2+
Ca2+
in the active site of the enzyme surrounded by an octahedral arrangement of hydroxyl and carboxyl ligands, mediates the deprotonation of the caffeoyl 3-hydroxyl group and maintains the resultant oxoanion in close proximity to the reactive methyl group of S-adenosyl-L-methionine allowing for facile transmethylation to occur, restores activity of EDTA treated CCoAOMT to 100% the level of untreated CCoAOMT
Co2+
-
0.15 mM, about 2fold increase of the rate of methylation of caffeoyl-CoA. Replacing Co2+ for Mg2+ drastically shifts the substrate preferences towards caffeic, 5-hydroxyferulic and 3,4-dihydroxybenzoic acid, which are not at all accepted in assays with Mg2+ as cofactor
Co2+
-
Co2+ results in recovery of 82% of OMT-15 and 41% of OMT-17 activity compared to the addition of Mg2+
Mg2+
restores activity of EDTA treated CCoAOMT to 100% the level of untreated CCoAOMT
Mn2+
-
0.15 mM, about 2fold increase of the rate of methylation of caffeoyl-CoA. Replacing Mn2+ for Mg2+ drastically shifts the substrate preferences towards caffeic, 5-hydroxyferulic and 3,4-dihydroxybenzoic acid, which are not at all accepted in assays with Mg2+ as cofactor
Mn2+
only restores activity of EDTA treated CCoAOMT to 35% the level of untreated CCoAOMT
Mn2+
-
the addition of Mn2+ restores 74% of OMT-15 activity and 69% of OMT-17 compared to the addition of Mg2+
Zn2+
restores activity of EDTA treated CCoAOMT to 100% the level of untreated CCoAOMT
Zn2+
-
Zn2+ results in recovery of less than 10% of OMT-15 and OMT-17 activity compared to the addition of Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
feruloyl-CoA
-
competitive to caffeoyl-CoA, non-competitive to S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
product inhibition, non-competitive to both substrates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Quercetin and Ferulic Acid Aggravate Renal Carcinoma in Long-Term Diabetic Victims.
Deafness
Integration of Tmc1/2 into the mechanotransduction complex in zebrafish hair cells is regulated by Transmembrane O-methyltransferase (Tomt).
Infections
An O-Methyltransferase Is Required for Infection of Tick Cells by Anaplasma phagocytophilum.
Infections
CbCTB2, an O-methyltransferase is essential for biosynthesis of the phytotoxin cercosporin and infection of sugar beet by Cercospora beticola.
Infections
cDNA cloning, substrate specificity and expression study of tobacco caffeoyl-CoA 3-O-methyltransferase, a lignin biosynthetic enzyme.
Infections
Transcriptional regulation of genes involved in the pathways of biosynthesis and supply of methyl units in response to powdery mildew attack and abiotic stresses in wheat.
Mycoses
Metabolic flux towards the (iso)flavonoid pathway in lignin modified alfalfa lines induces resistance against Fusarium oxysporum f. sp. medicaginis.
Mycoses
The effects of infection by Phytophthora infestans on the control of phenylpropanoid metabolism in wounded potato tissue.
Neoplasms
iTRAQ-Facilitated Proteomic Analysis of Human Prostate Cancer Cells Identifies Proteins Associated with Progression.
Tuberculosis
Crystal structure of Rv1220c, a SAM-dependent O-methyltransferase from Mycobacterium tuberculosis.
Tuberculosis
Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0827
cyanidin 3-O-glucoside
thrombin-cleaved enzyme, at pH 8.5 and 30°C
0.11
cyanidin 3-O-glucoside
GST-tagged recombinant enzyme, at pH 8.5 and 30°C
0.003
eriodictyol
wild-type, pH 7.5, temperature not specified in the publication
0.0225
eriodictyol
mutant D228A, pH 7.5, temperature not specified in the publication
0.184
eriodictyol
mutant K157A, pH 7.5, temperature not specified in the publication
0.00033
quercetagetin
wild-type, pH 7.5, temperature not specified in the publication
0.0014
quercetagetin
mutant D228A, pH 7.5, temperature not specified in the publication
0.0098
quercetagetin
mutant N181A, pH 7.5, temperature not specified in the publication
0.249
quercetagetin
mutant K157A, pH 7.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0027
cyanidin 3-O-glucoside
GST-tagged recombinant enzyme, at pH 8.5 and 30°C
0.0129
cyanidin 3-O-glucoside
thrombin-cleaved enzyme, at pH 8.5 and 30°C
0.0016
eriodictyol
mutant K157A, pH 7.5, temperature not specified in the publication
0.0028
eriodictyol
mutant D228A, pH 7.5, temperature not specified in the publication
0.1
eriodictyol
wild-type, pH 7.5, temperature not specified in the publication
0.0021
quercetagetin
mutant N181A, pH 7.5, temperature not specified in the publication
0.0116
quercetagetin
mutant D228A, pH 7.5, temperature not specified in the publication
0.078
quercetagetin
wild-type, pH 7.5, temperature not specified in the publication
0.106
quercetagetin
mutant K157A, pH 7.5, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0086
eriodictyol
mutant K157A, pH 7.5, temperature not specified in the publication
0.123
eriodictyol
mutant D228A, pH 7.5, temperature not specified in the publication
33.2
eriodictyol
wild-type, pH 7.5, temperature not specified in the publication
0.214
quercetagetin
mutant N181A, pH 7.5, temperature not specified in the publication
0.426
quercetagetin
mutant K157A, pH 7.5, temperature not specified in the publication
8.285
quercetagetin
mutant D228A, pH 7.5, temperature not specified in the publication
237
quercetagetin
wild-type, pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00143
0.00271
with coniferyl alcohol as substrate, at pH 7.5 and 37°C
0.00338
with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.00379
isoform CCoAOMT1, with 5-hydroxyconiferaldehyde as substrate, at pH 7.5 and 37°C
0.00443
with esculetin as substrate, at pH 7.5 and 37°C
0.00484
with caffeic alcohol as substrate, at pH 7.5 and 37°C
0.00518
with esculetin as substrate, at pH 7.5 and 37°C
0.00569
with coniferaldehyde as substrate, at pH 7.5 and 37°C
0.00664
isoform CCoAOMT2, with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.00705
with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.00804
isoform CCoAOMT2, with caffeoyl alcohol as substrate, at pH 7.5 and 37°C
0.00897
with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.0107
with eriodictyol as substrate, at pH 7.5 and 37°C
0.01107
isoform CCoAOMT2, with 5-hydroxyconiferaldehyde as substrate, at pH 7.5 and 37°C
0.01195
isoform CCoAOMT2, with baicalein as substrate, at pH 7.5 and 37°C
0.01285
with luteolin as substrate, at pH 7.5 and 37°C
0.01332
isoform CCoAOMT1, with caffeoyl aldehyde as substrate, at pH 7.5 and 37°C
0.01339
with quercetin as substrate, at pH 7.5 and 37°C
0.01476
isoform CCoAOMT2, with scutellarein as substrate, at pH 7.5 and 37°C
0.01607
with caffeoyl alcohol as substrate, at pH 7.5 and 37°C
0.0174
0.018
isoform CCoAOMT1, with eriodictyol as substrate, at pH 7.5 and 37°C
0.01923
with ferulic acid as substrate, at pH 7.5 and 37°C
0.02016
with caffeic acid as substrate, at pH 7.5 and 37°C
0.02313
isoform CCoAOMT1, with scutellarein as substrate, at pH 7.5 and 37°C
0.02643
isoform CCoAOMT1, with baicalein as substrate, at pH 7.5 and 37°C
0.02719
isoform CCoAOMT2, with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.03484
isoform CCoAOMT1, with caffeoyl-CoA as substrate, at pH 7.5 and 37°C
0.03572
with baicalein as substrate, at pH 7.5 and 37°C
0.03742
isoform CCoAOMT2, with luteolin as substrate, at pH 7.5 and 37°C
0.04316
isoform CCoAOMT2, with quercetin as substrate, at pH 7.5 and 37°C
0.04714
with eriodictyol as substrate, at pH 7.5 and 37°C
0.04848
isoform CCoAOMT2, with eriodictyol as substrate, at pH 7.5 and 37°C
0.05067
with scutellarein as substrate, at pH 7.5 and 37°C
0.05571
isoform CCoAOMT1, with luteolin as substrate, at pH 7.5 and 37°C
0.05666
with luteolin as substrate, at pH 7.5 and 37°C
0.05677
isoform CCoAOMT1, with quercetin as substrate, at pH 7.5 and 37°C
0.12782
with quercetin as substrate, at pH 7.5 and 37°C
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
additional information
determination of lignin content in transgenic plants, overview
additional information
-
determination of lignin content in transgenic plants, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
-
if CCoAOMT and cinnamoyl co-enzyme A reductase are coupled together, they can convert caffeoyl-CoA to coniferaldehyde if pH changes from 7.5 to 6.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
the enzyme has a very narrow pH range, it is most active at pH 7.5, and inactive below pH 6.5 and above pH 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12
after cold treatment in cultivar Doongara, upregulation of caffeoyl-CoA O-methyltransferase in anthers, accumulation of this protein does not vary greatly after cold treatment in panicles of cultivar Doongara or in the anthers of the cultivar HSC55v
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
5.1
5.3
5.4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
At4g34050; ecotypes Columbia (Col-0) and Wassilewskija (WS)
SwissProt
brenda
CCoAOMT 1; i.e. Leucaena glauca, isozyme CCoAOMT 1
UniProt
brenda
CCoAOMT 2; i.e. Leucaena glauca, isozyme CCoAOMT 2
UniProt
brenda
cv Apollo for non-transgenic and cv Regen SY for transgenic line with downregulated CCoAOMT
-
-
brenda
cv Samsun NN, 4 different clones were isolated from infected leaves
-
-
brenda
cold-sensitive cultivar Doongara and the relatively cold-tolerant cultivar HSC55
SwissProt
brenda
wheat lodging-resistant (H4546) and lodging-sensitive (C6001) cultivars
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
treated with crude cell wall elicitor from Phytophthora megasperma f.sp. glycinea
brenda
highest expression is noted in mature flower tissues
brenda
-
when oeat leaves are inocculated with Puccinia coronata, the mRNA expression of AsCCoAOMT increases in both incompatible and compatible interactions but more rapidly in incompatible interaction
brenda
-
expression during the early stages of leaf maturity, expression increases at advanced stages of leaf maturity
brenda
highly expressed in the hair cells of the developing pod
brenda
-
OMT-15 is expressed higher in stem and roots than in other tissues
brenda
-
the enzyme is highly expressed in stem, especially in the top portion of 6-week-old stem where lignification is occurring
brenda
-
maximal activity in the flowering phase, at the basal part of the stem
brenda
-
OMT-17 is expressed in stems only, OMT-15 is expressed higher in stem and roots than in other tissues
brenda
expression in all lignifying cells including vessel elements and fibers as well as in xylem ray parenchyma cells
brenda
additional information
the kenaf CCoAOMT transcript is detected in all plant tissues and organs
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
enzyme down-regulation activates anthocyanin biosynthesis in Petunia. Enzyme silencing results in a reduction of eugenol production but not of isoeugenol. Down-regulation of enzyme expression leads to the coloration of Petunia tissues
malfunction
interruptions of endogenous SAHH1 by artificial miRNA or SAMSs by T-DNA insertion significantly reduce ferulate contents in the stem cell wall
malfunction
-
interruptions of endogenous SAHH1 by artificial miRNA or SAMSs by T-DNA insertion significantly reduce ferulate contents in the stem cell wall
metabolism
COMT plays a pivotal position in the lignin biosynthetic pathway
metabolism
COMT plays a pivotal position in the lignin biosynthetic pathway
metabolism
the enzyme catalyzes central essential reactions in the lignin biosynthesis, pathway overview
metabolism
the enzyme is involved in lignin biosynthesis especially in the formation of cell wall ferulic esters of plants. It plays a pivotal role in the methylation of the 3-hydroxyl group of caffeoyl CoA
physiological function
-
CCoAOMT gene may play a role in innate generalized response to pathogen infection. CCoAOMT gene plays an essential role in the synthesis of guaiacyl lignin units and supply substrates for the synthesis of syringyl lignin units
physiological function
CCoAOMT gene may play a role in innate generalized response to pathogen infection. CCoAOMT gene plays an essential role in the synthesis of guaiacyl lignin units and supply substrates for the synthesis of syringyl lignin units
physiological function
downregulation by RNAi leads to a 22.4% decrease in Klason lignin content and a 23.3% increase in cellulose content compared with wild-type. The lignin monomer composition of the RNAi plants shows a 57.08% higher S/G ratio than wild-type plants. Histological staining of lignin with Wiesner reagent produces slightly more coloration in the xylem and sclerenchyma than in wild-type plants
physiological function
-
transgenic plants of tobacco and Medicago truncatula containing the GUS gene driven by the hi12 promoter show GUS expression following harvesting
physiological function
-
the enzyme confers resistance against cadmium (Cd) in transgenic Arabidopsis thaliana. A significant increase in biomass production, Cd uptake and translocation occurs in enzyme-transfected Arabidopsis plants compared with wild type when grown under Cd stress
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
physiological function
-
TaCCoAOMT1 is an important CCoAOMT for lignin biosynthesis that is critical for stem development, but not directly associated with lodging-resistant trait in wheat
physiological function
the enzyme contributes to anthocyanin methylation activity in grape berries, in particular under drought stress
physiological function
the enzyme contributes to lignin synthesis
physiological function
the enzyme is involved in lignin biosynthesis and affects the accumulation of phenolic acids
physiological function
the enzyme suppresses Rp1-D21-induced hypersensitive response in transgenic Nicotiana benthamiana
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
Show AA Sequence and Transmembrane Helices (783 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
28000
30000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
?
x * 28750, isoform CCoAOMT1, calculated from amino acid sequence
?
x * 32280, isoform CCoAOMT2, calculated from amino acid sequence
additional information
isozyme CCoAOMT 1, three dimensional structure building by computational methods, overview
additional information
isozyme CCoAOMT 1, three dimensional structure building by computational methods, overview
additional information
isozyme CCoAOMT 2, three dimensional structure building by computational methods, overview
additional information
isozyme CCoAOMT 2, three dimensional structure building by computational methods, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by vapor diffusion in hanging drops, at 2.45 A and 2.65 A resolution with CoA-linked substrates bound, and in complex with the reaction products
molecular docking of 16 putative substrates (intermediates of monolignol biosynthesis pathway). Both caffeic acid-O-methyltransferase, EC 2.1.1.68, and caffeoyl-coenzyme A-O-methyltransferase 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
vapor diffusion in hanging drops, enzyme in complex with the reaction products S-adenosine-L-homocysteine and feruloyl/sinapoyl CoAS
in complex with S-adenosyl-L-methionine, hanging drop vapor diffusion method, using 0.2 M calcium acetate hydrate, 0.1 M Tris, pH 8.0, and 20% (w/v) PEG 4000
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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
K157A
mutation decreases Km but not the kcat value of eriodictyol, a single, unusual product is formed, namely the yellow fluorescing quercetagetin 5-O-methyl ether
R220T
-
total loss of activity, R220 is involved in the electrostatic interaction with CoA-moiety of the substrate
E69L
-
the mutation results in about 14% loss of enzyme activity in OMT-15 and 40% loss of activity in OMT-17
L110A
the mutant shows about 9% of wild type activity with caffeic acid as substrate
L110G
the mutant shows about 9% of wild type activity with caffeic acid as substrate
L110S
the mutant shows about 9% of wild type activity with caffeic acid as substrate
L110V
the mutant shows about 29% of wild type activity with caffeic acid as substrate
L110Y
the mutant shows about 77% of wild type activity with caffeic acid as substrate
T51A
the mutation confers resistance to the bacterium Ralstonia solanacearum, resistance in F2 population is derived from a cross between a bacterial wilt-resistant variety, T51A, and a bacterial wilt-susceptible variety, T9230
additional information
additional information
enzyme downregulation leads to reduced lignin quantity a modified syringyl/guaiacyl lignin monomer ratio in the non-condensed lignin fraction, together with altered xylem organization, reduced cell-wall thickness and the appearance of an irregular xylem phenotype, phentypes of two independently down-regulated lines, overview
additional information
-
enzyme downregulation leads to reduced lignin quantity a modified syringyl/guaiacyl lignin monomer ratio in the non-condensed lignin fraction, together with altered xylem organization, reduced cell-wall thickness and the appearance of an irregular xylem phenotype, phentypes of two independently down-regulated lines, overview
additional information
construction of transgenic COMT knockout Nicotiana tabacum plants by antisense expression of COMT from Triticum aestivum, phenotype, overview
additional information
-
construction of transgenic COMT knockout Nicotiana tabacum plants by antisense expression of COMT from Triticum aestivum, phenotype, overview
additional information
construction of transgenic COMT knockout Nicotiana tabacum plants by antisense expression of COMT from Triticum aestivum via Agrobacterium tumefaciens transfection, phenotype, overview
additional information
-
construction of transgenic COMT knockout Nicotiana tabacum plants by antisense expression of COMT from Triticum aestivum via Agrobacterium tumefaciens transfection, phenotype, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography
Ni-NTA column chromatography, Resource-Q column chromatography and hydroxyapatite column chromatography
partially purified
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, expression of antisense enzyme in transgenic Nicotiana tabacum plants
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expressed as GFP fusion protein in Escherichia coli and Nicotiana tabacum
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells and Nicotiana benthamiana
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)
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli DH5alpha
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
gene CCoAOMT, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, genotyping
gene TaCCoAOMT1 is located in chromosome 7A, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of the enzyme in Escherichia coli strain BL21(DE3)
-
into the Escherichia coli expression vector pET-15b and transformed into Escherichia coli BL21(DE3)
isozyme CCoAOMT 1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
isozyme CCoAOMT 2, DNA and amino acid sequence determination and analysis, phylogenetic analysis
isozyme CCoAOMT1, DNA and amino acid sequence determination and analysis, expression profile, overview
isozyme CCoAOMT2, DNA and amino acid sequence determination and analysis, expression profile, overview
isozyme CCoAOMT5, DNA and amino acid sequence determination and analysis, expression profile, overview
ligated into pET28+(a) vector and transformed into Escherichia coli BL21(DE3)pLysS competent cells
OMT-15 and OMT-17 are expressed in Escherichia coli BL21(DE3) cells as glutathione S-transferase fusion proteins
-
recombinant expression in transgenic plants using the transformation by Agrobacterium tumefaciens strain LBA4404
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene CCoAOMT, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, genotyping
-
gene CCoAOMT, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, genotyping
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CCoAOMT is downregulated in susceptible tomato following infection with the bacterium Ralstonia solanacearum
enzyme expression is induced by methyl jasmonate and XC-1 treatment
gene expression is strongly induced by harvesting and wounding but not by heat shock. The promoter of the hi12 gene contains several stress response cis-elements
-
stress treatments highly induces the expression of CCoAOMT transcripts in the stems of 3-week-old kenaf. Cold and H2O2-treated samples show the highest levels of expression at 6 and 24 h after treatment, respectively
transcript accumulation of the enzyme is detected in berry skins, and increases during berry ripening on the plant, and in cultured berries treated with abscisic acid. Drought stress increases the enzyme transcript in berries
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
antisense repression of the enzyme ia an efficient means for genetic engineering of trees with low lignin content
analysis
-
downregulating caffeoyl CoA 3-O-methyltransferase in transgenic alfalfa lines neither reduces syringyl lignin units nor wall-bound ferulate, inconsistent with a role for this enzyme in 3-O-methylation of syringyl monolignol precursors and hydroxycinnamic acids
medicine
additional information
medicine
-
plays a role in the biosynthesis of curcuminoids, which are important pharmacologically active metabolites
medicine
-
plays a role in the biosynthesis of gingerols, which are important pharmacologically active metabolites
additional information
-
CCoAOMT and cinnamoyl co-enzyme A reductase are neighboring enzymes, reactions mediated by these two enzymes require different pH environments, indicating that compartmentalization is probably needed for CCoAOMT and cinnamoyl co-enzyme A reductase to function properly in vivo
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marita, J.M.; Ralph, J.; Hatfield, R.D.; Guo, D.; Chen, F.; Dixon, R.A.
Structural and compositional modifications in lignin of transgenic alfalfa down-regulated in caffeic acid 3-O-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase
Phytochemistry
62
53-65
2003
Medicago sativa
brenda
Day, A.; Dehorter, B.; Neutelings, G.; Czeszak, X.; Chabbert, B.; Belingheri, L.; David, H.
Caffeoyl-coenzyme A 3-O-methyltransferase enzyme activity, protein and transcript accumulation in flax (Linum usitatissimum) stem during development
Physiol. Plant.
113
275-284
2001
Linum usitatissimum
brenda
Hoffmann, L.; Maury, S.; Bergdoll, M.; Thion, L.; Erard, M.; Legrand, M.
Identification of the enzymatic active site of tobacco caffeoyl-coenzyme A O-methyltransferase by site-directed mutagenesis
J. Biol. Chem.
276
36831-36838
2001
Nicotiana tabacum
brenda
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
brenda
Zhong, R.; Morrison, W.H.; Himmelsbach, D.S.; Poole, F.L.; Ye, Z.H.
Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants
Plant Physiol.
124
563-578
2000
Populus tremula x Populus alba (Q43095)
brenda
Chen, C.; Meyermans, H.; Burggraeve, B.; De Rycke, R.M.; Inoue, K.; De Vleesschauwer, V.; Steenackers, M.; Van Montagu, M.C.; Engler, G.J.; Boerjan, W.A.
Cell-specific and conditional expression of caffeoyl-coenzyme A-3-O-methyltransferase in poplar
Plant Physiol.
123
853-867
2000
Populus tremula x Populus alba, Populus trichocarpa
brenda
Maury, S.; Geoffroy, P.; Legrand, M.
Tobacco O-methyltransferases involved in phenylpropanoid metabolism. The different caffeoyl-coenzyme A/5-hydroxyferuloyl-coenzyme A 3/5-O-methyltransferase and caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase classes have distinct substrate specificities and expression patterns
Plant Physiol.
121
215-224
1999
Nicotiana tabacum
brenda
Grimmig, B.; Kneusel, R.E.; Junghanns, K.T.; Matern, U.
Expression of bifunctional caffeoyl-CoA 3-O-methyltransferase in stress compensation and lignification
Plant Biol.
1
299-310
1999
Nicotiana tabacum, Petroselinum crispum
-
brenda
Martz, F.; Maury, S.; Pincon, G.; Legrand, M.
cDNA cloning, substrate specificity and expression study of tobacco caffeoyl-CoA 3-O-methyltransferase, a lignin biosynthetic enzyme
Plant Mol. Biol.
36
427-437
1998
Nicotiana tabacum
brenda
Meng, H.; Campbell, W.H.
Substrate profiles and expression of caffeoyl coenzyme A and caffeic acid O-methyltransferases in secondary xylem of aspen during seasonal development
Plant Mol. Biol.
38
513-520
1998
Populus tremuloides
brenda
Inoue, K.; Sewalt, V.J.H.; Ballance, G.M.; Ni, W.; Sturzer, C.; Dixon, R.A.
Developmental expression and substrate specificities of alfalfa caffeic acid 3-O-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase in relation to lignification
Plant Physiol.
117
761-770
1998
Medicago sativa (Q40313), Medicago sativa
brenda
Busam, G.; Junghanns, K.T.; Kneusel, R.E.; Kassemeyer, H.H.; Matern, U.
Characterization and expression of caffeoyl-coenzyme A 3-O-methyltransferase proposed for the induced resistance response of Vitis vinifera L
Plant Physiol.
115
1039-1048
1997
Vitis vinifera
brenda
Ni, W.; Sewalt, V.J.H.; Korth, K.L.; Blount, J.W.; Ballance, G.M.; Dixon, R.A.
Stress responses in alfalfa. XXI. Activation of caffeic acid 3-O-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase genes does not contribute to changes in metabolite accumulation in elicitor-treated cell-suspension cultures
Plant Physiol.
112
717-726
1996
Medicago sativa
brenda
Pakusch, A.E.; Matern, U.; Schiltz, E.
Elicitor-inducible caffeoyl-coenzyme A 3-O-methyltransferase from Petroselinum crispum cell suspensions
Plant Physiol.
95
137-143
1991
Petroselinum crispum
brenda
Pakusch, A.E.; Matern, U.
Kinetic characterization of caffeoyl-coenzyme A-specific 3-O-methyltransferase from elicited parsley cell suspensions
Plant Physiol.
96
327-330
1991
Petroselinum crispum
brenda
Schmidt, D.; Pakusch, A.E.; Matern, U.
Molecular cloning, induction and taxonomic distribution of caffeoyl-CoA 3-O-methyltransferase, an enzyme involved in disease resistance
J. Biol. Chem.
266
17416-17423
1991
Ammi majus, Carthamus tinctorius, Daucus carota, Dianthus caryophyllus, Petroselinum crispum
brenda
Pakusch, A.E.; Kneusel, R.E.; Matern, U.
S-Adenosyl-L-methionine:trans-caffeoyl-coenzyme A 3-O-methyltransferase from elicitor-treated parsley cell suspension cultures
Arch. Biochem. Biophys.
271
488-494
1989
Petroselinum crispum
brenda
Ye, Z.H.; Zhong, R.; Morrison, W.H.; Himmelsbach, D.S.
Caffeoyl coenzyme A O-methyltransferase and lignin biosynthesis
Phytochemistry
57
1177-1185
2001
Zinnia sp.
brenda
Vincent, D.; Lapierre, C.; Pollet, B.; Cornic, G.; Negroni, L.; Zivy, M.
Water deficits affect caffeate O-methyltransferase, lignification, and related enzymes in maize leaves. A proteomic investigation
Plant Physiol.
137
949-960
2005
Zea mays
brenda
Lukacin, R.; Matern, U.; Specker, S.; Vogt, T.
Cations modulate the substrate specificity of bifunctional class I O-methyltransferase from Ammi majus
FEBS Lett.
577
367-370
2004
Ammi majus
brenda
Yang, Q.; Trinh, H.X.; Imai, S.; Ishihara, A.; Zhang, L.; Nakayashiki, H.; Tosa, Y.; Mayama, S.
Analysis of the involvement of hydroxyanthranilate hydroxycinnamoyltransferase and caffeoyl-CoA 3-O-methyltransferase in phytoalexin biosynthesis in oat
Mol. Plant Microbe Interact.
17
81-89
2004
Avena sativa
brenda
Ferrer, J.L.; Zubieta, C.; Dixon, R.A.; Noel, J.P.
Crystal structures of alfalfa caffeoyl coenzyme A 3-O-methyltransferase
Plant Physiol.