Information on EC 2.1.1.104 - caffeoyl-CoA O-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.104
-
RECOMMENDED NAME
GeneOntology No.
caffeoyl-CoA O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
capsaicin biosynthesis
-
-
chlorogenic acid biosynthesis I
-
-
coumarins biosynthesis (engineered)
-
-
Flavonoid biosynthesis
-
-
Metabolic pathways
-
-
Phenylalanine metabolism
-
-
phenylpropanoid biosynthesis
-
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Phenylpropanoid biosynthesis
-
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phenylpropanoids methylation (ice plant)
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scopoletin biosynthesis
-
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Stilbenoid, diarylheptanoid and gingerol biosynthesis
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suberin monomers biosynthesis
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phenylpropanoid biosynthesis
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suberin monomers biosynthesis
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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 hide
120433-42-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. US10, safflower
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ssp. sativus, carrot
-
-
Manually annotated by BRENDA team
cv. Mei Ling, carnation
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
resistant genotype against Ralstonia solanacearum
-
-
Manually annotated by BRENDA team
cv Gamay Fréaux, fungal elicitation
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-
Manually annotated by BRENDA team
Zinnia sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 3,4-dihydroxybenzaldehyde
?
show the reaction diagram
moderate activity
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxybenzoic acid
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-ferulic acid
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
activity in presence of Co2+, no activity in presence of Mg2+
-
-
?
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
show the reaction diagram
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
show the reaction diagram
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
show the reaction diagram
S-adenosyl-L-methionine + 5-hydroxyferulic acid
?
show the reaction diagram
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + sinapic acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid ethyl ester
?
show the reaction diagram
high activity
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferuoyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
show the reaction diagram
S-adenosyl-L-methionine + 7,8-dihydroxyflavone
?
show the reaction diagram
-
OMT-15 shows 102% activity and OMT-17 shows 143% activity compared to myricetin
-
-
?
S-adenosyl-L-methionine + caffeic acid
?
show the reaction diagram
low activity
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
show the reaction diagram
S-adenosyl-L-methionine + caffeic acid ethyl ester
?
show the reaction diagram
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
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
show the reaction diagram
33% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
show the reaction diagram
S-adenosyl-L-methionine + caffeoyl-D-glucose
S-adenosyl-L-homocysteine + feruloyl-D-glucose
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + caffeoylaldehyde
?
show the reaction diagram
low activity
-
-
?
S-adenosyl-L-methionine + dihydroquercetin
S-adenosyl-L-homocysteine + ?
show the reaction diagram
2.5% of the activity with luteolin
-
-
?
S-adenosyl-L-methionine + epigallocatechin-3-O-gallate
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
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
show the reaction diagram
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
show the reaction diagram
-
single product
-
?
S-adenosyl-L-methionine + esculetin
S-adenosyl-L-homocysteine + ?
show the reaction diagram
20% of the activity with luteolin
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-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + scoparol
show the reaction diagram
-
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + myricetin
?
show the reaction diagram
high activity
-
-
?
S-adenosyl-L-methionine + quercetagetin
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
no activity in presence of Co2+, low activity in presence of Mg2+
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-
?
S-adenosyl-L-methionine + quercetagetin
S-adenosyl-L-homocysteine + quercetagetin 6,3'-di-O-methylether
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + quercetin
?
show the reaction diagram
moderate activity
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + isorhamnetin
show the reaction diagram
60% of the activity with luteolin
synthesis of a single meta-methylated product
-
?
S-adenosyl-L-methionine + trans-caffeic acid esters
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
such as methyl caffeate, chlorogenic acid, trans-5-O-caffeoylshikimate, rosmarinic acid, poor substrates
-
-
?
S-adenosyl-L-methionine + tricetin
S-adenosyl-L-homocysteine + selgin
show the reaction diagram
highest activity
tricin, also identified as product
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 5-hydroxy-feruloyl-CoA
S-adenosyl-L-homocysteine + sinapoyl-CoA
show the reaction diagram
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
show the reaction diagram
Q4JHB1
-
-
-
?
S-adenosyl-L-methionine + caffeoyl-CoA
S-adenosyl-L-homocysteine + feruloyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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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
NaCl
-
activation, 0.4 M
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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0.15 mM, completely abolishes the rate of methylation of caffeoyl-CoA
Feruloyl-CoA
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competitive to caffeoyl-CoA, non-competitive to S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
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product inhibition, non-competitive to both substrates
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
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activation, 12% v/v
NaCl
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activation, 0.4 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.039
3,4-dihydroxybenzoic acid
-
pH 7.5, 37°C, in presence of 0.1 mM Co2+
0.0173
5-hydroxy-coniferaldehyde
-
0.0952
5-hydroxy-feruloyl-CoA
-
0.068
5-hydroxyferulic acid
-
pH 7.5, 37°C, in presence of 0.1 mM Co2+
0.0007 - 0.0062
5-hydroxyferuoyl-CoA
0.039 - 0.088
caffeic acid
0.0437
caffeoyl aldehyde
-
0.00024 - 0.64
caffeoyl-CoA
0.061 - 0.93
caffeoyl-D-glucose
0.101
epigallocatechin-3-O-gallate
-
pH 6.8, 35°C
0.003 - 0.28
eriodictyol
0.00033 - 0.249
quercetagetin
0.031 - 0.073
quercetin
0.16
S-adenosyl-L-methionine
-
pH 6.8, 35°C
0.109 - 0.158
tricetin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
3,4-dihydroxybenzoic acid
Ammi majus
-
pH 7.5, 37°C, in presence of 0.1 mM Co2+
0.143
5-hydroxyferulic acid
Ammi majus
-
pH 7.5, 37°C, in presence of 0.1 mM Co2+
0.068
caffeic acid
Ammi majus
-
pH 7.5, 37°C, in presence of 0.1 mM Co2+
0.149 - 6.08
caffeoyl-CoA
0.206 - 6.08
caffeoyl-D-glucose
0.184
epigallocatechin-3-O-gallate
Camellia sinensis
-
pH 6.8, 35°C
0.0016 - 0.1
eriodictyol
0.0021 - 0.106
quercetagetin
0.268 - 6.08
quercetin
0.049
S-adenosyl-L-methionine
Camellia sinensis
-
pH 6.8, 35°C
0.011 - 0.0913
tricetin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000503
caffeoyl-CoA
Oryza sativa
-
OMT-17, in 10 mM Tris-HCl buffer (pH 7.5), at 37°C
537
1.84
epigallocatechin-3-O-gallate
Camellia sinensis
-
pH 6.8, 35°C
9591
0.0086 - 33.2
eriodictyol
2485
0.214 - 237
quercetagetin
4128
0.31
S-adenosyl-L-methionine
Camellia sinensis
-
pH 6.8, 35°C
24
0.069 - 0.838
tricetin
2788
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
with 5-hydroxyferulic acid
0.008
-
with 5-hydroxyferuloyl-CoA
0.021
-
with caffeoyl-CoA
0.0313
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unreliable, great loss during purification
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
40% of maximum activity
6.9 - 8.6
-
about half-maximal activity at pH 6.9 and 8.6
8.5
-
40% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
40
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40% of maximum activity
50
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almost complete loss of activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
calculated
5.3
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression is noted in mature flower tissues
Manually annotated by BRENDA team
highly expressed in the hair cells of the developing pod; low expression
Manually annotated by BRENDA team
tapetum of young stamen
Manually annotated by BRENDA team
interfascicular fibres
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
2 * 24000, SDS-PAGE
27230
-
calculated mass for the translated polypeptide
27800
-
OMT-15, calculated from amino acid sequence
27900
x * 27900, about, sequence calculation
27910
calculated from cDNA
27930
calculated from cDNA
28400
predicted
28802
-
x * 28802, calculated
29000
x * 29000, SDS-PAGE
30600
-
recombinant OMT-17, SDS-PAGE
31100
-
recombinant OMT-15, SDS-PAGE
32000
-
OMT-17, calculated from amino acid sequence
33000
-
SDS-PAGE
33220
calculated from cDNA
38600
x * 38600, about, sequence calculation
48000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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; vapor diffusion in hanging drops, enzyme in complex with the reaction products S-adenosine-L-homocysteine and feruloyl/sinapoyl CoAS
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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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
unstable below
485077
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; by sonication, centrifugation and Ni2+-NTA column, more than 98% pure
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affinity chromatography on Blue Sepharose CL-6B, isoelectric focusing
-
by nickel affinity chromatography
glutathione Sepharose 4 column chromatography
-
mutant and wild-type protein
partially purified
recombinant enzyme
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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
using Ni-NTA chromatography; using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 clones were expressed in Escherichia coli
-
4 clones were expressed in Escherichia coli; expression in Escherichia coli DH5alpha
-
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 in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein; expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli strain TG2
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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
-
expression in Escherichia coli JM109 DE3
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gene CCoAOMT, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, genotyping
into the Escherichia coli expression vector pET-15b and transformed into Escherichia coli BL21(DE3)
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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
transformed with parsley gene
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CCoAOMT is downregulated in susceptible tomato following infection with the bacterium Ralstonia solanacearum
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
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
D228A
only residual enzyme activities are detectable
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
N181A
complete loss of activity with eriodictyol
D58A
-
decrease of catalytic activity
Q61S
-
decrease of catalytic activity
R220T
-
total loss of activity, R220 is involved in the electrostatic interaction with CoA-moiety of the substrate
D168L
-
the mutation abolishes the enzyme activity of OMT-15
D194L
-
the mutation abolishes the enzyme activity of OMT-15
D209L
-
the mutation abolishes the enzyme activity of OMT-17
D234L
-
the mutation abolishes the enzyme activity of OMT-17
E69L
-
the mutation results in about 14% loss of enzyme activity in OMT-15 and 40% loss of activity in OMT-17
N195I
-
the mutation abolishes the enzyme activity of OMT-15
N235I
-
the mutation abolishes the enzyme activity of OMT-17
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Show AA Sequence (283 entries)
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