Information on EC 2.1.1.68 - caffeate O-methyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.1.1.68
-
RECOMMENDED NAME
GeneOntology No.
caffeate O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ferulate and sinapate biosynthesis
-
-
free phenylpropanoid acid biosynthesis
-
-
phenylpropanoid biosynthesis
-
-
phenylpropanoids methylation (ice plant)
-
-
suberin monomers biosynthesis
-
-
superpathway of scopolin and esculin biosynthesis
-
-
phenylpropanoid biosynthesis
-
-
Phenylpropanoid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3,4-dihydroxy-trans-cinnamate 3-O-methyltransferase
3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
50936-45-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bambusa sp.
bamboo
-
-
Manually annotated by BRENDA team
ssp. vulgaris, spinach beet
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. Mandarin, soybean
-
-
Manually annotated by BRENDA team
flax, strain cv Barbara
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Saranac, alfalfa
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
parsley
-
-
Manually annotated by BRENDA team
french bean
-
-
Manually annotated by BRENDA team
pea
-
-
Manually annotated by BRENDA team
black cottonwood
UniProt
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
3,4-dihydroxybenzaldehyde is not the preferred substrate. The higher catalytic efficiency of the purified recombinant enzyme with the substrates caffeoyl aldehyde and 5-hydroxyconiferaldehyde, and its tissue distribution, suggest this methyltransferase may primarily unction in lignin biosynthesis
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
delphinidin
?
show the reaction diagram
-
-
-
?
eriodictyol
?
show the reaction diagram
-
best substrate, 131% relative activity
-
-
?
ethyl gallate
?
show the reaction diagram
-
-
-
?
luteolin
?
show the reaction diagram
-
88% relative activity
-
-
-
methyl gallate
?
show the reaction diagram
-
-
-
?
myricetin
?
show the reaction diagram
myricitrin
?
show the reaction diagram
-
-
-
?
n-propyl gallate
?
show the reaction diagram
best substrate
-
-
?
quercetin
?
show the reaction diagram
-
71% relative activity
-
-
-
S-adenosyl-L-methionine + 3,4,5-trihydroxycinnamic acid
S-adenosyl-L-homocysteine + 4,5-dihydroxy-3-methoxycinnamic acid
show the reaction diagram
S-adenosyl-L-methionine + 3,4-dihydroxy-5-methoxy-benzaldehyde
S-adenosyl-L-homocysteine + 4-hydroxy-3,5-dimethoxybenzaldehyde
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-hydrocinnamic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxyhydrocinnamic acid
show the reaction diagram
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
show the reaction diagram
S-adenosyl-L-methionine + 3,4-dihydroxybenzaldehyde
S-adenosyl-L-homocysteine + vanillin
show the reaction diagram
S-adenosyl-L-methionine + 3-(3,4-dihydroxyphenyl)propanoic acid
S-adenosyl-L-homocysteine + 3-(4-hydroxy-3-methoxyphenyl)propanoic acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + 5-methoxyconiferaldehyde
show the reaction diagram
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
S-adenosyl-L-homocysteine + sinapaldehyde
show the reaction diagram
S-adenosyl-L-methionine + 5-hydroxyconiferyl alcohol
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferyl alcohol
S-adenosyl-L-homocysteine + 5-hydroxy-3-methoxyconiferyl alcohol
show the reaction diagram
S-adenosyl-L-methionine + 5-hydroxyconiferyl alcohol
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyconiferyl aldehyde
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
S-adenosyl-L-homocysteine + ?
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
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
?
show the reaction diagram
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-trans-cinnamic acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + caffeic acid
S-adenosyl-L-homocysteine + ferulic acid
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + caffeic acid ethyl ester
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
?
show the reaction diagram
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + 4-[(1E)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol
show the reaction diagram
S-adenosyl-L-methionine + caffeoyl alcohol
S-adenosyl-L-homocysteine + coniferyl alcohol
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
?
show the reaction diagram
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + coniferyl aldehyde
show the reaction diagram
S-adenosyl-L-methionine + caffeoyl aldehyde
S-adenosyl-L-homocysteine + ferulic aldehyde
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + catechol
S-adenosyl-L-homocysteine + 2-methoxyphenol
show the reaction diagram
S-adenosyl-L-methionine + chlorogenic acid
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + daidzein
?
show the reaction diagram
S-adenosyl-L-methionine + esculetin
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + genistein
?
show the reaction diagram
-
poor substrate
-
-
?
S-adenosyl-L-methionine + homocatechol
S-adenosyl-L-homocysteine + 2-methoxy-4-methylphenol
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + protocatechuic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxybenzoate
show the reaction diagram
S-adenosyl-L-methionine + protocatechuic acid
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxybenzoic acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + protocatechuic aldehyde
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxybenzaldehyde
show the reaction diagram
S-adenosyl-L-methionine + pyrogallol
?
show the reaction diagram
-
poor substrate
-
-
?
S-adenosyl-L-methionine + quercetin
?
show the reaction diagram
-
-
-
-
?
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 + 3,4,5-trihydroxycinnamic acid
S-adenosyl-L-homocysteine + 4,5-dihydroxy-3-methoxycinnamic acid
show the reaction diagram
-
key lignin biosynthetic enzyme. Down-regulated transgenic plants show substantially reduced levels of transcripts, significantly reduced enzymatic activities, significantly decreased lignin content, apparently altered lignin composition and significantly increased digestibility
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
show the reaction diagram
S-adenosyl-L-methionine + 3,4-dihydroxybenzaldehyde
S-adenosyl-L-homocysteine + vanillin
show the reaction diagram
Q6Q796
3,4-dihydroxybenzaldehyde is not the preferred substrate
i.e. 4-hydroxy-3-methoxybenzaldehyde
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
?
show the reaction diagram
-
alternative pathway to monolignols involving methylation of caffeoyl aldehyde and/or caffeoyl alcohol
-
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
?
show the reaction diagram
-
alternative pathway to monolignols involving methylation of caffeoyl aldehyde and/or caffeoyl alcohol
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Methoxyethanol
-
-
5-hydroxyconiferaldehyde
-
-
5-hydroxyferulic acid
Bambusa sp.
-
competitive
ammonium sulfate
-
-
Ba2+
-
relative activity 70% of control
Ca2+
-
relative activity 58% of control
Co2+
-
strongly inhibits, relative activity 7% of control
Cu2+
-
relative activity 0% of control
EDTA
-
relative activity 77% of control
ethanol
-
-
Hg2+
-
relative activity 0% of control
luteolin
-
-
Mn2+
-
relative activity 24% of control
quercetin
-
-
Rabbit anti-O-methyltransferase immunoglobulin G
-
strong
-
S-adenosyl-L-homocysteine
Zn2+
-
relative activity 9% of control
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
7% activity increase at 20 mM
dithiothreitol
-
7% activity increase at 20 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
3,4,5-trihydroxycinnamic acid
-
-
0.005 - 0.087
3,4-dihydroxy-5-methoxy-benzaldehyde
0.01013 - 0.22
3,4-dihydroxy-trans-cinnamate
0.255
3,4-Dihydroxybenzaldehyde
pH and temperature not specified in the publication
0.00086 - 0.12
5-hydroxyconiferaldehyde
0.0038 - 0.1002
5-hydroxyconiferyl alcohol
0.0179
5-hydroxyconiferyl aldehyde
-
pH 7.5, temperature not specified in the publication
0.0068 - 0.091
5-hydroxyferulic acid
0.021
5-hydroxyferulic acid ethyl ester
pH and temperature not specified in the publication
0.009 - 0.335
caffeic acid
0.023
caffeic acid ethyl ester
pH and temperature not specified in the publication
0.012 - 0.08403
caffeoyl alcohol
0.0069 - 0.04372
caffeoyl aldehyde
2
catechol
-
isozyme I
2.5
chlorogenic acid
-
isozyme I
0.03
esculetin
-
isozyme I, m- and p-methylation
0.04
homocatechol
-
isozyme I
0.23
Hydrocaffeic acid
-
isozyme I
0.96
methyl gallate
;
0.052 - 2.5
protocatechuic acid
0.005 - 0.7
Protocatechuic aldehyde
0.0237
quercetin
-
pH 7.5, temperature not specified in the publication
0.0021 - 0.051
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.23
5-hydroxyconiferyl alcohol
Arabidopsis thaliana
-
pH 7.5, temperature not specified in the publication
2.85
5-hydroxyconiferyl aldehyde
Arabidopsis thaliana
-
pH 7.5, temperature not specified in the publication
1.3
5-hydroxyferulic acid
Arabidopsis thaliana
-
pH 7.5, temperature not specified in the publication
0.62
caffeic acid
Arabidopsis thaliana
-
pH 7.5, temperature not specified in the publication
1.52
caffeoyl alcohol
Arabidopsis thaliana
-
pH 7.5, temperature not specified in the publication
1.55
caffeoyl aldehyde
Arabidopsis thaliana
-
pH 7.5, temperature not specified in the publication
0.23
methyl gallate
Vanilla planifolia
Q27I62, Q27I63
;
0.068
myricetin
Vanilla planifolia
Q27I62, Q27I63
;
0.16
quercetin
Arabidopsis thaliana
-
pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014
3,4-dihydroxy-trans-cinnamate
Triticum aestivum
Q38J50
-
10495
0.0037
5-hydroxyconiferaldehyde
Triticum aestivum
Q38J50
-
3403
0.0011
5-hydroxyconiferyl alcohol
Triticum aestivum
Q38J50
-
6766
0.0017
caffeoyl alcohol
Triticum aestivum
Q38J50
-
6769
0.0024
caffeoyl aldehyde
Triticum aestivum
Q38J50
-
5329
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0027 - 0.01
5-hydroxyconiferaldehyde
0.00044 - 0.0069
S-adenosyl-L-homocysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0027
-
-
0.00546
-
-
0.14
-
with caffeoyl-CoA as substrate
0.265
-
with 5-hydroxyferuoyl-CoA as substrate
0.48
-
with caffeic acid as substrate
1.077
-
with 5-hydroxyferulic acid as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
around
6.5 - 7
-
methylation of caffeic and 5-hydroxyferulic acid
7
-
around
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
more than half-maximal activity at pH 5.0 and 8.5
5 - 9
-
-
5.4 - 7.6
-
about half-maximal activity at pH 5.4 and 7.6
6.5 - 8
-
more than half-maximal activity at pH 6.5 and 8.0
7 - 7.4
-
37% of maximal activity at pH 7.0, 75% of maximal activity at pH 7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression level
Manually annotated by BRENDA team
Bambusa sp.
-
-
Manually annotated by BRENDA team
-
COMT1 is not localized in the tapetum, but in two directly adjacent cells layers, the endothecium and the epidermal layer of stamens
Manually annotated by BRENDA team
strong expression level
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38770
sequence analysis
38920
sequence analysis
39800
-
amino acid analysis
42300
-
sequence analysis
43000
-
SDS-PAGE, recombinant enzyme
60000
-
HPLC gel filtration
80000
gel filtration
93000
-
isozyme I, gel filtration
103000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 40000, SDS-PAGE, 2 * 39839, calculated
monomer
-
1 * 41000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
x-ray crystallographic structures of Lp OMT1 are reported in open conformational state, apo- and holoenzyme forms and, most significantly, in a closed conformational state complexed with the products S-adenosyl-L-homocysteine and sinapaldehyde. The product-bound complex reveals the postmethyl-transfer organization of COMTs catalytic groups with reactant molecules and the fully formed phenolic-ligand binding site. The core scaffold of the phenolic ligand forges a hydrogen-bonding network involving the 4-hydroxy group that anchors the aromatic ring and thereby permits only metahydroxyl groups to be positioned for transmethylation
-
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
-
apo-form and binary complex with S-adenosyl-methionine, to 2.1 and 2.8 A resolution, respectively, and molecular modeling of the ternary complex structure with 5-hydroxyconiferaldehyde
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
isozyme I inactivates after 5 min, isozyme II loses 70% of activity after 2 h, isozyme III has 50% activation after 2 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol or dithiothreitol or GSH reduces storage stability
-
2-mercaptoethanol stabilizes
-
freezing causes complete inactivation
-
gel filtration leads to severe loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, at least a month in absence of thiol compounds
-
-70C, 2 months, stable
-
-80C, Tris-HCl buffer, 10% glycerol and 2-mercaptoethanol, pH 8.0
-
-80C, Tris-HCl buffer, pH 7.5
-
0C, 65%-85% of initial activity retained after 5 months in the presence of 2-mercaptoethanol
-
4C, 0.02% NaN3, at least 2 months
-
4C, 4-5 d, assay buffer, 50% activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
affinity chromatography on S-adenosyl-homocysteine-agarose
-
by His-Bind column chromatography
-
by nickel affinity chromatography; by nickel affinity chromatography
native enzyme partially by adenosine-agarose affinity chromatography, 18.2fold for 3,4-dihydroxybenzaldehyde-O-methyltransferase activity and 16.7fold for caffeic acid O-methyltransferase activity
Ni-NTA column chromatography
Ni2+-agarose affinity column chromatography, gel filtration; Ni2+-agarose affinity column chromatography, gel filtration
three caffeic acid methylating activities: isozymes I, II, III, with an enzyme density of 1.277 kg/l, determined by isopycnic equilibrium centrifugation
-
using affinity chromatography
-
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA clone Ptomt1 in Escherichia coli
-
cloning from phage library, DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression in Escherichia coli strain BL21(DE3), subcloning in strain JM109
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells and in Nicotiana tabacum cultivar Wisconsin 38
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression as N-terminal polyhistidine-tagged fusion in Escherichia coli BL21-CodonPlus (DE3)-RIPL competent cells based on the expression vector pET-15bexpression; expression as N-terminal polyhistidine-tagged fusion in Escherichia coli BL21-CodonPlus (DE3)-RIPL competent cells based on the expression vector pET-15bexpression
expression in Escherichia coli
expression in Escherichia coli BL21
-
expression in Escherichia coli XL-1 Blue
-
expression in Escherichia coli. Transgenic Festuca arundinacea plants carrying either sense or antisense COMT gene constructs are obtained by microprojectile bombardment of single-genotype-derived embryogenic suspension cells. Two co-suppressed transgenic lines are down-regulated in their lignin biosynthesis. These down-regulated transgenic plants show substantially reduced levels of transcripts, significantly reduced enzymatic activities, significantly decreased lignin content, apparently altered lignin composition and significantly increased digestibility
-
maize COMT gene expressed in Arabidopsis thaliana plants
-
recombinantly expressed as a His-tagged fusion protein
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by wounding, salicylic acid, cold and H2O2 treatments, and treatment with methyl jasmonate and NaCl
expression of both OMT1 and OMT3 genes is elevated during the early elongation (E1) stage. OMT1 shows low expression at E2 and E3 stages and is strongly upregulated at the R1 stage, with the highest level of expression in the uppermost internode. Both OMT3 and OMT1 genes show a low level of expression at R2 and R3 developmental stages; expression of both OMT1 and OMT3 genes is elevated during the early elongation (E1) stage. OMT3 shows almost complementary expression profiles to OMT1 at the E2, E3, and R1 stages with low expression at R1 stage. Both OMT3 and OMT1 genes show a low level of expression at R2 and R3 developmental stages
-
increase in expression level under chilling treatment suggesting that COMT might play an important role in the accumulation of ferulic acid under chilling treatment
mRNA levels are higher in cultivar H4546 from elongation to the milky stages and in cultivar C6001 the mRNA levels decrease markedly at the heading and milky stages, the protein levels and COMT activity are also higher in cultivar H4564 than that in cultivar C6001 at the heading and milky stages. mRNA levels, protein levels, and enzyme activity in developing wheat stems were associated with stem strength and lodging index
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H268L
complete loss of catalytic acitivity
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
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
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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
A71V
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mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
G225D
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mutation greatly reduces protein accumulation and mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
G325S
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mutation impairs enzyme activity compared to wild type and mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
P150L
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mutation impairs enzyme activity and mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
additional information
the brown-midrib-3 mutant is disrupted in the caffeic acid O-methyltransferase gene with nearly null COMT activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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engineered COMT enzymes can be useful for metabolic engineering of both lignin and benzaldehyde-derived flavors and fragances
additional information