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4-coumarate + MgATP2- + tetrapolyphosphate
adenosine 5'-pentaphosphate + ?
-
CoA omitted from the incubation mixture
-
r
4-coumarate + MgATP2- + tripolyphosphate
adenosine 5'-tetraphosphate + ?
-
CoA omitted from the incubation mixture
-
r
AMP + 3-oxo-2-(2'-[Z]-pentenyl)-cyclopentane-1-butanoic acid + CoA
?
-
weak substrate
-
-
?
AMP + 3-oxo-2-(2'-[Z]-pentenyl)-cyclopentane-1-hexanoic acid + CoA
?
-
weak substrate
-
-
?
AMP + dinor-12-oxo-phytodienoic acid + CoA
?
-
-
-
-
?
ATP + (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid + CoA
?
-
-
-
-
?
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
ATP + 3,4,5-trimethoxycinnamate + CoA
AMP + diphosphate + 3,4,5-trimethoxycinnamoyl-CoA
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
ATP + 3-methoxcinnamate + CoA
AMP + diphosphate + 3-methoxycinnamoyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
ATP + 4-methoxyferulate + CoA
AMP + diphosphate + 4-methoxyferuloyl-CoA
-
-
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
ATP + caffeic acid + CoA
AMP + diphosphate + caffeoyl-CoA
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
ATP + cinnamic acid + CoA
AMP + diphosphate + cinnamoyl-CoA
-
3-phenyl-2-propenoic acid, 98%
-
-
?
ATP + decanoate + CoA
AMP + diphosphate + decanoyl-CoA
-
weak substrate
-
-
?
ATP + dihydro-4-coumarate + CoA
AMP + diphosphate + dihydro-4-coumaroyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
ATP + ferulate + CoA
AMP + diphosphate + ferulyl-CoA
ATP + ferulic acid + CoA
AMP + diphosphate + 4-feruloyl-CoA
-
4-hydroxy-3-methoxycinnamic acid, 99%
-
-
?
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
-
-
-
-
?
ATP + hexadecanoate + CoA
AMP + diphosphate + hexadecanoyl-CoA
-
weak substrate
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
-
-
-
-
?
ATP + indole propanoic acid + CoA
?
-
-
-
-
?
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
ATP + nonanoate + CoA
AMP + diphosphate + nonanoyl-CoA
-
-
-
-
?
ATP + octadecanoate + CoA
AMP + diphosphate + octadecanoyl-CoA
-
weak substrate
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
-
-
-
-
?
ATP + propanoate + CoA
AMP + diphosphate + propanoyl-CoA
-
weak substrate
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
ATP + sinapic acid + CoA
AMP + diphosphate + 4-sinapoyl-CoA
-
3,5-dimethoxy-4-hydroxycinnamic acid, 98%, predominantly trans isomer
-
-
?
ATP + sinapinate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
ATP + sinapoylmalate + CoA
AMP + diphosphate + sinapoylmaloyl-CoA
ATP + tetradecanoate + CoA
AMP + diphosphate + tetradecanoyl-CoA
-
-
-
-
?
ATP + trans-cinnamate + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
CTP + ferulate + CoA
CMP + diphosphate + feruloyl-CoA
-
7.7% of the activity relative to ATP
-
-
?
GTP + ferulate + CoA
GMP + diphosphate + feruloyl-CoA
-
5.7% of the activity relative to ATP
-
-
?
ITP + ferulate + CoA
IMP + diphosphate + feruloyl-CoA
-
20.2% of the activity relative to ATP
-
-
?
MgATP2-
diadenosine 5',5'',P1,P4-tetraphosphate + ?
-
no additional substrate, CoA omitted from the incubation mixture
-
?
UTP + ferulate + CoA
UMP + diphosphate + feruloyl-CoA
-
12.5% of the activity relative to GTP
-
-
?
additional information
?
-
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
-
-
-
-
?
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
-
-
-
-
?
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
-
-
-
-
?
ATP + 2-coumarate + CoA
AMP + diphosphate + 2-coumaroyl-CoA
-
-
-
?
ATP + 3,4,5-trimethoxycinnamate + CoA
AMP + diphosphate + 3,4,5-trimethoxycinnamoyl-CoA
-
isoenzyme 1 is active, isoenzyme 2 not
-
-
?
ATP + 3,4,5-trimethoxycinnamate + CoA
AMP + diphosphate + 3,4,5-trimethoxycinnamoyl-CoA
-
no activity
-
-
?
ATP + 3,4,5-trimethoxycinnamate + CoA
AMP + diphosphate + 3,4,5-trimethoxycinnamoyl-CoA
-
no activity
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
84% of the activity relative to ferulate
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
isoenzyme 1 is active, isoenzyme 2 not
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
substrate for 4CL1 but not for 4CL2 and 4CL3
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
-
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
-
-
-
?
ATP + 3,4-dimethoxycinnamate + CoA
AMP + diphosphate + 3,4-dimethoxycinnamoyl-CoA
-
no activity
-
-
?
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
-
high activity
-
-
?
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
-
-
-
-
?
ATP + 3-coumarate + CoA
AMP + diphosphate + 3-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
?
-
4-coumarate-CoA ligase is the last enzyme of the general phenylpropanoid metabolism, supplying substrates for lignin formation and other individual phenylpropanoid pathways
-
-
?
ATP + 4-coumarate + CoA
?
-
enzyme of B-ring-deoxy flavonoid biosymthesis
-
-
?
ATP + 4-coumarate + CoA
?
-
enzyme is involved in the resistance response of soybean against pathogen attack. The different substrate affinities for substituted cinnamic acids and the differential regulation of the 3 isoenzymes, may play a pivotal role in distributing substituted cinnamate intermediates at a branch point of general phenylpropanoid metabolism into subsequent specific pathways
-
-
?
ATP + 4-coumarate + CoA
?
-
enzyme has an important role in the determination of the composition and the amount of lignin in tobacco plants
-
-
?
ATP + 4-coumarate + CoA
?
-
key enzyme of general phenylpropanoid metabolism
-
-
?
ATP + 4-coumarate + CoA
?
-
the isoenzymes can play an important role in the control of the monomeric composition of lignins
-
-
?
ATP + 4-coumarate + CoA
?
-
physiological role in lignin biosynthesis
-
-
?
ATP + 4-coumarate + CoA
?
-
key enzyme of phenylpropanoid metabolism
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
52% of the activity with caffeate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
high activity
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism, 4CL2 involved in coenzyme A ester formation and cocatalytic AMP-donor in (di)adenosine polyphosphate synthesis
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
plant phenylpropanoid metabolism, class II enzymes part of flavonoid pathway, class I enzymes probably involved in lignin formation and phenolic compound other than flavonoids
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
140% of the activity relative to ferulate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
Forsythia sp.
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
assay at pH 7.5
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
ir
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
the enzyme is involved in the phenylpropanoid pathway
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
4-hydroxycinnamic acid, 98%, predominantly trans-isomer
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
best substrate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
best substrate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
best substrate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
high activity
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
highest catalytic efficiency towards 4-coumarate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
94% of the activity relative to ferulate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
preferred substrate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
4-coumarate is the most favorable substrate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
Polyporus hispidus
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
Polyporus hispidus UBC 513
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
plant phenylpropanoid metabolism
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
isoenzyme 4CL1 exhibits very high activity towards p-coumarate, isoenzymes 4CL2 and 4CL3 are active
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
100% activity
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
100% activity
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
the enzyme is involved in the phenylpropanoid pathway
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
preferred substrate
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-coumarate + CoA
AMP + diphosphate + 4-coumaroyl-CoA
-
-
-
-
?
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
-
-
-
-
?
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
-
68% of the activity relative to ferulate
-
-
?
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
-
isoenzyme 1 is active, isoenzyme 2 not
-
-
?
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
-
12% of the activity relative to 4-coumarate
-
-
?
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
-
-
-
-
?
ATP + 4-methoxycinnamate + CoA
AMP + diphosphate + 4-methoxycinnamoyl-CoA
-
-
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
17% of the activity relative to ferulate
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
-
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
-
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
18% of the activity relative to ferulate
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
41% of the activity relative to p-hydroxycinnamate
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
-
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
isoenzyme I is active, no activity is detectable with isoenzyme II and III
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
isoenzyme 4CL2, weak activity, isoenzyme 4CL1 and 4CL3 show no activity
-
-
?
ATP + 5-hydroxyferulate + CoA
AMP + diphosphate + 5-hydroxyferuloyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
high activity
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
at 4% of the activity relative to 4-coumarate
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
48% of the activity relative to ferulate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
14% of the activity relative to 4-coumarate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
low activity
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
low activity
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
86% of the activity relative to ferulate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
same activity as with 4-coumarate
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
Polyporus hispidus
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
Polyporus hispidus UBC 513
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
61% of the activity relative to p-hydroxycinnamate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
isoenzyme III is active, no activity is detectable with isoenzyme I and II
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
isoenzyme 4CL1, 4CL2 and 4CL3 show activity
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
48% activity compared to 4-coumarate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
86% activity compared to 4-coumarate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
86% activity compared to 4-coumarate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
48% activity compared to 4-coumarate
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
?
ATP + caffeate + CoA
AMP + diphosphate + caffeoyl-CoA
-
-
-
-
?
ATP + caffeic acid + CoA
AMP + diphosphate + caffeoyl-CoA
-
3,4-dihydroxycinnamic acid, 98%
-
-
?
ATP + caffeic acid + CoA
AMP + diphosphate + caffeoyl-CoA
-
3,4-dihydroxycinnamic acid, 98%, predominantly trans-isomer
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
9% of the activity with caffeate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
same Vmax like 4-coumarate
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
10% of the activity relative to 4-coumarate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
-
ir
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
low activity
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
ir
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
14% of the activity relative to ferulate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
roughly 30% of activity
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
5.0% activity compared to 4-coumarate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
54% activity compared to 4-coumarate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
54% activity compared to 4-coumarate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
5.0% activity compared to 4-coumarate
-
-
?
ATP + cinnamate + CoA
AMP + diphosphate + cinnamoyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
16% of the activity with caffeate
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
M293P/K320L mutant enzyme, no substrate for wild type enzyme
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
only 4CL1 and 4CL3, no substrate for 4CL2, some 4CL2 mutants are active with ferulate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
only 4CL1, no substrate for 4CL2
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
very poor substrate for the wild type enzyme, effective substrate for M293P/K320L mutant enzyme
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
3% of the activity relative to 4-coumarate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
Forsythia sp.
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
49% of the activity relative to 4-coumarate
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
substrate for 4CL1 and 4CL2, very poor substrate for 4CL3
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
high activity
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
strong preference for ferulate by isozyme Os4CL2, high activity
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
same activity as with 4-coumarate
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
Polyporus hispidus
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
Polyporus hispidus UBC 513
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
67% of the activity relative to p-hydroxycinnamate
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
good substrate for isoform 4CL4
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
good substrate for isoform 4CL5
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
only 4CL1, no substrate for 4CL2
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
roughly 60% of activity
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
isoenzyme 4CL2 and 4CL3 are active, no activity with isoenzyme 4CL1
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
2.5% activity compared to 4-coumarate
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
50.5% activity compared to 4-coumarate
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
2.5% activity compared to 4-coumarate
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
50.5% activity compared to 4-coumarate
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + feruloyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + ferulyl-CoA
-
-
-
-
?
ATP + ferulate + CoA
AMP + diphosphate + ferulyl-CoA
-
-
-
?
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
-
as effective as ferulate
-
-
?
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
-
-
-
-
?
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
-
-
-
-
?
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
-
-
-
?
ATP + isoferulate + CoA
AMP + diphosphate + isoferuloyl-CoA
-
-
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
-
substrate for 4CL1 but not for 4CL2 and 4CL3
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
?
ATP + sinapate + CoA
AMP + diphosphate + sinapoyl-CoA
-
isoenzymes 4CL2 and 4CL3 are active, isoenzyme 4CL1 is inactive
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
no activity
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
48% of the activity relative to ferulate
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
isoenzyme 1 is active with sinapoate, isoenzyme 2 not
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
no activity
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
no activity
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
no activity
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
isoenzyme I is active, no activity with isoenzyme II and III
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
-
-
-
?
ATP + sinapoate + CoA
AMP + diphosphate + sinapoyl-CoA
-
no activity
-
-
?
ATP + sinapoylmalate + CoA
AMP + diphosphate + sinapoylmaloyl-CoA
substrate for isoform 4CL1
-
-
?
ATP + sinapoylmalate + CoA
AMP + diphosphate + sinapoylmaloyl-CoA
substrate for isoform 4CL3
-
-
?
ATP + trans-cinnamate + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
-
-
-
?
ATP + trans-cinnamate + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
-
-
-
?
additional information
?
-
no activity with either sinapate or 4-hydroxybenzoate. The more hydroxyl groups are present, the better is the activity of the enzyme. Methoxy groups on the aromatic ring have a negative effect on enzyme activity. It is possible that methoxy groups cause a steric obstruction. No activity can be measured if there is no acryl group present in the substrate
-
-
?
additional information
?
-
inactive against sinapic acid
-
?
additional information
?
-
inactive against sinapic acid
-
?
additional information
?
-
-
inactive against sinapic acid
-
?
additional information
?
-
inactive against sinapic acid and ferulic acid
-
?
additional information
?
-
inactive against sinapic acid and ferulic acid
-
?
additional information
?
-
-
inactive against sinapic acid and ferulic acid
-
?
additional information
?
-
-
biosynthesis of lignin monomers occurs via the phenylpropanoid pathway, in which the enzyme 4-coumarate-CoA ligase plays a key role by catalyzing the formation of hydroxycinnamoyl-CoA esters, subsequently reduced to the corresponding monolignols hydroxycinnamoyl alcohols, overview, cis-regulatory elements involved in the developmental and wound-induced regulation of the 4CL gene family members, stress-regulated expression, overview
-
-
?
additional information
?
-
-
the 4-coumarate-CoA ligase, 4CL, gene family members are involved in channeling carbon flow into branch pathways of phenylpropanoid metabolism, identification of regulatory genes, overview
-
-
?
additional information
?
-
-
the enzyme from different tissues varies significantly in substrate specificity
-
-
?
additional information
?
-
-
a 7fold increase in 4CL activity is observed in elicited cultures after 24 h of chitosan treatment (200 mg/l) as compared to control
-
-
?
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
?
additional information
?
-
-
in ATP-diphosphate exchange reaction absolute specificity for cinnamate
-
-
?
additional information
?
-
no reaction with 3,4-dimethoxycinnamate and sinapate
-
?
additional information
?
-
no reaction with 3,4-dimethoxycinnamate and sinapate
-
?
additional information
?
-
no reaction with 3,4-dimethoxycinnamate and sinapate
-
?
additional information
?
-
no reaction with 3,4-dimethoxycinnamate and sinapate
-
?
additional information
?
-
-
no reaction with 3,4-dimethoxycinnamate and sinapate
-
?
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
?
additional information
?
-
no activity with sinapic acid
-
-
?
additional information
?
-
-
no activity with sinapic acid
-
-
?
additional information
?
-
no activity with sinapic acid
-
-
?
additional information
?
-
the enzyme catalyzes the conversion of 4-coumaric acid into coumaroyl-CoA and a few related substrates into their corresponding products such as cinnamoyl-CoA, caffeoyl-CoA, and feruloyl-CoA in a process utilizing ATP, and thus channels the common, phenylalanine-derived building block into the widely distinct branches of general phenylpropanoid metabolism
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
-
high affinity for 4-coumarate and ferulate by isozyme Os4Cl4, no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
-
no activity with sinapate and caffeate
-
-
?
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
?
additional information
?
-
-
absolute requirement for ATP
-
-
?
additional information
?
-
-
ATP-diphosphate exchange reaction is activated by cinnamate, dihydro-4-coumarate, caprylate and malonate
-
-
?
additional information
?
-
isoform 4CL10 has no catalytic activity toward hydroxycinnamic acid compounds
-
-
?
additional information
?
-
isoform 4CL10 has no catalytic activity toward hydroxycinnamic acid compounds
-
-
?
additional information
?
-
isoform 4CL10 has no catalytic activity toward hydroxycinnamic acid compounds
-
-
?
additional information
?
-
isoform 4CL7 has no catalytic activity toward hydroxycinnamic acid compounds
-
-
?
additional information
?
-
isoform 4CL7 has no catalytic activity toward hydroxycinnamic acid compounds
-
-
?
additional information
?
-
isoform 4CL7 has no catalytic activity toward hydroxycinnamic acid compounds
-
-
?
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
?
additional information
?
-
sinapate is not accepted as a substrate
-
-
?
additional information
?
-
sinapate is not accepted as a substrate
-
-
?
additional information
?
-
sinapate is not accepted as a substrate
-
-
?
additional information
?
-
sinapate is not accepted as a substrate
-
-
?
additional information
?
-
-
sinapate is not accepted as a substrate
-
-
?
additional information
?
-
4CL has a key role in the biosynthesis of monolignols in softwood species
-
-
?
additional information
?
-
-
4CL has a key role in the biosynthesis of monolignols in softwood species
-
-
?
additional information
?
-
no activity with ferulate, 5-hydroxyferylate, and sinapate
-
-
?
additional information
?
-
-
no activity with ferulate, 5-hydroxyferylate, and sinapate
-
-
?
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
inactive against sinapic acid
-
?
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
?
additional information
?
-
isozyme Pl4CL2 has a broader substrate specificity than Pl4CL1
-
-
?
additional information
?
-
isozyme Pl4CL2 has a broader substrate specificity than Pl4CL1
-
-
?
additional information
?
-
-
isozyme Pl4CL2 has a broader substrate specificity than Pl4CL1
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate
-
-
?
additional information
?
-
-
no activity with sinapate
-
-
?
additional information
?
-
no activity with sinapate, ferulate and caffeate
-
-
?
additional information
?
-
no activity with sinapate, ferulate and caffeate
-
-
?
additional information
?
-
-
no activity with sinapate, ferulate and caffeate
-
-
?
additional information
?
-
-
most of angiosperm and gymnosperm enzymes are active with ferulate but not with sinapoate (?). The enzymes of Erythrina crista-galli, Robinia pseudoacacia and bamboo show considerable activity with sinapoate
-
-
?
additional information
?
-
-
the isoform 4CL1 has a strong substrate preference for p-coumarate, but lacked the activity for ferulate and sinapate. The other hand, 4CL2 and 4CL3 display activity towards sinapate and also possess high activity towards caffeate as well as p-coumarate
-
-
?
additional information
?
-
the enzyme does not activate sinapate, 2,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, acetylsalicylic acid, anthranilic acid, and (N-methyl)anthranilic acid
-
-
?
additional information
?
-
the enzyme does not activate sinapate, 2,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, acetylsalicylic acid, anthranilic acid, and (N-methyl)anthranilic acid
-
-
?
additional information
?
-
the enzyme does not activate sinapate, 2,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, acetylsalicylic acid, anthranilic acid, and (N-methyl)anthranilic acid
-
-
?
additional information
?
-
the enzyme does not activate sinapate, 2,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, acetylsalicylic acid, anthranilic acid, and (N-methyl)anthranilic acid
-
-
?
additional information
?
-
-
the enzyme performs synthesis of (5,7-dihydroxy-4-chromanone)-propenoic acid in concert with chalcone synthase, chalcone isomerase, and flavanone 3-hydroxylase, fed with a number of aromatic acrylic acids, mechanism, overview
-
-
?
additional information
?
-
no activity with benzoate and sinapate
-
-
?
additional information
?
-
no activity with benzoate and sinapate
-
-
?
additional information
?
-
no activity with benzoate and sinapate
-
-
?
additional information
?
-
-
no activity with benzoate and sinapate
-
-
?
additional information
?
-
-
three key enzymes: phenylalanine ammonia-lyase, cinnamate-4-hydroxylase, and 4-coumarate-coenzyme A ligase, catalyzing the biosynthesis of these compounds during berry development, contents of gallic, protocatechuic, gentisic and caffeic acid all change drastically during berry development, while other compounds containing 4-hydroxybenzoic, vanillic, syringic, chlorogenic, 4-coumaric, ferulic and sinapic acid vary only slightly
-
-
?
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0.23
3,4,5-trimethoxycinnamate
-
isoenzyme 1
0.049 - 0.55
3,4-dimethoxycinnamate
0.336
3-methoxcinnamate
-
-
-
0.0009 - 0.6149
4-coumarate
0.246
4-coumaric acid
-
-
0.38
4-methoxycinnamate
-
isoenzyme 1
0.5
4-methoxyferulate
-
-
0.012 - 0.34
5-hydroxyferulate
0.064
adenosine 5'-tetraphosphate
-
reverse reaction, M293P/K320L mutant enzyme, pH 7.0, 30°C
0.253 - 0.4418
dihydro-4-coumarate
0.69
p-methoxycinnamate
-
-
1.32
sinapinate
wild type enzyme, at pH 7.5 and 25°C
0.02576 - 0.664
trans-cinnamate
additional information
additional information
-
0.09
2-coumarate
-
isoenzyme 2
0.18
2-coumarate
-
isoenzyme 1
0.049
3,4-dimethoxycinnamate
-
4CL1
0.083
3,4-dimethoxycinnamate
-
0.55
3,4-dimethoxycinnamate
-
-
0.028
3-coumarate
-
-
0.03
3-coumarate
-
isoenzyme 2
0.0009
4-coumarate
mutant enzyme K443A, at pH 7.5 and 25°C
0.0015
4-coumarate
wild type enzyme, at pH 7.5 and 25°C
0.00166
4-coumarate
pH 7.5, 30°C
0.0025
4-coumarate
pH 7.5, 22°C
0.0029
4-coumarate
mutant enzyme T193A, at pH 7.5 and 25°C
0.0031
4-coumarate
isozyme 4CL2, at pH 7.8 and 32°C
0.0035
4-coumarate
pH 7.8, 22°C
0.0036
4-coumarate
-
4CL2, pH 7.5, 30°C
0.0036
4-coumarate
-
recombinant F269L/K415T, pH 7.8, 30°C
0.0039
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.004
4-coumarate
recombinant isozyme 4CL1
0.0049
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.0049
4-coumarate
-
recombinant V186I/V187L, pH 7.8, 30°C
0.0051
4-coumarate
-
recombinant V186G, pH 7.8, 30°C
0.0051
4-coumarate
mutant enzyme T336A, at pH 7.5 and 25°C
0.0055
4-coumarate
isozyme 4CL1, pH 7.8, 32°C
0.0069
4-coumarate
mutant enzyme Y239F, at pH 7.5 and 25°C
0.0073
4-coumarate
pH 7.5, 22°C
0.00747
4-coumarate
-
recombinant wild-type enzyme, pH 7.8, 30°C
0.009
4-coumarate
pH 7.5, 22°C
0.0091
4-coumarate
pH 7.8, 22°C
0.01
4-coumarate
-
isoenzyme II
0.0103
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0104
4-coumarate
-
recombinant F239S, pH 7.8, 30°C
0.01097
4-coumarate
isoform 4CL3, pH and temperature not specified in the publication
0.0119
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.01271
4-coumarate
isoform 4CL2, pH and temperature not specified in the publication
0.013
4-coumarate
-
isoenzyme III
0.0139
4-coumarate
mutant enzyme K197A, at pH 7.5 and 25°C
0.016
4-coumarate
recombinant isozyme 4CL2
0.0168
4-coumarate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.017
4-coumarate
-
isoenzyme 2
0.017
4-coumarate
-
5-hydroxyferulate
0.0179
4-coumarate
-
recombinant Q274H, pH 7.8, 30°C
0.022
4-coumarate
-
M293P/K320L mutant enzyme
0.023
4-coumarate
room temperature
0.025
4-coumarate
-
4CL1, pH 7.8, room temperature
0.02611
4-coumarate
isoform 4CL4, pH and temperature not specified in the publication
0.027
4-coumarate
-
M293P/K320L mutant enzyme, pH 7.0, 30°C
0.0272
4-coumarate
isoform 4CL5, pH and temperature not specified in the publication
0.029
4-coumarate
recombinant isozyme 4CL3
0.0302
4-coumarate
isoform 4CL1, pH and temperature not specified in the publication
0.032
4-coumarate
-
isoenzyme 1
0.038
4-coumarate
room temperature
0.042
4-coumarate
-
isoenzyme I
0.05399
4-coumarate
isoform 4CL3, pH and temperature not specified in the publication
0.056
4-coumarate
-
4CL1, pH 7.5, 30°C
0.05679
4-coumarate
isoform 4CL1, pH and temperature not specified in the publication
0.08
4-coumarate
-
room temperature
0.103
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.136
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.143
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.1434
4-coumarate
mutant enzyme H237A, at pH 7.5 and 25°C
0.155
4-coumarate
mutant enzyme M247Y, at pH 7.5 and 30°C
0.1887
4-coumarate
wild type enzyme, at pH 7.5 and 30°C
0.212
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.22
4-coumarate
-
4CL2, pH 7.8, room temperature
0.2281
4-coumarate
mutant enzyme Y239A, at pH 7.5 and 25°C
0.233
4-coumarate
-
wild-type enzyme
0.233
4-coumarate
-
wild-type enzyme, pH 7.0, 30°C
0.252
4-coumarate
room temperature
0.282
4-coumarate
pH not specified in the publication, 30°C, isozyme Os4Cl3
0.283
4-coumarate
mutant enzyme M247Y/A251S, at pH 7.5 and 30°C
0.389
4-coumarate
mutant enzyme A251S, at pH 7.5 and 30°C
0.5207
4-coumarate
mutant enzyme M344A, at pH 7.5 and 25°C
0.6149
4-coumarate
mutant enzyme R435A, at pH 7.5 and 25°C
0.012
5-hydroxyferulate
-
isoenzyme 1
0.12
5-hydroxyferulate
-
isoenzyme 2
0.34
5-hydroxyferulate
-
-
0.004
ATP
-
wild-type enzyme, pH 7.0, 30°C
0.029
ATP
-
K457S mutant enzyme
0.151
ATP
-
K211S mutant enzyme
0.17
ATP
-
3-coumarate, , isoenzyme 1
0.173
ATP
-
C403 mutant enzyme
0.24
ATP
-
E401Q mutant enzyme
1.507
ATP
-
R449Q mutant enzyme
0.0009
caffeate
pH 7.5, 22°C
0.001
caffeate
wild type enzyme, at pH 7.5 and 25°C
0.00494
caffeate
pH 7.5, 30°C
0.005
caffeate
-
K457S mutant enzyme
0.0058
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0068
caffeate
pH 7.5, 22°C
0.0109
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.011
caffeate
room temperature
0.0125
caffeate
pH 7.5, 22°C
0.014
caffeate
-
isoenzyme 2
0.014
caffeate
-
2-coumarate
0.014
caffeate
-
K211S mutant enzyme
0.0149
caffeate
pH 7.8, 22°C
0.018
caffeate
-
C403A mutant enzyme
0.02
caffeate
room temperature
0.022
caffeate
-
wild-type enzyme
0.024
caffeate
wild type enzyme
0.024
caffeate
-
wild type
0.024
caffeate
-
wild-type enzyme, pH 7.0, 30°C
0.025
caffeate
30°C, pH 7.0
0.025
caffeate
recombinant isozyme 4CL1
0.0261
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.02631
caffeate
isoform 4CL3, pH and temperature not specified in the publication
0.02643
caffeate
isoform 4CL5, pH and temperature not specified in the publication
0.0276
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.028
caffeate
-
E401Q mutant enzyme
0.0293
caffeate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0296
caffeate
isoform 4CL1, pH and temperature not specified in the publication
0.035
caffeate
-
4CL1, pH 7.5, 30°C
0.037
caffeate
isozyme 4CL2, at pH 7.8 and 32°C
0.04
caffeate
-
isoenzyme 1
0.041
caffeate
-
M293P/K320L mutant enzyme
0.042
caffeate
-
4CL2, pH 7.5, 30°C
0.0423
caffeate
isoform 4CL3, pH and temperature not specified in the publication
0.04414
caffeate
isoform 4CL4, pH and temperature not specified in the publication
0.045
caffeate
recombinant isozyme 4CL2
0.048
caffeate
-
M293P/K320L mutant enzyme, pH 7.0, 30°C
0.0484
caffeate
isozyme 4CL1, pH 7.8, 32°C
0.06132
caffeate
isoform 4CL2, pH and temperature not specified in the publication
0.08417
caffeate
isoform 4CL1, pH and temperature not specified in the publication
0.154
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.1929
caffeate
mutant enzyme M247Y, at pH 7.5 and 30°C
0.2089
caffeate
wild type enzyme, at pH 7.5 and 30°C
0.234
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.262
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.282
caffeate
pH not specified in the publication, 30°C, isozyme Os4Cl3
0.374
caffeate
room temperature
0.4
caffeate
-
R449Q mutant enzyme
0.725
caffeate
recombinant isozyme 4CL3
0.0094
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.0157
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.021
cinnamate
pH 7.5, 22°C
0.0217
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.023
cinnamate
pH 7.5, 22°C
0.0282
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.033
cinnamate
pH 7.5, 22°C
0.037
cinnamate
isozyme 4CL2, at pH 7.8 and 32°C
0.05
cinnamate
recombinant isozyme 4CL1
0.0544
cinnamate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.059
cinnamate
isozyme 4CL1, pH 7.8, 32°C
0.064
cinnamate
recombinant isozyme 4CL3
0.066
cinnamate
recombinant isozyme 4CL2
0.07366
cinnamate
isoform 4CL3, pH and temperature not specified in the publication
0.13571
cinnamate
isoform 4CL5, pH and temperature not specified in the publication
0.14266
cinnamate
isoform 4CL1, pH and temperature not specified in the publication
0.19649
cinnamate
isoform 4CL2, pH and temperature not specified in the publication
0.20002
cinnamate
isoform 4CL4, pH and temperature not specified in the publication
0.292
cinnamate
-
M293P/K320L mutant enzyme, pH 7.0, 30°C
0.8875
cinnamate
isoform 4CL3, pH and temperature not specified in the publication
1.048
cinnamate
-
room temperature
1.0803
cinnamate
isoform 4CL1, pH and temperature not specified in the publication
1.3
cinnamate
-
isoenzyme 1
2.07
cinnamate
room temperature
4.5
cinnamate
-
isoenzyme 2
6.32
cinnamate
room temperature
6.35
cinnamate
-
wild-type enzyme, pH 7.0, 30°C
6.63
cinnamate
room temperature
0.0032
CoA
-
-
0.004
CoASH
-
isoenzyme 2
0.007
CoASH
-
isoenzyme 1
0.253
dihydro-4-coumarate
mutant enzyme M247Y, at pH 7.5 and 30°C
0.4418
dihydro-4-coumarate
wild type enzyme, at pH 7.5 and 30°C
0.0009
ferulate
pH 7.5, 22°C
0.0022
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2
0.0029
ferulate
wild type enzyme, at pH 7.5 and 25°C
0.00302
ferulate
pH 7.5, 30°C
0.0035
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl3
0.0046
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4
0.0054
ferulate
pH 7.5, 22°C
0.00609
ferulate
-
recombinant wild-type enzyme, pH 7.8, 30°C
0.0069
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.0083
ferulate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1
0.009
ferulate
-
isoenzyme 1
0.0106
ferulate
-
recombinant F269L/K415T, pH 7.8, 30°C
0.011
ferulate
-
isoenzyme II
0.0119
ferulate
-
recombinant F239S, pH 7.8, 30°C
0.0142
ferulate
-
recombinant V186G, pH 7.8, 30°C
0.015
ferulate
-
isoenzyme III
0.02
ferulate
-
ferulate, , isoenzyme I
0.02699
ferulate
isoform 4CL4, pH and temperature not specified in the publication
0.03
ferulate
-
M293P/K320L mutant enzyme
0.03516
ferulate
isoform 4CL5, pH and temperature not specified in the publication
0.0353
ferulate
-
recombinant Q274H, pH 7.8, 30°C
0.04217
ferulate
isoform 4CL1, pH and temperature not specified in the publication
0.046
ferulate
-
M293P/K320L mutant enzyme, pH 7.0, 30°C
0.05
ferulate
pH 7.5, 22°C
0.0522
ferulate
isoform 4CL1, pH and temperature not specified in the publication
0.057
ferulate
-
4CL1, pH 7.8, room temperature
0.06868
ferulate
isoform 4CL2, pH and temperature not specified in the publication
0.073
ferulate
recombinant isozyme 4CL2
0.079
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.08261
ferulate
isoform 4CL3, pH and temperature not specified in the publication
0.0849
ferulate
isoform 4CL3, pH and temperature not specified in the publication
0.0884
ferulate
pH 7.8, 22°C
0.102
ferulate
-
room temperature
0.112
ferulate
-
4CL1, pH 7.5, 30°C
0.13
ferulate
-
isoenzyme 2
0.139
ferulate
-
4CL2, pH 7.5, 30°C
0.166
ferulate
room temperature
0.18
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.187
ferulate
recombinant isozyme 4CL1
0.199
ferulate
room temperature
0.309
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.38
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl3
0.384
ferulate
pH not specified in the publication, 30°C, isozyme Os4Cl1
0.8
ferulate
recombinant isozyme 4CL3
0.026
isoferulate
-
-
0.1
isoferulate
-
3,4-dimethoxycinnamate, , isoenzyme 1
0.15
isoferulate
-
isoenzyme 2
0.005
sinapate
-
4CL1
0.0589
sinapate
pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5
0.001
sinapoate
-
-
0.011
sinapoate
-
isoenzyme 1
0.022
sinapoate
-
isoenzyme I
0.02576
trans-cinnamate
pH 7.5, 30°C
0.141
trans-cinnamate
pH 7.8, 22°C
0.664
trans-cinnamate
pH 7.8, 22°C
additional information
additional information
Km values for all mutant enzymes given
-
additional information
additional information
-
Km values for all mutant enzymes given
-
additional information
additional information
-
kinetics in presence of inhibitors
-
additional information
additional information
-
catalytic reaction scheme and kinetics, overview
-
additional information
additional information
kinetic analysis of the recombinant engineered isozyme At4CL1-VvSTS fusion enzyme, overview
-
additional information
additional information
-
kinetic analysis of the recombinant engineered isozyme At4CL1-VvSTS fusion enzyme, overview
-
additional information
additional information
steady-state MichaelisMenten kinetics
-
additional information
additional information
steady-state MichaelisMenten kinetics
-
additional information
additional information
steady-state MichaelisMenten kinetics
-
additional information
additional information
-
steady-state MichaelisMenten kinetics
-
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evolution
in rice, Os4CL2 belongs to the same clade as type II 4CLs in dicots, while the rest of the 4CLs (Os4CL1/3/4/5) belongs to a separate cluster, named type III, which is distinct from the lignin-associated type I 4CLs found in dicots
evolution
isozyme Pl4CL1 belongs to the class II 4-coumarate-CoA ligases
evolution
isozyme Pl4CL2 belongs to the class I 4-coumarate-CoA ligases
evolution
phylogenetically, isozymes Sa4CL1 and Sa4CL2 belong to the class I cluster and Sa4CL3 groups in the class II cluster
evolution
the enzyme belongs to the class II 4-coumarate-CoA ligases
evolution
the enzyme belongs to the class II 4-coumarate-CoA ligases
evolution
the enzyme belongs to the class II 4-coumarate-CoA ligases
evolution
the enzyme belongs to the proteins containing the GEICIRG motif, phylogeny based on AMP-dependent synthetase/ligase domain sequences, overview
evolution
-
the enzyme is a type I 4CL, phylogenetic analysis
evolution
-
the enzyme belongs to the class II 4-coumarate-CoA ligases
-
evolution
-
the enzyme belongs to the class II 4-coumarate-CoA ligases
-
malfunction
a significant reduction in the expression levels is observed for OB4CL_ctg4-related transcripts in suppressed trichome compared with transcripts similar to the other four isoforms, OB4CL_ctg1, 2, 3 and 5
malfunction
suppression of Os4CL3 expression results in significant lignin reduction, shorter plant growth, and other morphological changes. 4CL-suppressed transgenics also display decreased panicle fertility, which may be attributed to abnormal anther development as a result of disrupted lignin synthesis, isozyme Os4Cl3 suppressed phenotype, overview
malfunction
transient RNAi suppression of OS4CL in leaves causes a reduction in leaf eugenol content and trichome transcript level, with a considerable increase in endogenous 4-coumaric, ferulic, trans-cinnamic and caffeic acids, but no significant effect of OS4CL suppression on the total lignin content
malfunction
-
growth reduction is observed when the enzyme gene expression is inhibited by more than 70%
malfunction
loss of isoform 4CL1 leads to reduction in lignin content but no growth defect
malfunction
-
a significant reduction in the expression levels is observed for OB4CL_ctg4-related transcripts in suppressed trichome compared with transcripts similar to the other four isoforms, OB4CL_ctg1, 2, 3 and 5
-
malfunction
-
transient RNAi suppression of OS4CL in leaves causes a reduction in leaf eugenol content and trichome transcript level, with a considerable increase in endogenous 4-coumaric, ferulic, trans-cinnamic and caffeic acids, but no significant effect of OS4CL suppression on the total lignin content
-
metabolism
4-coumarate:CoA ligases are a group of essential enzymes involved in the phenylpropanoid-derived compound pathway, which converts hydroxylated cinnamic acids into their corresponding thioesters. The PDC pathway as well as its branch pathways generates various classes of secondary compounds, including lignin, flavones, flavonols, anthocyanins, isoflavonoids, and furanocoumarins
metabolism
key enzyme in the phenylpropanoid metabolic pathways for monolignol and flavonoid biosynthesis
metabolism
the enzyme is involved in the biosynthetic pathway of eugenol/chavicol synthesis in Ocimum sanctum, overview
metabolism
the enzyme is involved in the flavonoid biosynthesis from cinnamic acid, it is the last enzyme of the general phenylpropanoid pathway, overview
metabolism
the enzyme is involved in the reduction of the carbon-carbon double bond of phenylacrylates such as caffeate. The overall reaction is coupled to ATP synthesis by a chemiosmotic mechanism with Na+ as the coupling ion
metabolism
isoform 4CL3 plays an important role in flavonoid biosynthesis
metabolism
-
the enzyme is involved in the biosynthetic pathway of eugenol/chavicol synthesis in Ocimum sanctum, overview
-
physiological function
isozyme Pl4CL1 might play a role in isoflavone biosynthesis
physiological function
isozyme Pl4CL2 might function as a housekeeping enzyme concerning lignification
physiological function
metabolite channeling of intermediates towards eugenol by a specific 4-coumarate:CoA ligase and involvement of the enzyme in creation of virtual compartments through substrate utilization and committing metabolites for eugenol biosynthesis at an early stage of the pathway, overview
physiological function
Os4CL3 may play a role in the synthesis of lignin as well as other phenolic compounds
physiological function
Sorbus aucuparia cell cultures accumulate biphenyl and dibenzofuran phytoalexins from the starter substrate benzoyl-CoA in response to elicitor treatment involving cinnamate:CoA ligase and benzoate:CoA ligase, but not 4-coumarate:CoA ligase
physiological function
the enzyme is a key regulatory enzyme of the phenylpropanoid pathway that regulates the activation of cinnamic acid, leading to the synthesis of flavonoids and lignin
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of flavonoids
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of flavonoids. Isozyme Os4Cl shows potential involvement in flavonoid formation
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of lignin
physiological function
the isozyme catalyzes the conversion of hydroxycinnamates into corresponding CoA esters for biosynthesis of lignin, 4-coumaric acid and ferulic acid are the two main substrates of the enzyme for monolignol biosynthesis in rice
physiological function
isoform 4CL1 is required for wild type levels of lignin biosynthesis
physiological function
-
metabolite channeling of intermediates towards eugenol by a specific 4-coumarate:CoA ligase and involvement of the enzyme in creation of virtual compartments through substrate utilization and committing metabolites for eugenol biosynthesis at an early stage of the pathway, overview
-
additional information
-
putative substrate binding residues are I196, Y197, G317, G343, P349, V350, and L351
additional information
putative substrate binding residues are I196, Y197, G317, G343, P349, V350, and L351
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
-
rice 4CL isoforms display different substrate specificities and catalytic turnover rates
additional information
the enzyme has two conserved putative AMP-binding motifs, the SSGTTGLPKGV and GEICIRG domains
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
-
the existence of a valine residue at the substrate-binding pocket may mainly affect rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
additional information
-
the existence of a valine residue at the substrate-binding pocket may mainly affect the rice enzyme activity toward sinapic acid. The amino acid sequence similarities within the Os4CL gene family share a percentage of identity between 56% and 84%, positions of the four introns in these genes are conserved, but the introns differ in length and sequence, sequence comparisons of rice isozymes, overview
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C403A
-
activity reduced to 45% of wild-type level, no effect on Km values for ATP and caffeate
E401Q
-
activity reduced to 21% of wild-type level, no effect on Km values for ATP and caffeate
K211S
-
activity reduced to 2.7% of wild-type level
K320A
new substrate specificity, accepts ferulate as substrate
K320L
new substrate specificity, accepts ferulate as substrate
K445T
-
activity reduced to 0.2% of wild-type level
K457S
-
activity reduced to 4% of wild-type level
L356A
-
only little effect on activity
M293A
new substrate specificity, accepts ferulate as substrate
M293A/V294L
substitution of valine decreases Km for ferulate 2-3fold compared to single methionine substitution mutant
M293F
no reaction with ferulate, increases Km for caffeate
M293P
new substrate specificity, accepts ferulate as substrate
M293P/V294M
substitution of valine decreases Km for ferulate 2-3fold compared to single methionine substitution mutant
M293W
no reaction with ferulate
M293Y
no reaction with ferulate, increases Km for caffeate
N256A/M293P/K320L
-
effectively uses ferulate and cinnamate as substrates, 10fold reduced activity with caffeate
R449Q
-
activity reduced to 3% of wild-type level, Km values significantly increased
V294L
slightly reduced activity with caffeate, no activity with ferulate
V294M
slightly reduced activity with caffeate, no activity with ferulate
V355A
-
strongly reduced activity
V355A/L356A
-
strongly reduced activity
E340A
-
4CL1-mutant, activity almost completely abolished
G333A
-
4CL1-mutant, activity almost completely abolished
G337A
-
4CL1-mutant, activity almost completely abolished
G342A
-
4CL1-mutant, activity almost completely abolished
I346A
-
4CL1-mutant, very low activity with all substrates
L344A
-
4CL1-mutant, activity almost completely abolished
M338A
-
4CL1-mutant, activity almost completely abolished
M348A
-
4CL1-mutant, activity almost completely abolished
P285A
-
4CL1-mutant, very low activity with all substrates
P286A
-
4CL1-mutant, minor changes in activity
P343A
-
4CL1-mutant, very low activity with all substrates
Q334A
-
4CL1-mutant, very low activity with all substrates
T331A
-
4CL1-mutant, minor changes in activity
T339A
-
4CL1-mutant, activity almost completely abolished
V284A
-
4CL1-mutant, minor changes in activity
Y336A
-
4CL1-mutant, activity almost completely abolished
H237A
the mutant shows reduced activity compared to the wild type enzyme
K197A
the mutant shows reduced activity compared to the wild type enzyme
K443A
the mutant shows reduced activity compared to the wild type enzyme
M344A
the mutant shows reduced activity compared to the wild type enzyme
R435A
the mutant shows reduced activity compared to the wild type enzyme
T193A
the mutant shows reduced activity compared to the wild type enzyme
T336A
the mutant shows reduced activity compared to the wild type enzyme
Y239A
the mutant shows reduced activity compared to the wild type enzyme
Y239F
the mutant shows reduced activity compared to the wild type enzyme
A251S
the mutant enzyme shows a lower binding affinity and catalytic efficiency than the wild type enzyme
A251S/M247Y
the mutant enzyme shows a lower binding affinity and catalytic efficiency than the wild type enzyme
M247Y
the catalytic efficiency of, 4-coumaric, caffeic and dihydro-4-coumaric acids are higher in the mutant than in the wild type enzyme
V388del
deletion of V338 residues in isoform 4CL1 results in activity towards sinapate
Y236F
the mutant of isoform 4CL2 exhibits high substrate catalytic efficiency for 4-coumarate but very low substrate affinities and specificities for caffeate and ferulate
F239A
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
F239N
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
F239R
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
F239S
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme. The mutant strain produces more naringenin chalcone compared to the wild-type
F269G
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
F269I
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
F269L
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type, loss of feedback inhibition by naringenin
F269L/K415T
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme
F269V
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
Q274E
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
Q274G
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
Q274H
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme, loss of feedback inhibition by naringenin, the mutant strain produces more naringenin chalcone compared to the wild-type
Q274S
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
V186A
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
V186G
-
site-directed mutagenesis, the mutant shows highly increased activity in vivo, and in vitro with coumaric acid, but reduced activity with ferulic acid compared to the wild-type enzyme. The mutant strain produces highly increased naringenin chalcone content compared to the wild-type
V186I
-
site-directed mutagenesis, the mutant strain produces highly increased naringenin chalcone content compared to the wild-type
V186I/V187L
-
site-directed mutagenesis, the mutant shows increased activity in vivo, and in vitro with coumaric acid compared to the wild-type enzyme, but no activity with ferulic acid
V186L
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
V235M/A325G
-
site-directed mutagenesis, highly unstable inactive mutant
M293P/K320L
-
effectively uses ferulate as substrate, changes in Km for all substrates
M293P/K320L
-
strongly affects Km for all substrates, capable in using ferulate, capable in adenosine 5'-tetraphosphate formation at 10fold higher rate than wild type enzyme
Q274D
-
site-directed mutagenesis, the mutant strain produces less naringenin chalcone compared to the wild-type
Q274D
-
site-directed mutagenesis, the mutant strain produces more naringenin chalcone compared to the wild-type
additional information
-
construction of chimeric proteins consisting of fragments of isoforms 4CL1 and 4CL2
additional information
-
domain exchange experiments with gramicidine synthetase from Bacillus brevis
additional information
-
expression of artificial zinc finger chimeras, e.g. transgenic lines expressing chimeras with the KOX/KRAB repression domain or the VP16 activation domain, regulates the enzyme in positive and negative manner, repression of gene 4CL1 results in reduced lignin production and severely diminished lignin distribution, while enzyme upregulation causes an increase in lignin content and ectopic lignin distribution by plant stems
additional information
-
generation of ethyl methyl sulfate mutagenized populations of At4CL1-GUS and At4CL2-GUS transgenic lines, DNA methylation of the proximal promoter sequences of the transgene only in the mutant lines, while silencing in the seedlings of the At4CL1-GUS lines is root-specific in seedlings, it affects all organs in the At4CL2-GUS lines, analysis of endogenous 4CL expression in epimutant lines, and phenotype analysis, overview
additional information
the engineered fusion protein of Arabidopsis thaliana At4CL1 and Vitis vinifera stilbene synthase VvSTS shows 15fold increased resveratrol levels relative to yeast expressing the individual enzymes, but only less than 3fold increased 4-coumaroyl-CoA ligase or stilbene synthase activities compared to the wild-type enzymes. Co-localization of the two enzyme active sites within 70 A of each other provides the basis for enhanced in vivo synthesis of resveratrol
additional information
-
the engineered fusion protein of Arabidopsis thaliana At4CL1 and Vitis vinifera stilbene synthase VvSTS shows 15fold increased resveratrol levels relative to yeast expressing the individual enzymes, but only less than 3fold increased 4-coumaroyl-CoA ligase or stilbene synthase activities compared to the wild-type enzymes. Co-localization of the two enzyme active sites within 70 A of each other provides the basis for enhanced in vivo synthesis of resveratrol
additional information
-
construction of hybrid enzymes using different portions of isoforms 4CL1-4CL3, some of the constructed proteins were found to be inactive
additional information
transient silencing of the OS4CL gene in planta by RNA interference
additional information
-
transient silencing of the OS4CL gene in planta by RNA interference
additional information
-
transient silencing of the OS4CL gene in planta by RNA interference
-
additional information
-
interactions of the Q274H mutation with other mutants, overview
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Barillas, W.; Beerhues, L.
3-Hydroxybenzoate:coenzyme A ligase and 4-coumarate:coenzyme A ligase from cultured cells of Centaurium erythraea
Planta
202
112-116
1997
Centaurium erythraea
brenda
Meng, H.; Campbell, W.H.
Facile enzymic synthesis of caffeoyl CoA
Phytochemistry
44
605-608
1997
Populus sp.
-
brenda
Becker-Andre, M.; Schulze-Lefert, P.; Hahlbrock, K.
Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate:CoA ligase genes in potato
J. Biol. Chem.
266
8551-8559
1991
Solanum tuberosum
brenda
Zhang, X.H.; Chiang, V.L.
Molecular cloning of 4-coumarate:coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood
Plant Physiol.
113
65-74
1997
Pinus taeda
brenda
Kajita, S.; Katayama, Y.; Omori, S.
Alterations in the biosynthesis of lignin in transgenic plants with chimeric genes for 4-coumarate:coenzyme A ligase
Plant Cell Physiol.
37
957-965
1996
Nicotiana tabacum
brenda
Uhlmann, A.; Ebel, J.
Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an enzyme involved in the resistance response of soybean (Glycine max L.) against pathogen attack
Plant Physiol.
102
1147-1156
1993
Glycine max
brenda
Lee, D.; Douglas, C.J.
Two divergent members of a tobacco 4-coumarate:coenzyme A ligase (4CL) gene family. cDNA structure, gene inheritance and expression, and properties of recombinant proteins
Plant Physiol.
112
193-205
1996
Nicotiana tabacum
brenda
Yazaki, K.; Tabata, M.
Isolation and characterization of two cDNAs encoding 4-coumarate:CoA ligase in Lithospermum cell culture
Plant Cell Physiol.
36
1319-1329
1995
Lithospermum erythrorhizon
brenda
Liu, Q.; Bonness, M.S.; Liu, M.; Seradge, E.; Dixon, R.A.; Mabry, T.J.
Enzymes of B-ring-deoxy flavonoid biosynthesis in elicited cell cultures of "old man" cactus (Cephalocereus senilis)
Arch. Biochem. Biophys.
321
397-404
1995
Cephalocereus senilis
brenda
Lee, D.; Ellard, M.; Wanner, L.A.; Davis, K.R.; Douglas, C.J.
The Arabidopsis thaliana 4-coumarate: CoA ligase (4CL) gene: stress and developmentally regulated expression and nucleotide sequence of its cDNA
Plant Mol. Biol.
28
871-884
1995
Arabidopsis thaliana
brenda
Voo, K.S.; Whetten, R.W.; O'Malley, D.M.; Sederoff, R.R.
4-Coumarate:coenzyme A ligase from loblolly pine xylem. Isolation characterization, and complementary DNA cloning
Plant Physiol.
108
85-97
1995
Pinus taeda
brenda
Lindl, T.; Kreuzaler, F.; Hahlbrock, K.
Synthesis of p-coumaryl coenzyme A with a partially purified p-coumarate:CoA ligase from cell suspension cultures of soybean (Glycine max)
Biochim. Biophys. Acta
302
457-464
1973
Glycine max
brenda
Gross, G.G.; Zenk, M.H.
Isolation and properties of hydroxycinnamate:CoA ligase from lignifying tissues of Forsythia
Eur. J. Biochem.
42
453-459
1974
Forsythia suspensa
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