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6.2.1.12: 4-coumarate-CoA ligase

This is an abbreviated version!
For detailed information about 4-coumarate-CoA ligase, go to the full flat file.

Word Map on EC 6.2.1.12

Reaction

ATP
+
4-coumarate
 +
CoA
=
AMP
 +
diphosphate
 +
4-coumaroyl-CoA

Synonyms

4-CL, 4-coumarate CoA ligase, 4-coumarate coenzyme A ligase, 4-coumarate/coenzyme A ligase, 4-coumarate: CoA ligase, 4-coumarate: coenzyme A ligase, 4-coumarate:CoA ligase, 4-coumarate:CoA-ligase, 4-coumarate:coenzyme A (CoA) ligase, 4-Coumarate:coenzyme A ligase, 4-coumarate:coenzyme-A ligase-1, 4-coumaroyl CoA ligase, 4-coumaroyl coenzyme A ligase, 4-coumaroyl-CoA ligase, 4-coumaroyl-CoA synthase, 4-coumaroyl:CoA ligase, 4-Coumaryl-CoA synthetase, 4CL, 4CL-A1, 4CL-A2, 4CL-B, 4CL1, 4CL10, 4CL2, 4CL3, 4CL4, 4CL5, 4CL7, Ar4CL, At4CL1, Caffeolyl coenzyme A synthetase, caffeoyl-CoA ligase, caffeoyl-CoA synthetase, caffeoyl-coenzyme A synthetase, CarB, Clone 4CL14, Clone 4CL16, coumarate:CoA ligase, Feruloyl CoA ligase, Feruloyl coenzyme A synthetase, Hc4CL, Hydroxy-cinnamate:CoA ligase, Hydroxycinnamate:CoA ligase, Hydroxycinnamoyl CoA synthetase, LJ4CL1, OB4CL_ctg4, OS4CL, Os4Cl1, Os4Cl2, Os4Cl3, Os4Cl4, Os4Cl5, p-Coumaroyl CoA ligase, p-coumaroyl-CoA ligase, p-Coumaryl coenzyme A synthetase, p-Coumaryl-CoA ligase, p-Coumaryl-CoA synthetase, p-Hydroxycinnamic acid:CoA ligase, p-Hydroxycinnamoyl coenzyme A synthetase, Pc4CL2, Pl4CL1, Pl4CL2, Sa4CL1, Sa4CL2, Sa4CL3, Sinapoyl coenzyme A snthetase, Synthetase, p-coumaroyl coenzyme A, type I 4CL

ECTree

     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.12 4-coumarate-CoA ligase

Engineering

Engineering on EC 6.2.1.12 - 4-coumarate-CoA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
K540N
-
no activity
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/K320L
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
Q274D
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
additional information