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6.2.1.33: 4-chlorobenzoate-CoA ligase

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

Word Map on EC 6.2.1.33

Reaction

4-Chlorobenzoate
+
CoA
 +
ATP
=
4-chlorobenzoyl-CoA
 +
AMP
 +
diphosphate

Synonyms

4-CB:CoA ligase, 4-CBA:CoA ligase, 4-chlorobenzoate:CoA ligase, 4-Chlorobenzoate:coenzyme A ligase, 4-Chlorobenzoyl-CoA ligase, 4-Chlorobenzoyl-coenzyme A ligase, 4-Halobenzoate-coenzyme A ligase, CBAL, CBL, chlorobenzoate:CoA ligase, Synthetase, 4-chlorobenzoyl coenzyme A

ECTree

     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.33 4-chlorobenzoate-CoA ligase

Engineering

Engineering on EC 6.2.1.33 - 4-chlorobenzoate-CoA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D385A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E410A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F473A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzymem but increased kcat
G408A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H207A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H207F
site-directed mutagenesis,the mutant shows reduced activity compared to the wild-type enzyme
H207Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H254A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K477A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K492A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K492L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K492R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
M203A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N302A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R400A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R439A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R475A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R87A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S407A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T161A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T251A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T306A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T307A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W440A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but increased kcat
Y304F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D402A
100fold decrease in ratio kcat/Km for CoA
D402P
crystallization data. Mutant adopts the proposed adenylate-forming conformation with very little change to the overall structure.The ability of the mutant to catalyze the adenylate-forming half-reaction is reduced by about 3fold, catalysis of the second half-reaction is reduced by 4 orders of magnitude
E306Q
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
G163I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
G166I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
K169M
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
P168A
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
E306Q
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
G163I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
G166I
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
K169M
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-
P168A
-
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
-