3.8.1.7: 4-chlorobenzoyl-CoA dehalogenase
This is an abbreviated version!
For detailed information about 4-chlorobenzoyl-CoA dehalogenase, go to the full flat file.
Word Map on EC 3.8.1.7
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3.8.1.7
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dehalogenation
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4-hydroxybenzoyl-coa
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meisenheimer
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4-hydroxybenzoate
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thioesterase
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4-hba-coa
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raman
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arthrobacter
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dechlorination
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dunaway-mariano
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homotetramer
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expulsion
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pi-electrons
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4-position
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crotonase
- 3.8.1.7
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dehalogenation
- 4-hydroxybenzoyl-coa
-
meisenheimer
- 4-hydroxybenzoate
-
thioesterase
-
4-hba-coa
-
raman
- arthrobacter
-
dechlorination
-
dunaway-mariano
-
homotetramer
-
expulsion
-
pi-electrons
-
4-position
- crotonase
Reaction
Synonyms
4-CBA-CoA dehalogenase, 4-CBCoA dehalogenase, 4-CBS-CoA dehalogenase, 4-chlorobenzoate-CoA-dehalogenase, 4-chlorobenzoate-coenzyme A dehalogenase, 4-chlorobenzoyl CoA dehalogenase, 4-chlorobenzoyl-CoA dehalogenase, 4-chlorobenzoyl-coenzyme A dehalogenase, CHD, dehalogenase, 4-chlorobenzoyl coenzyme A, dehalogenase, 4-chlorobenzoyl coenzyme A (Pseudomonas strain CBS-3 clone pMMB22 reduced), FcbB
ECTree
3.8.1.7 4-chlorobenzoyl-CoA dehalogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.8.1.7 - 4-chlorobenzoyl-CoA dehalogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A112V
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site-directed mutagenesis, overexpression as soluble protein, reduced activity
D145A
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mutant enzymes D145A and H90Q show no catalytic activity, but no effect on ligand binding or the induction of the red shift in the benzoyl ring absorption
D337A
site-directed mutagenesis, the Km for the mutant Chd increases to 0.176 mM, 50% transformation activity compared to the wild-type Chd
E232D
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mutant enzyme binds the substrate analogue 4-methylbenzoyl-CoA more tightly than does the wild-type dehalogenase. The kcat for 4-chlorobenzoyl-CoS conversion to product is reduced 10000fold in the mutant. Increased sibstrate binding, decreased ring polarization, and decreased catalytic efficiency indicate that the repositioning of the point charge in the Glu232Arg mutant might affect the orientation of the Arg145 carboxylate with respect to the aromatic ring
F64A
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site-directed mutagenesis, decreased kcat and slightly increased Km compared to the wild-type enzyme
F64L
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
F64P
F82L
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
G113A
G113N
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G113S
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G114A
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The G114A mutant is strongly inhibited in both substrate binding and activation
H63Q
site-directed mutagenesis, the Km for the mutant Chd increases to 0.154 mM compared to the wild-type
H81Q
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mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity
H90Q
H94Q
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The mutant enzymes H94Q, H208Q, and W179F have a catalytic activity comparable to the wild-type enzyme
R24K
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site-directed mutagenesis, increased kcat and increased Km compared to the wild-type enzyme
R24L
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site-directed mutagenesis, decreased kcat and increased Km compared to the wild-type enzyme
R257K
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site-directed mutagenesis, slightly decreased kcat and slightly increased Km compared to the wild-type enzyme
R257L
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site-directed mutagenesis, decreased kcat and increased Km compared to the wild-type enzyme
R67K
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site-directed mutagenesis, decreased kcat and slightly increased Km compared to the wild-type enzyme
W137F
W89F
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
Y65D
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site-directed mutagenesis, overexpression as soluble protein, slightly reduced activity
F64L
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
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F64P
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
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F82L
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
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G113A
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
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G113S
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
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G114A
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The G114A mutant is strongly inhibited in both substrate binding and activation
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W89F
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The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift
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D337A
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site-directed mutagenesis, the Km for the mutant Chd increases to 0.176 mM, 50% transformation activity compared to the wild-type Chd
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F64P
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site-directed mutagenesis, highly decreased kcat compared to the wild-type enzyme, nearly inactive
F64P
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G113A
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site-directed mutagenesis, decreased kcat and increased Km compared to the wild-type enzyme
G113A
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site-directed mutagenesis, overexpression as soluble protein, highly reduced activity
G113A
mutation significantly increases the barrier by disrupting the hydrogen bond with the Gly114 backbone
H90Q
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mutant enzymes D145A and H90Q show no catalytic activity, but no effect on ligand binding or the induction of the red shift in the benzoyl ring absorption
H90Q
site-directed mutagenesis, exchange of the active site H90, reduced formation of arylated enzyme intermediate, and 154fold reduction of arylated enzyme intermediate hydrolysis, active site structure
W137F
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mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity
