BRENDA - Enzyme Database

Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: a combined theoretical and experimental study

Wu, J.; Xu, D.; Lu, X.; Wang, C.; Guo, H.; Dunaway-Mariano, D.; Biochemistry 45, 102-112 (2006)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.8.1.7
E232D
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
Pseudomonas sp.
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.8.1.7
0.0037
-
4-chlorobenzoyl-CoA
pH 7.5, 25°C, wild-type enzyme
Pseudomonas sp.
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.8.1.7
Pseudomonas sp.
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.8.1.7
4-chlorobenzoyl-CoA + H2O
-
667699
Pseudomonas sp.
4-hydroxybenzoyl-CoA + chloride
-
-
-
?
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.8.1.7
0.00015
-
4-chlorobenzoyl-CoA
pH 7.5, 25°C, mutant enzyme E232G
Pseudomonas sp.
3.8.1.7
0.6
-
4-chlorobenzoyl-CoA
pH 7.5, 25°C, wild-type enzyme
Pseudomonas sp.
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.8.1.7
E232D
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
Pseudomonas sp.
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.8.1.7
0.0037
-
4-chlorobenzoyl-CoA
pH 7.5, 25°C, wild-type enzyme
Pseudomonas sp.
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.8.1.7
4-chlorobenzoyl-CoA + H2O
-
667699
Pseudomonas sp.
4-hydroxybenzoyl-CoA + chloride
-
-
-
?
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.8.1.7
0.00015
-
4-chlorobenzoyl-CoA
pH 7.5, 25°C, mutant enzyme E232G
Pseudomonas sp.
3.8.1.7
0.6
-
4-chlorobenzoyl-CoA
pH 7.5, 25°C, wild-type enzyme
Pseudomonas sp.