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Literature summary extracted from

  • Wu, J.; Xu, D.; Lu, X.; Wang, C.; Guo, H.; Dunaway-Mariano, D.
    Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: a combined theoretical and experimental study (2006), Biochemistry, 45, 102-112.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment 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 Comment 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 UniProt Comment Textmining
3.8.1.7 Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.8.1.7 4-chlorobenzoyl-CoA + H2O
-
 Pseudomonas sp. 4-hydroxybenzoyl-CoA + chloride
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment 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.