BRENDA - Enzyme Database

QM/MM studies of the enzyme-catalyzed dechlorination of 4-chlorobenzoyl-CoA provide insight into reaction energetics

Xu, D.; Wei, Y.; Wu, J.; Dunaway-Mariano, D.; Guo, H.; Cui, Q.; Gao, J.; J. Am. Chem. Soc. 126, 13649-13658 (2004)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.8.1.7
G113A
mutation significantly increases the barrier by disrupting the hydrogen bond with the Gly114 backbone
Pseudomonas sp.
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.8.1.7
Pseudomonas sp.
A5JTM5
-
-
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
reaction rate is limited by the formation of the Meisenheimer comlex, rather than by its decomposition
669044
Pseudomonas sp.
4-hydroxybenzoyl-CoA + chloride
-
-
-
?
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.8.1.7
G113A
mutation significantly increases the barrier by disrupting the hydrogen bond with the Gly114 backbone
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
reaction rate is limited by the formation of the Meisenheimer comlex, rather than by its decomposition
669044
Pseudomonas sp.
4-hydroxybenzoyl-CoA + chloride
-
-
-
?