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Literature summary for 3.8.1.7 extracted from

  • Yang, G.; Liu, R.Q.; Taylor, K.L.; Xiang, H.; Price, J.; Dunaway-Mariano, D.
    Identification of active site residues essential to 4-chlorobenzoyl-coenzyme A dehalogenase catalysis by chemical modification and site directed mutagenesis (1996), Biochemistry, 35, 10879-10885.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H81Q mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity Pseudomonas sp.
H94Q The mutant enzymes H94Q, H208Q, and W179F have a catalytic activity comparable to the wild-type enzyme Pseudomonas sp.
W137F mutant enzymes H81Q, W137F and H90Q show significant loss in catalytic activity Pseudomonas sp.

Inhibitors

Inhibitors Comment Organism Structure
diethyl dicarbonate activity is fully regained by subsequent treatment with hydroxylamine Pseudomonas sp.
N-bromosuccinimide
-
 Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
 recombinant enzyme expressed in Escherichia coli
-

Reaction

Reaction Comment Organism Reaction ID
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride it is proposed that Asp125 functions as the active site nucleophile, that Trp137 serves as a hydrogen bond donor to the Asp145 carbonyl group , and that His90 serves to deprotonate the bound H2O molecule Pseudomonas sp.
a