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Literature summary 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

Protein Variants

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

Inhibitors

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

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.8.1.7 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