acid-phosphatase and bromoacetate

The kinetics of inhibition of penaeus penicillatus acid phosphatase by bromoacetic acid has been studied. The results show that inhibition of the enzyme by bromoacetic acid is a slow, reversible reaction. The microscopic rate constants for the reaction of inhibitor with the enzyme were determined. The presence of the substrate offers marked protection of this enzyme against inhibition by bromoacetic acid. The above results suggest that the histidine residue is essential for activity and are situated at the active site of the enzyme.

Topics: Acetates; Acid Phosphatase; Animals; Dose-Response Relationship, Drug; Enzyme Inhibitors; Kinetics; Nitrophenols; Organophosphorus Compounds; Penaeidae