Premium
Kinetics of inhibition of penaeus penicillatus acid phosphatase by bromoacetic acid
Author(s) -
Chen QingXi,
Chen SuLi,
Zhou HaiMeng
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203722
Subject(s) - chemistry , enzyme kinetics , acid phosphatase , enzyme , kinetics , histidine , substrate (aquarium) , non competitive inhibition , stereochemistry , organic chemistry , active site , biology , ecology , physics , quantum mechanics
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.