title: Kinetics of inactivation of Penaeus penicillatus acid phosphatase during inhibition by N-bromosuccinimide.
abstract: In the present investigation, the inactivation by N-bromosuccinimide of acid phosphatase from penaeus penicillatus has been studied using the kinetic method of the substrate reaction during modification of enzyme activity as previously described by Tsou [(1988, Adv. Enzymemol. Related Areas Mol. Biol. 61, 381-436]. The results show that inactivation of the enzyme by N-bromosuccinimide is a slow, reversible reaction. The results also clearly show that the modification of the tryptophan residues of penaeus penicillatus acid phosphatase by high concentrations of N-bromosuccinimide led to the complete inactivation of the enzyme. The microscopic rate constants were determined for the reaction of the inactivator with the free enzyme and with the enzyme-substrate complex. Comparison of the obtained microscopic rate constants indicates that the presence of the substrate offers marked protection of the enzyme against inactivation by N-bromosuccinimide. The above results suggest that the tryptophan residue is essential for activity and may be situated at the active site of the enzyme.
authors.affiliation: Department of Biology, Xiamen University, People's Republic of China.
authors.forename: P Z
authors.initials: PZ
authors.lastname: Yang
authors.forename: Q X
authors.initials: QX
authors.lastname: Chen
authors.forename: Y
authors.initials: Y
authors.lastname: Li
authors.forename: S L
authors.initials: SL
authors.lastname: Chen
authors.forename: H M
authors.initials: HM
authors.lastname: Zhou
mesh_terms: D000135:Acid Phosphatase / Q000037:antagonists & inhibitors*; D000818:Animals; D001974:Bromosuccinimide / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007700:Kinetics; D033561:Penaeidae / Q000201:enzymology*
chemical_list: D004791:Enzyme Inhibitors; D000135:Acid Phosphatase; D001974:Bromosuccinimide