Kinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by L-cysteine

J Protein Chem. 1999 Jul;18(5):603-7. doi: 10.1023/a:1020611602818.

Abstract

The inhibition of alkaline phosphatase from green crab (Scylla serrata) by L-cysteine has been studied. The results show that L-cysteine gives a mixed-type inhibition. The progress-of-substrate-reaction method previously described by Tsou [(1988), Adv. Enzymol. Related Areas Mol. Biol. 61, 391-436] was used to study the inactivation kinetics of the enzyme by L-cysteine. The microscopic rate constants were determined for reaction of the inhibitor with the free enzyme and the enzyme-substrate complex (ES) The results show that inactivation of the enzyme by L-cysteine is a slow, reversible reaction. Comparison of the inactivation rate constants of free enzyme and ES suggests that the presence of the substrate offers marked protection of this enzyme against inactivation by L-cysteine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / antagonists & inhibitors*
  • Animals
  • Brachyura / enzymology*
  • Cysteine / pharmacology*
  • Enzyme Inhibitors / pharmacology*
  • Kinetics
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Alkaline Phosphatase
  • Cysteine