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Abstract
Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme which catalyzes the nonspecific hydrolysis of phosphate monoesters. The effects of several inhibitors on its activity have been studied. The results show that Na2HPO4, Na2HAsO4 and Na2WO4 are competitive inhibitors, L-phenylalanine is an uncompetitive inhibitor, while L-cysteine is a mixed-type inhibitor. The equilibrium constants were determined for inhibitor binding. The order of potency was Na2HPO4 (K1 = 0.95 mM) > Na2AsO4 (l.10 mM) > Na2WO4 (1.55 mM).