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The effects of N‐thiophosphoryl amino acids on the activity of green crab (Scylla Serrata) alkaline phosphatase
Author(s) -
Chen QingXi,
Zhu ChunMing,
Zhou HaiMeng,
Lu HaiYan,
Lin HaiNing
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 - 10.1080/15216549800202852
Subject(s) - chemistry , alkaline phosphatase , amino acid , enzyme , hydrolysis , biochemistry , scylla serrata , non competitive inhibition , substrate (aquarium) , biology , ecology
Green crab (Scylla Serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme which catalyzed the nonspecific hydrolysis of phosphate monoesters. In the present paper, the effects of several N‐thiophosphoryl amino acids on the activity of green crab alkaline phosphatase have been studied. The results show that these derivatives of amino acids can lead to reversible inactivation. The equilibrium constants for inhibitors binding with the enzyme and/or the enzyme‐substrate complexes have been determined. The obtained results show that both N‐thiophosphoryl‐Cys and N‐thiophosphoryl‐Glu were non‐competitive inhibitors, while other five N‐thiophosphoryl amino acids were un‐competitive inhibitors. For the un‐competitive inhibitors, the inhibition strength follows the order N‐thiophosphoryl‐Ile>‐Val>‐Lys>‐Ala>‐Tyr. Compared with respective free amino acids, it can be seen that N‐thiophosphorylation of the amino acids increased their inhibition strength except the N‐thiophosphoryl‐Cys.