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Kinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by phenylglyoxal
Author(s) -
Xie WenZhang,
Wang HongRui,
Chen QingXi,
Zhou HaiMeng
Publication year - 1996
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 - 10.1080/15216549600201613
Subject(s) - phenylglyoxal , chemistry , enzyme kinetics , enzyme , alkaline phosphatase , kinetics , substrate (aquarium) , enzyme assay , non competitive inhibition , arginine , active site , biochemistry , stereochemistry , biology , ecology , physics , amino acid , quantum mechanics
The kinetics method of the substrate reaction during modification of enzyme activity previously described by Tsou (Adv. Enzymol. Related. Areas Mol. Biol., 1988, 61, 381‐436) has been applied to study the kinetics of the course of inactivation of green crab alkaline phosphatase by phenylglyoxal. The obtained results shows that the inactivation of the enzyme by phenylglyoxal is a slow reversible reaction. The microscopic rate constants for the reaction of the inhibitor with the enzyme were determined. The presence of substrate offers marked protection of this enzyme against inactivation by phenylglyoxal. The above results suggest that the arginine residue is essential for activity and is situated at the active site of the enzyme.