A KINETIC STUDY ON IRREVERSIBLE INACTIVITION OF AMINOACYLASE BY PAR
PAR对氨基酰化酶不可逆抑制动力学研究

The kinetic theory of the sulstrate reaction during modification of enzyme activity previously described by Tsou, C.-L. has been used to study the kinetics of the course of removal of Zn2 + from aminoacylase leading to inactivation of enzyme by PAR. The kinetics of the substrate reaction under different concentrations of the substrate chloroacetyl-L-alanine and the inactivator PAR suggest a complex mechanism for inadivation by PAR and substrate competition with PAR at the active site.The initial formation of an enzyme-Zn-PAR complex is a relatively rapid reaction followed by a slow inactivation step which involves probably- a change in conformation of the enzyme.The presence of Zn2+ stabilizes the active site conformation required for enzyme activity.