%0 Journal Article
%T A KINETIC STUDY ON IRREVERSIBLE INACTIVITION OF AMINOACYLASE BY PAR<br>PAR对氨基酰化酶不可逆抑制动力学研究
%A 张英侠
%A 王希成
%A 周海梦
%J 生物物理学报
%D 1992
%I 
%X 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.
%K 失活动力学
%K 锌
%K 氨基酰化酶
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=6D1F5ACBF151588E70E0AF22DBB5B5BF&yid=F53A2717BDB04D52&vid=5D311CA918CA9A03&iid=CA4FD0336C81A37A&sid=1F199509C0B6C4D6&eid=03A030BB0C519C60&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=3