邻苯二醛修饰过程中肌酸激酶不可逆抑制动力学。

Enzyme & protein Pub Date : 1994-01-01 DOI:10.1159/000474963
Z F Wang, Y K Xu, H M Zhou
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引用次数: 3

摘要

以前有报道说,由邻苯二醛(OPTA)和肌酸激酶活性位点或附近的巯基和氨基形成的荧光探针,在分子整体展开之前,探针的失活和暴露同时发生。在本研究中,比较了纯化兔肌肌酸激酶的OPTA失活和修饰动力学,前者通过在先前描述的失活剂存在下的底物反应进行。测定了失活剂与游离酶和酶-底物配合物反应的微观速率常数。从得到的结果来看,OPTA对两种底物都是非竞争性的。OPTA的失活动力学是单相的,ATP和肌酸都不影响酶的失活速率常数,表明OPTA对肌酸激酶的不可逆抑制是非竞争性的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Kinetics of irreversible inhibition of creatine kinase during modification by o-phthaldehyde.

It has been previously reported that, with a fluorescence probe formed from o-phthaldehyde (OPTA) and the thiol and amino groups at or near the active site of creatine kinase, inactivation and exposure of the probe take place simultaneously and well before unfolding of the molecule as a whole. In this study, the inactivation and modification kinetics of purified rabbit muscle creatine kinase by OPTA have been compared, the former by following the substrate reaction in the presence of a previously described inactivator. The microscopic rate constants for the reaction of the inactivator with the free enzyme and with the enzyme-substrate complexes were determined. From the results obtained it appears that OPTA is noncompetitive with respect to both substrates. The inactivation kinetics is monophasic with OPTA, and neither ATP nor creatine alone affect the rate constant of inactivation of the enzyme, indicating that the irreversible inhibition of creatine kinase by OPTA is of the noncompetitive type.

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