使用Mn2+离子重构的氨基酰化酶再活化过程的动力学。

Kinetics of the course of reactivation of aminoacylase reconstituted using Mn2+ ions.

作者信息

Zhang Y X, Le W P, Zhou H M

机构信息

Department of Chemistry, Capital University of Medical Science, Beijing, China.

出版信息

J Protein Chem. 1995 Nov;14(8):695-701. doi: 10.1007/BF01886908.

DOI:10.1007/BF01886908

PMID:8747430

Abstract

The kinetic theory of the substrate reaction during irreversible change of enzyme activity previously described by Tsou [Tsou (1988), Adv. Enzymol Relat. Areas Mol. Biol. 61, 381-436] has been applied to a study of the kinetics of the course of reactivation during reconstitution of apo-aminoacylase using Mn2+ or Zn2+. The kinetic parameters for Mn(2+)- and Zn(2+)-reconstituted enzymes and the microscopic rate constants for reactivation during reconstitution were determined. The kinetic analysis suggests the presence of a second Mn2+ binding site in Mn(2+)-reconstituted aminoacylase.

摘要

邹[邹(1988年)，《酶学及相关分子生物学领域进展》61卷，381 - 436页]之前描述的酶活性不可逆变化过程中底物反应的动力学理论，已应用于使用Mn2 +或Zn2 +对脱辅基氨基酰化酶进行重组过程中再活化过程的动力学研究。测定了Mn(2 +)和Zn(2 +)重组酶的动力学参数以及重组过程中再活化的微观速率常数。动力学分析表明，在Mn(2 +)重组的氨基酰化酶中存在第二个Mn2 +结合位点。