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锌离子对核糖核酸酶T1催化作用抑制效应的稳态动力学研究。

Steady-state kinetic studies of the inhibitory action of Zn2+ on ribonuclease T1 catalysis.

作者信息

Itaya M, Inoue Y

出版信息

Biochem J. 1982 Nov 1;207(2):357-62. doi: 10.1042/bj2070357.

DOI:10.1042/bj2070357
PMID:6818948
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1153868/
Abstract

The kinetic mechanism of specific inhibition by Zn2+ of ribonuclease T1 catalysis was studied by steady-state kinetic analysis of transphosphorylation of dinucleotides, GpCp(3'), GpUp(2') and GpUp(3'), and dinucleoside monophosphates, GpC and GpU. The inhibition was not simply competitive, non-competitive or uncompetitive, but the kinetic data were compatible with a mechanism of 'fully mixed inhibition' in which a fully non-competitive action was associated with a partially competitive action. Apparent equilibrium quotients involved in this model of inhibition were determined for the dinucleotide substrates, and we found that binding of either of Zn2+ and substrate was facilitated when the other was bound. The location of Zn2+ was suggested to be near His-40 and/or His-92 of the ribonuclease T1 molecule.

摘要

通过对二核苷酸GpCp(3')、GpUp(2')和GpUp(3')以及二核苷单磷酸GpC和GpU的转磷酸化进行稳态动力学分析，研究了Zn2+对核糖核酸酶T1催化的特异性抑制的动力学机制。这种抑制并非简单的竞争性、非竞争性或反竞争性抑制，但其动力学数据符合“完全混合抑制”机制，即完全非竞争性作用与部分竞争性作用相关。针对二核苷酸底物确定了该抑制模型中涉及的表观平衡商，我们发现当Zn2+和底物中的一方结合时，另一方的结合会变得更容易。有人认为Zn2+的位置靠近核糖核酸酶T1分子的His-40和/或His-92。

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本文引用的文献

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Ribonucleases in taka-diastase: properties, chemical nature, and applications.淀粉酶中的核糖核酸酶：特性、化学性质及应用
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