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蛋白质构象紊乱与酶催化作用。

Protein conformational disorder and enzyme catalysis.

作者信息

Schulenburg Cindy, Hilvert Donald

机构信息

Laboratory of Organic Chemistry, ETH Zürich, 8093, Zürich, Switzerland.

出版信息

Top Curr Chem. 2013;337:41-67. doi: 10.1007/128_2012_411.

Abstract

Though lacking a well-defined three-dimensional structure, intrinsically unstructured proteins are ubiquitous in nature. These molecules play crucial roles in many cellular processes, especially signaling and regulation. Surprisingly, even enzyme catalysis can tolerate substantial disorder. This observation contravenes conventional wisdom but is relevant to an understanding of how protein dynamics modulates enzyme function. This chapter reviews properties and characteristics of disordered proteins, emphasizing examples of enzymes that lack defined structures, and considers implications of structural disorder for catalytic efficiency and evolution.

摘要

尽管内在无序蛋白缺乏明确的三维结构,但它们在自然界中却无处不在。这些分子在许多细胞过程中发挥着关键作用,尤其是信号传导和调控。令人惊讶的是,即使是酶催化也能容忍相当程度的无序。这一观察结果与传统观念相悖,但对于理解蛋白质动力学如何调节酶的功能却具有重要意义。本章回顾了无序蛋白的性质和特征,重点介绍了缺乏明确结构的酶的实例,并探讨了结构无序对催化效率和进化的影响。

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