Attwood Paul V
School of Biomedical, Biomolecular and Chemical Sciences (M310), The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia.
Biochim Biophys Acta. 2013 Jan;1834(1):470-8. doi: 10.1016/j.bbapap.2012.03.001. Epub 2012 Mar 10.
The current work briefly reviews what is currently known about protein phosphorylation on arginine, lysine and histidine residues, where PN bonds are formed, and the protein kinases that catalyze these reactions. Relatively little is understood about protein arginine and lysine kinases and the role of phosphorylation of these residues in cellular systems. Protein histidine phosphorylation and the two-component histidine kinases play important roles in cellular signaling systems in bacteria, plants and fungi. Their roles in vertebrates are much less well researched and there are no protein kinases similar to the two-component histidine kinases. The main focus of the review however, is to present current knowledge of the characterization, mechanisms of action and biological roles of the phosphatases that catalyze the hydrolysis of these phosphoamino acids. Very little is known about protein phosphoarginine and phospholysine phosphatases, although their existence is well documented. Some of these phosphatases exhibit very broad specificity in terms of which phosphoamino acids are substrates, however there appear to be one or two quite specific protein phospholysine and phosphoarginine phosphatases. Similarly, there are phosphatases with broad substrate specificities that catalyze the hydrolysis of phosphohistidine in protein substrates, including the serine/threonine phosphatases 1, 2A and 2C. However there are two, more specific, protein phosphohistidine phosphatases that have been well characterized and for which structures are available, SixA is a phosphatase associated with two-component histidine kinase signaling in bacteria, and the other is found in a number of organisms, including mammals. This article is part of a Special Issue entitled: Chemistry and mechanism of phosphatases, diesterases and triesterases.
当前的工作简要回顾了目前已知的关于精氨酸、赖氨酸和组氨酸残基上的蛋白质磷酸化、PN键形成的位置以及催化这些反应的蛋白激酶。关于蛋白质精氨酸和赖氨酸激酶以及这些残基的磷酸化在细胞系统中的作用，人们了解得相对较少。蛋白质组氨酸磷酸化和双组分组氨酸激酶在细菌、植物和真菌的细胞信号系统中发挥着重要作用。它们在脊椎动物中的作用研究得少得多，而且不存在类似于双组分组氨酸激酶的蛋白激酶。然而，本综述的主要重点是介绍目前关于催化这些磷酸氨基酸水解的磷酸酶的特性、作用机制和生物学作用的知识。尽管蛋白质磷酸精氨酸和磷酸赖氨酸磷酸酶的存在有充分的文献记载，但人们对它们知之甚少。其中一些磷酸酶在作为底物的磷酸氨基酸方面表现出非常广泛的特异性，然而似乎有一两种相当特异的蛋白质磷酸赖氨酸和磷酸精氨酸磷酸酶。同样，也有一些具有广泛底物特异性的磷酸酶催化蛋白质底物中磷酸组氨酸的水解，包括丝氨酸/苏氨酸磷酸酶1、2A和2C。然而，有两种特征明确且有结构信息的更特异的蛋白质磷酸组氨酸磷酸酶，SixA是一种与细菌双组分组氨酸激酶信号传导相关的磷酸酶，另一种存在于包括哺乳动物在内 的许多生物体中。本文是名为：磷酸酶、二酯酶和三酯酶的化学与机制的特刊的一部分。
