Zinc metalloproteases (ZnMPs) participate in diverse biological reactions, encompassing the synthesis and degradation of all the major metabolites in living organisms. In particular, ZnMPs have been recognized to play a very important role in controlling the concentration level of several peptides and/or proteins whose homeostasis has to be finely regulated for the correct physiology of cells. Dyshomeostasis of aggregation‐prone proteins causes pathological conditions and the development of several different diseases. For this reason, in recent years, many analytical approaches have been applied for studying the interaction between ZnMPs and their substrates and how environmental factors can affect enzyme activities. In this scenario, mass spectrometric methods occupy a very important role in elucidating different aspects of ZnMPs‐substrates interaction. These range from identification of cleavage sites to quantitation of kinetic parameters. In this work, an overview of all the main achievements regarding the application of mass spectrometric methods to investigating ZnMPs‐substrates interactions is presented. A general experimental protocol is also described which may prove useful to the study of similar interactions. © 2020 John Wiley & Sons Ltd. Mass Spec Rev

中文翻译：

---

使用质谱法研究锌-金属蛋白酶-底物相互作用。

锌金属蛋白酶 (ZnMP) 参与多种生物反应，包括生物体中所有主要代谢物的合成和降解。特别是，人们已经认识到 ZnMPs 在控制几种肽和/或蛋白质的浓度水平方面发挥着非常重要的作用，这些肽和/或蛋白质的稳态必须被精细调节以实现细胞的正确生理机能。易聚集蛋白的动态平衡导致病理状况和几种不同疾病的发展。为此，近年来，许多分析方法已被应用于研究 ZnMPs 与其底物之间的相互作用以及环境因素如何影响酶活性。在这种情况下，质谱方法在阐明 ZnMPs-底物相互作用的不同方面起着非常重要的作用。这些范围从切割位点的鉴定到动力学参数的定量。在这项工作中，概述了有关应用质谱方法研究 ZnMPs 与底物相互作用的所有主要成就。还描述了一个通用的实验协议，它可能对研究类似的相互作用有用。© 2020 John Wiley & Sons Ltd. 质谱修订版 还描述了一个通用的实验协议，它可能对研究类似的相互作用有用。© 2020 John Wiley & Sons Ltd. 质谱修订版 还描述了一个通用的实验协议，它可能对研究类似的相互作用有用。© 2020 John Wiley & Sons Ltd. 质谱修订版