Department of Microbial Bioactive Compounds, Interfaculty Institute of Microbiology and Infection Medicine, University of Tuebingen, Germany.
Nat Prod Rep. 2017 Jul 6;34(7):815-831. doi: 10.1039/c6np00125d.
Covering: up to 2017The bacterial Clp protease is a highly conserved and structurally versatile machine. It has gained a lot of recognition during the last decade as a novel antibacterial drug target with an unprecedented mechanism of action. Due to its complexity, there are distinct means of interfering with its natural functions and several compounds targeting this machine have been identified. In this review, we summarize the current state of knowledge about natural products deregulating Clp proteolysis, a crucial and delicate process within the cell. Among those, acyldepsipeptide antibiotics of the ADEP class (ADEPs) are characterized best. The molecular mechanism of ADEP-mediated deregulation sheds light on the inner workings of the Clp protease.
截至 2017 年
细菌 Clp 蛋白酶是一种高度保守且结构多样的机器。在过去十年中，它作为一种具有前所未有的作用机制的新型抗菌药物靶标而得到了广泛的认可。由于其复杂性，存在着多种干扰其天然功能的方法，并且已经鉴定出几种针对该机器的化合物。在这篇综述中，我们总结了目前关于天然产物调节 Clp 蛋白水解的知识状态，这是细胞内一个关键而微妙的过程。在这些产物中，酰基二肽抗生素 ADEP 类（ADEPs）的特征最为明显。ADEP 介导的调节失控的分子机制揭示了 Clp 蛋白酶的内部工作原理。
