Paetzel Mark
Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, British Columbia V5A 1S6, Canada.
Biochim Biophys Acta. 2014 Aug;1843(8):1497-508. doi: 10.1016/j.bbamcr.2013.12.003. Epub 2013 Dec 11.
Type I signal peptidase is the enzyme responsible for cleaving off the amino-terminal signal peptide from proteins that are secreted across the bacterial cytoplasmic membrane. It is an essential membrane bound enzyme whose serine/lysine catalytic dyad resides on the exo-cytoplasmic surface of the bacterial membrane. This review discusses the progress that has been made in the structural and mechanistic characterization of Escherichia coli type I signal peptidase (SPase I) as well as efforts to develop a novel class of antibiotics based on SPase I inhibition. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.
I型信号肽酶是一种负责从穿过细菌细胞质膜分泌的蛋白质上切割掉氨基末端信号肽的酶。它是一种必需的膜结合酶,其丝氨酸/赖氨酸催化二元组位于细菌膜的胞外表面。本综述讨论了在大肠杆菌I型信号肽酶(SPase I)的结构和机制表征方面取得的进展,以及基于抑制SPase I开发新型抗生素的努力。本文是名为“细菌中的蛋白质运输和分泌”的特刊的一部分。客座编辑:阿纳斯塔西奥斯·埃科诺莫和罗斯·达尔贝。