| Literature DB >> 24333859 |
Abstract
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.Entities:
Keywords: Leader peptidase; Leader peptide; Preprotein processing; Protein secretion; Signal peptidase; Signal peptide
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Year: 2013 PMID: 24333859 DOI: 10.1016/j.bbamcr.2013.12.003
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002