Identification of the l , d -Transpeptidases Responsible for Attachment of the Braun Lipoprotein to Escherichia coli Peptidoglycan
- 15 May 2007
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 189 (10) , 3927-3931
- https://doi.org/10.1128/jb.00084-07
Abstract
The L,D-transpeptidase Ldt(fm) catalyzes peptidoglycan cross-linking in beta-lactam-resistant mutant strains of Enterococcus faecium. Here, we show that in Escherichia coli Ldt(fm) homologues are responsible for the attachment of the Braun lipoprotein to murein, indicating that evolutionarily related domains have been tailored to use muropeptides or proteins as acyl acceptors in the L,D-transpeptidation reaction.Keywords
This publication has 22 references indexed in Scilit:
- Crystal Structure of a Novel β-Lactam-insensitive Peptidoglycan TranspeptidaseJournal of Molecular Biology, 2006
- Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive BacteriaMicrobiology and Molecular Biology Reviews, 2006
- A Novel Peptidoglycan Cross-linking Enzyme for a β-Lactam-resistant Transpeptidation PathwayJournal of Biological Chemistry, 2005
- Synthesis of Mosaic Peptidoglycan Cross-bridges by Hybrid Peptidoglycan Assembly Pathways in Gram-positive BacteriaJournal of Biological Chemistry, 2004
- Covalent lipoprotein from the outer membrane of escherichia coliPublished by Elsevier ,2003
- Balance between Two Transpeptidation Mechanisms Determines the Expression of β-Lactam Resistance in Enterococcus faeciumJournal of Biological Chemistry, 2002
- Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 å resolution 1 1Edited by D. ReesJournal of Molecular Biology, 2000
- Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coliGene, 1988
- Separation and quantification of muropeptides with high-performance liquid chromatographyAnalytical Biochemistry, 1988
- On the process of cellular division in Escherichia coli: a mutant of E. coli lacking a murein-lipoprotein.Proceedings of the National Academy of Sciences, 1977