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Identification of the L,D-transpeptidases responsible for attachment of the Braun lipoprotein to Escherichia coli peptidoglycan.

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.
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https://www.hal.inserm.fr/inserm-00185689
Contributor : Maxime Lecerf <>
Submitted on : Tuesday, November 6, 2007 - 4:58:16 PM
Last modification on : Friday, September 11, 2020 - 3:01:05 AM
Long-term archiving on: : Monday, April 12, 2010 - 1:32:22 AM

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Sophie Magnet, Samuel Bellais, Lionel Dubost, Martine Fourgeaud, Jean-Luc Mainardi, et al.. Identification of the L,D-transpeptidases responsible for attachment of the Braun lipoprotein to Escherichia coli peptidoglycan.. Journal of Bacteriology, American Society for Microbiology, 2007, 189 (10), pp.3927-31. ⟨10.1128/JB.00084-07⟩. ⟨inserm-00185689⟩

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