Answers are grounded in this paper and cite their sources.
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.
No takes yet. Share an insight, caveat, or question.
Magnet et al. (2007) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: