2006
DOI: 10.1074/jbc.m600114200
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Aslfm, the D-Aspartate Ligase Responsible for the Addition of D-Aspartic Acid onto the Peptidoglycan Precursor of Enterococcus faecium

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Cited by 88 publications
(75 citation statements)
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“…Thus, Ldt fm tolerated the substitution only in the donor substrate, in contrast to the PBPs that catalyzed peptidoglycan cross-linking with modified donor and acceptor substrates. Modifications of the side chain of peptidoglycan precursors were also shown to be tolerated by PBPs of E. faecalis and S. aureus in previous studies (12,24). (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…Thus, Ldt fm tolerated the substitution only in the donor substrate, in contrast to the PBPs that catalyzed peptidoglycan cross-linking with modified donor and acceptor substrates. Modifications of the side chain of peptidoglycan precursors were also shown to be tolerated by PBPs of E. faecalis and S. aureus in previous studies (12,24). (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…1A) (23). In E. faecium, D-Asp is added to the precursors by the Asl fm ligase and subsequently partially amidated (12). The bppA1 gene of E. faecalis was cloned under the control of an inducible promoter to generate plasmid pJEH6 and introduced into E. faecium M512 in order to manipulate the structure of the substrate of the cross-linking reaction that can be catalyzed in this mutant by Ldt fm and by the PBPs (28).…”
Section: Resultsmentioning
confidence: 99%
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“…One entails the addition of L-amino acids or glycine from aminoacyl-tRNAs (23,24,62,84,108,114,135,153), while the other one, which is ATP dependent and presumably specific for D-amino acids, proceeds without aminoacyl-tRNAs (15,162,185).…”
Section: Biosynthesis Of Modified Lipid Intermediatesmentioning
confidence: 99%
“…In contrast, in Weissella viridescens (formerly Lactobacillus viridescens), the in vivo addition of L-alanine onto UDP-MurNAc-pentapeptide was substantiated by the presence of a high UDP-MurNAc-hexapeptide pool and the absence of UDP-MurNAc-pentapeptide (83). The peptidyltransferases from Enterococcus faecalis (BppA1 and BppA2) and Enterococcus faecium (Aslfm) were overproduced and purified by using UDP-MurNAc-pentapeptide as an in vitro substrate (15,23,24). However, since the turnover observed with this substrate was very low and since no large UDP-MurNAc-hexapeptide pool level has been encountered in studies of enterococci (20), it can be assumed that in vivo the addition of the bridging amino acids occurs on the lipid intermediates.…”
Section: Biosynthesis Of Modified Lipid Intermediatesmentioning
confidence: 99%