Characterization of the Peptidoglycan of Vancomycin-Susceptible Enterococcus faecium†

摘要: Vancomycin and other antibacterial glycopeptide analogues target the cell wall affect enzymatic processes involved with cell-wall biosynthesis. Understanding structure organization of peptidoglycan is first step in establishing mode action these glycopeptides. We have used solid-state NMR to determine relative concentrations stem-links (64%), bridge-links (61%), cross-links (49%) walls vancomycin-susceptible Enterococcus faecium (ATTC 49624). Furthermore, we determined that vivo only 7% stems terminate d-Ala-d-Ala, well-known vancomycin-binding site. Presumably, d-Ala-d-Ala cleaved from uncross-linked mature by an active carboxypeptidase. believe most few pentapeptide ending occur template nascent strands are crucial for