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  • Synthetic tripeptides as alternate substrates of murein peptide ligase (Mpl)
    Hervé, Mireille ...
    Murein peptide ligase (Mpl) is an enzyme found in Gram-negative bacteria. It catalyses the addition of tripeptide L-Ala-g-D-Glu-meso-diaminopimelate to nucleotide precursor UDP-N-acetylmuramic acid ... during the recycling of peptidoglycan. Although not essential, this enzyme represents an interesting target for antibacterial compounds through the synthesis of alternate substrates whose incorporation into peptidoglycan might be deleterious for the bacterial cell. Therefore, we have synthesised 10 tripeptides L-Ala-g-D-Glu-Xaa in which Xaa represents amino acids different from diaminopimelic acid. Tripeptide with Xaa Ž Ž-D-Lys proved to be an excellent substrate of Escherichia coli Mpl in vitro. Tripeptides with Xaa Ž p-amino- orp-nitro-L-phenylalanine were poor substrates, while tripeptides with Xaa Ž D- or L-2-aminopimelate, DL-2-aminoheptanoic acid, L-Glu, L-norleucine, L-norvaline, L-2- aminobutyric acid or L-Ala were not substrates at all. Although a good Mpl substrate, the D-Lyscontaining tripeptide was devoid of antibacterial activity against E. coli, presumably owing to poor uptake.
    Vir: Biochimie. - ISSN 0300-9084 (Vol. 95, issue 6, 2013, str. 1120-1126)
    Vrsta gradiva - članek, sestavni del
    Leto - 2013
    Jezik - angleški
    COBISS.SI-ID - 3374961

    Povezava(-e):

    http://www.sciencedirect.com/science/article/pii/S0300908412005020
    DOI

vir: Biochimie. - ISSN 0300-9084 (Vol. 95, issue 6, 2013, str. 1120-1126)

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