Synthetic tripeptides as alternate substrates of murein peptide ligase (Mpl)
Hervé, Mireille (Author), Kovač, Andreja (Author), Cardoso, Cécile (Author), Patin, Delphine (Author), Brus, Boris (Author), Barreteau, Hélène (Author), Mengin-Lecreulx, Dominique (Author), Gobec, Stanislav (Author), Blanot, Didier (Author)

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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.

Keywords:Escherichia coli, Mpl, Murein peptide ligase, peptidoglycan recycling, tripeptide substrates
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Number of pages:str. 1120-1126
Numbering:Vol. 95, issue 6
ISSN on article:0300-9084
DOI:10.1016/j.biochi.2012.12.011 Link is opened in a new window
COBISS.SI-ID:3374961 Link is opened in a new window
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Shortened title:Biochimie
Publisher:Masson & cie
COBISS.SI-ID:4254474 This link opens in a new window

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