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  • Biochemical characterization and physiological properties of Escherichia coli UDP-N-acetylmuramate:L-alanyl-[gamma]-D-glutamyl-meso-diaminopimelate ligase (Mpl)
    Hervé, Mireille ...
    The UDP-N-acetylmuramateČL-alanyl- -D-glutamyl-meso-diaminopimelate ligase (Murein peptide ligase, Mpl) is known to be a recycling enzyme allowing reincorporation into peptidoglycan (murein) of the ... tripeptide L-alanyl- -D-glutamyl-meso-diaminopimelate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division. Mpl adds this peptide onto UDP-N-acetylmuramic acid, thereby providing an economic additional source of UDP-MurNAc-tripeptide available forde novo peptidoglycan biosynthesis. The Mpl enzyme from Escherichia coli has now been purified to homogeneity as a His-tagged form and its kinetic properties and parameters were determined. Mpl is shown to accept tri-, tetra-and pentapeptide as substrates in vitro, with similar efficiencies, but very poorly the dipeptide L-Ala-D-Glu and L-Ala. Replacement of meso-diaminopimelic acid by L-Lys results in an important decrease of the catalytic efficacy. The effects of disrupting the E. coli mpl gene andžor the ldcA gene encoding the L,D-carboxypeptidase on peptidoglycan metabolism were investigated. The variations of the pools of UDP-MurNAc-peptides and of free peptides observed between the wild-type and mutant strains demonstrated that the recycling activity of Mpl is not restricted to the tripeptide but that tetra- and pentapeptides are also directly reused by this process in vivo. Therelatively broad substrate specificity of the Mpl ligase makes us envision that it could represent an interesting potential target for antibacterial compounds.
    Source: Journal of bacteriology. - ISSN 0021-9193 (Vol. 189, no. 11, 2007, str. 3987-3995)
    Type of material - article, component part
    Publish date - 2007
    Language - english
    COBISS.SI-ID - 2074737

source: Journal of bacteriology. - ISSN 0021-9193 (Vol. 189, no. 11, 2007, str. 3987-3995)
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