VSE knjižnice (vzajemna bibliografsko-kataložna baza podatkov COBIB.SI)
  • MurD enzymes from different bacteria: evaluation of inhibitors
    Barreteau, Hélène ...
    d-Glutamic acid-adding enzyme (MurD ligase) catalyses the addition of d-glutamic acid to UDP-N-acetylmuramoyl-l-alanine, an essential cytoplasmic step in the pathway for bacterial cell-wall ... peptidoglycan synthesis. As such, it represents an important antibacterial drug-discovery target enzyme. Recently, several series of compounds have been synthesised and found to inhibit MurD from Escherichia coli, the best one having an IC50 value of 8 ŽM.In the present work, we have tested 20 of these compounds against the MurD enzymes from Staphylococcus aureus, Streptococcus pneumoniae, Borrelia burgdorferi and Mycobacterium tuberculosis. Most of the E. coli MurD inhibitors appeared less efficient against the four other orthologues. This divergent result can be explained by the differences in amino acid sequences and topologies of the active sites of the MurD ligases studied.
    Vir: Biochemical pharmacology. - ISSN 0006-2952 (Vol. 85, issue 5, 2012, str. 625-632)
    Vrsta gradiva - članek, sestavni del
    Leto - 2012
    Jezik - angleški
    COBISS.SI-ID - 3274609

    Povezava(-e):

    http://www.sciencedirect.com/science/article/pii/S0006295212004042
    DOI

vir: Biochemical pharmacology. - ISSN 0006-2952 (Vol. 85, issue 5, 2012, str. 625-632)
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