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Showing 1–6 of 6 results
Advanced filters: Author: Andreas Prester Clear advanced filters

  • Class-A β-lactamases can render antibiotics ineffective through hydrolysis, but the associated enzyme-antibiotic complexes remain largely underexplored at room temperatures. Here, the authors use RT serial synchrotron crystallography to report acyl-enzyme intermediates of the catalytically impaired β-lactamase CTX-M-14 mutant (E166A) from Klebsiella pneumoniae, and show that different isoxazolyl-penicillins adopt different conformations at room temperature.

    • Gargi Gore
    • Andreas Prester
    • Eike C. Schulz
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-12

  • Metallo-β-lactamases dismantle most β-lactam antibiotics and cause antibiotic resistance, however, no metallo-β-lactamase inhibitors are clinically available. Here, the authors report stereodynamically chiral phosphonic acids as potential metallo-β-lactamase inhibitors, showing unparalleled adaptability to the structural diversity of metallo-β-lactamases.

    • Kinga Virág Gulyás
    • Liping Zhou
    • Máté Erdélyi
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-13

  • Boronate-based ß-lactamase inhibitors play an important role in treating multidrug-resistant bacteria infection, however, the molecular mechanism of inhibition remains unclear. Here, the authors use time-resolved serial crystallography to investigate the binding process by using boric acid as a model against β-lactamase CTX-M-14, revealing the binding to the active site serine within 80–100 ms, a subsequent 1,2-diol boric ester formation with glycerol within 100–150 ms, as well as the displacement of the sulfate anion in the active site.

    • Andreas Prester
    • Markus Perbandt
    • Christian Betzel
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-12