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Showing 1–3 of 3 results
Advanced filters: Author: Clarissa Melo Czekster Clear advanced filters
  • Cyclodipeptide oxidases are filamentous enzymes. Here, the authors dissect the mechanism of a promiscuous flavoenzyme from the biosynthesis of cyclodipeptide natural products, unveiling fast catalysis for peptide oxidation in a distinct active site.

    • Emmajay Sutherland
    • Christopher J. Harding
    • Clarissa Melo Czekster
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14
  • The secreted aminopeptidase Pseudomonas aeruginosa aminopeptidase (PaAP) is required for nutrient recycling in biofilms. Using the information from protein structure and kinetics, a potent cyclic peptide inhibitor for PaAP was designed that killed cells in late-stage biofilms.

    • Christopher John Harding
    • Marcus Bischoff
    • Clarissa Melo Czekster
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 19, P: 1158-1166
  • Cyclodipeptide synthases (CDPSs) generate a wide range of cyclic dipeptides using aminoacylated tRNAs as substrates, however the substrate selection mechanism is not yet known. Here, the authors investigate the substrate promiscuity of two histidine-incorporating CDPSs to generate an extensive library of products which complement the chemical realm of histidine-containing cyclic dipeptides.

    • Emmajay Sutherland
    • Christopher John Harding
    • Clarissa Melo Czekster
    ResearchOpen Access
    Communications Chemistry
    Volume: 5, P: 1-10