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Showing 1–3 of 3 results
Advanced filters: Author: Manuela Tosin Clear advanced filters

  • The tetronate ring appears in several natural products, but the biosynthetic path to this structure has proven elusive. Reconstitution of a polyketide assembly line and in vitro assays with a chemically synthesized intermediate now point to a single enzyme as catalyzing ring formation.

    • Yuhui Sun
    • Frank Hahn
    • Peter F Leadlay
    Research
    Nature Chemical Biology
    Volume: 6, P: 99-101

  • Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes assembling complex natural products. Here, the structures of a Thermobifida fusca NRPS condensation domain bound to the substrate-bearing peptidyl carrier protein (PCP) domain provide insight into the mechanisms of substrate selectivity and engagement within the catalytic pocket.

    • Thierry Izoré
    • Y. T. Candace Ho
    • Max J. Cryle
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • This work shows that the biosynthesis of the polyether tetronasin involves an apparent enzyme-catalysed inverse-electron-demand hetero-Diels–Alder reaction to form an unexpected oxadecalin intermediate. A second enzyme then rearranges the oxadecalin to form the four-ringed tetronasin.

    • Rory Little
    • Fernanda C. R. Paiva
    • Peter F. Leadlay
    Research
    Nature Catalysis
    Volume: 2, P: 1045-1054