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Showing 1–6 of 6 results
Advanced filters: Author: Glyn R Hemsworth Clear advanced filters

  • Crystal structures of human O-GlcNAc hydrolase (hOGA) fragments show that hOGA's dimeric structure is organized by swapping of an α-helical element and reveal features of inhibitor binding to the catalytic domain.

    • Christian Roth
    • Sherry Chan
    • Gideon J Davies
    Research
    Nature Chemical Biology
    Volume: 13, P: 610-612

  • Lytic polysaccharide monooxygenases (LPMOs) are industrially important enzymes that oxidatively deconstruct polysaccharides. Here, Lo Leggio et al. report the activity, spectroscopy and three-dimensional structure of a LPMO of the new CAZy AA13 family active on recalcitrant-retrograded starch.

    • Leila Lo Leggio
    • Thomas J. Simmons
    • Paul H. Walton
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-9

  • Use of a domain of unknown function as the input for bioinformatic searching reveals a new Cu-dependent family of chitinases, assigned as CAZy group AA11, that diverge in sequence but share structural homology with the existing AA9 and AA10 families.

    • Glyn R Hemsworth
    • Bernard Henrissat
    • Paul H Walton
    Research
    Nature Chemical Biology
    Volume: 10, P: 122-126

  • Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes that oxidatively degrade polysaccharides and find use in industrial processing of lignocellulose. Crystallographic and spectroscopic studies define how LPMOs recognize their oligosaccharide substrates and mediate oxidative cleavage.

    • Kristian E H Frandsen
    • Thomas J Simmons
    • Paul H Walton
    Research
    Nature Chemical Biology
    Volume: 12, P: 298-303

  • LPMOs catalyze the oxidative breakdown of polysaccharides, thereby facilitating biomass degradation. By analyzing the digestive proteome of firebrats, the authors here identify a yet uncharacterized LPMO family and provide phylogenetic, structural and biochemical insights into its origin and functions.

    • Federico Sabbadin
    • Glyn R. Hemsworth
    • Simon J. McQueen-Mason
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12