The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases

Kristian E H Frandsen, Thomas J Simmons, Paul Dupree, Jens-Christian N Poulsen, Glyn R Hemsworth, Luisa Ciano, Esther M Johnston, Morten Tovborg, Katja S Johansen, Pernille von Freiesleben, Laurence Marmuse, Sébastien Fort, Sylvain Cottaz, Hugues Driguez, Bernard Henrissat, Nicolas Lenfant, Floriana Tuna, Amgalanbaatar Baldansuren, Gideon J Davies, Leila Lo LeggioPaul H Walton

    Research output: Contribution to journalArticlepeer-review


    Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains.

    Original languageEnglish
    Pages (from-to)298-303
    Number of pages6
    JournalNature chemical biology
    Issue number4
    Early online date29 Feb 2016
    Publication statusPublished - Apr 2016


    • Amino Acid Sequence
    • Aspergillus oryzae
    • Binding Sites
    • Catalytic Domain
    • Cellulose
    • Chitin
    • Copper
    • Crystallography, X-Ray
    • Fluorescence Resonance Energy Transfer
    • Lentinula
    • Mixed Function Oxygenases
    • Models, Molecular
    • Molecular Sequence Data
    • Oligosaccharides
    • Oxidation-Reduction
    • Substrate Specificity
    • Journal Article
    • Research Support, Non-U.S. Gov't


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