| Literature DB >> 26928935 |
Kristian E H Frandsen1, Thomas J Simmons2, Paul Dupree2, Jens-Christian N Poulsen1, Glyn R Hemsworth3, Luisa Ciano3, Esther M Johnston3, Morten Tovborg4, Katja S Johansen4, Pernille von Freiesleben4, Laurence Marmuse5, Sébastien Fort5, Sylvain Cottaz5, Hugues Driguez5, Bernard Henrissat6,7,8, Nicolas Lenfant6,7, Floriana Tuna9, Amgalanbaatar Baldansuren9, Gideon J Davies3, Leila Lo Leggio1, Paul H Walton3.
Abstract
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.Entities:
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Year: 2016 PMID： 26928935 PMCID： PMC4817220 DOI： 10.1038/nchembio.2029
Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040