The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases

• Published in: Nature chemical biology Vol. 12; no. 4; pp. 298 - 303
• Main Authors: Frandsen, Kristian E H, Simmons, Thomas J, Dupree, Paul, Poulsen, Jens-Christian N, Hemsworth, Glyn R, Ciano, Luisa, Johnston, Esther M, Tovborg, Morten, Johansen, Katja S, von Freiesleben, Pernille, Marmuse, Laurence, Fort, Sébastien, Cottaz, Sylvain, Driguez, Hugues, Henrissat, Bernard, Lenfant, Nicolas, Tuna, Floriana, Baldansuren, Amgalanbaatar, Davies, Gideon J, Lo Leggio, Leila, Walton, Paul H
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.04.2016; Nature Publishing Group
• Subjects: 631/535/1266; 631/92/173; 631/92/72; 639/638/263/49; Amino Acid Sequence; Aspergillus oryzae - enzymology; Aspergillus oryzae - genetics; Binding Sites; Biochemical Engineering; Biochemistry; Biochemistry, Molecular Biology; Biomass; Bioorganic Chemistry; Catalytic Domain; Cell Biology; Cellulose; Cellulose - metabolism; Chemistry; Chemistry/Food Science; Chitin; Chitin - metabolism; Copper; Copper - metabolism; Crystallography, X-Ray; Enzymes; Fluorescence Resonance Energy Transfer; Lentinula - enzymology; Lentinula - genetics; Life Sciences; Mixed Function Oxygenases - chemistry; Mixed Function Oxygenases - genetics; Mixed Function Oxygenases - metabolism; Models, Molecular; Molecular Sequence Data; Oligosaccharides - chemistry; Oxidation-Reduction; Quantitative Methods; Resonance; Saccharides; Spectroscopy; Spectrum analysis; Structural Biology; Substrate Specificity; enzyme; chemistry; oxygenases; discovery; conformation; activation; mechanism; cellulose degradation; substrate-specificity; coordination
• ISSN: 1552-4450; 1552-4469; 1552-4469
• DOI: 10.1038/nchembio.2029

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. 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.