The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases
Copyright policy )The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases
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.
- Laboratoire Parole et Langage France
- Grenoble Alpes University France
- University of Cambridge United Kingdom
- Aix-Marseille University France
- King Abdulaziz University Saudi Arabia
conformation, Models, Molecular, 570, coordination, oxygenases, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Aspergillus oryzae, Molecular Sequence Data, mechanism, Oligosaccharides, Chitin, Lentinula, chemistry, Crystallography, X-Ray, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Mixed Function Oxygenases, Substrate Specificity, cellulose degradation, Catalytic Domain, Journal Article, Fluorescence Resonance Energy Transfer, Amino Acid Sequence, 1307, Cellulose, [SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Binding Sites, Molecular Biology/Structural Biology [q-bio.BM], Research Support, Non-U.S. Gov't, 1312, 540, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], enzyme, substrate-specificity, activation, Oxidation-Reduction, discovery, Copper
conformation, Models, Molecular, 570, coordination, oxygenases, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Aspergillus oryzae, Molecular Sequence Data, mechanism, Oligosaccharides, Chitin, Lentinula, chemistry, Crystallography, X-Ray, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Mixed Function Oxygenases, Substrate Specificity, cellulose degradation, Catalytic Domain, Journal Article, Fluorescence Resonance Energy Transfer, Amino Acid Sequence, 1307, Cellulose, [SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Binding Sites, Molecular Biology/Structural Biology [q-bio.BM], Research Support, Non-U.S. Gov't, 1312, 540, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], enzyme, substrate-specificity, activation, Oxidation-Reduction, discovery, Copper
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