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Engineering lytic polysaccharide monooxygenases (LPMOs)
2020Lytic polysaccharide monooxygenases (LPMOs) are mono-copper enzymes that catalyze the hydroxylation of glycosidic bonds found in the most abundant and recalcitrant polysaccharides on Earth. Since their discovery in 2010, these enzymes have received extensive attention in both fundamental and applied research due to their remarkable oxidative power and ...
Zarah, Forsberg +4 more
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On the catalytic mechanisms of lytic polysaccharide monooxygenases
Current Opinion in Chemical Biology, 2016Lytic polysaccharide monooxygenases (LPMOs) are recently discovered copper-containing oxygenases. LPMOs oxidise recalcitrant polysaccharides such as chitin and cellulose, thereby making these substrates more tractable to canonical chitinase or cellulase action. As such, LPMOs are attracting much attention not only for their capacity to greatly increase
Paul H Walton, Gideon J Davies
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Lytic Polysaccharide Monooxygenases in Biomass Conversion
Trends in Biotechnology, 2015The derivation of second-generation biofuels from non-edible biomass is viewed as crucial for establishing a sustainable bio-based economy for the future. The inertness of lignocellulosic biomass makes its breakdown for conversion into fuels and other compounds a challenge.
Glyn R, Hemsworth +3 more
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Peptide-based chemical models for lytic polysaccharide monooxygenases
Dalton Transactions, 2022The Cu( ii )–HPH-NH 2 and Cu( ii )–HPHPY-NH 2 systems were proved to be relevant functional models of LPMOs, even at neutral pH.
Azza A. Hassoon +5 more
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Chitin-Active Lytic Polysaccharide Monooxygenases
2019Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the cleavage of 1,4-glycosidic bonds various plant cell wall polysaccharides and chitin. In contrast to glycoside hydrolases, LPMOs are active on the crystalline regions of polysaccharides and thus synergize with hydrolytic enzymes. This synergism leads to an overall
Gaston, Courtade, Finn L, Aachmann
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Recent insights into lytic polysaccharide monooxygenases (LPMOs)
Biochemical Society Transactions, 2018Lytic polysaccharide monooxygenases (LPMOs) are copper enzymes discovered within the last 10 years. By degrading recalcitrant substrates oxidatively, these enzymes are major contributors to the recycling of carbon in nature and are being used in the biorefinery industry.
Tandrup, Tobias +4 more
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The interplay between lytic polysaccharide monooxygenases and glycoside hydrolases
Essays in Biochemistry, 2023Abstract In nature, enzymatic degradation of recalcitrant polysaccharides such as chitin and cellulose takes place by a synergistic interaction between glycoside hydrolases (GHs) and lytic polysaccharide monooxygenases (LPMOs). The two different families of carbohydrate-active enzymes use two different mechanisms when breaking glycosidic
Morten Sørlie +2 more
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Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase
Carbohydrate Research, 2015For decades, the enzymatic conversion of recalcitrant polysaccharides such as cellulose and chitin was thought to solely rely on the synergistic action of hydrolytic enzymes, but recent work has shown that lytic polysaccharide monooxygenases (LPMOs) are important contributors to this process. Here, we have examined the initial rate enhancement an LPMO (
Anne Grethe, Hamre +3 more
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[Progress in lytic polysaccharide monooxygenase].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2019Lignocellulose is the most abundant renewable biomass resource. Enzymatic breakdown of lignocellulose into oligosaccharides or monosaccharides is the key to exploit lignocellulosic biomass. However, traditional glycoside hydrolases are insufficient to degrade lignocellulose.
Xiaobao, Sun +4 more
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In Silico Molecular Characterization of a Cyanobacterial Lytic Polysaccharide Monooxygenase
Journal of Molecular Graphics and ModellingLytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of β(1-4) glycosidic bonds and have attracted considerable attention because of their potential for enhancing efficiency in degrading recalcitrant polymeric substrates, in synergism with hydrolytic enzymes.
Rodrigo Virgolino +4 more
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