Interaction between Cellobiose Dehydrogenase and Lytic Polysaccharide Monooxygenase

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Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase.

Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds using molecular oxygen and an external electron donor. We have used NMR and isothermal titration calorimetry (ITC) to study the interactions of a broad-specificity fungal LPMO, NcLPMO9C, with various substrates and with cellobiose dehydrogenase (CDH), a known natural sup...

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A fast and sensitive activity assay for lytic polysaccharide monooxygenase

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Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability

Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-containing enzymes that oxidatively degrade insoluble plant polysaccharides and soluble oligosaccharides. Upon reductive activation, they cleave the substrate and promote biomass degradation by hydrolytic enzymes. In this study, we employed LPMO9C from Neurospora crassa, which is active toward cellulose and soluble β-glucans, to ...

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Cellobiose Dehydrogenase Production by the Genus Cladosporium

Cellobiose dehydrogenase (CDH EC.1.1.5.1) is an extracellular enzyme that mainly produced by wood-degrading fungi. It oxidizes cellobiose to cellobionolactone using a wide spectrum of electron acceptors. The key roles of CDH in growth, metabolism, and some other important cellular processes such as cellulose degradation in fungi have been noted. Since the demands for finding new sources of CDH ...

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ژورنال

عنوان ژورنال: Biochemistry

سال: 2019

ISSN: 0006-2960,1520-4995

DOI: 10.1021/acs.biochem.8b01178