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Results 1 - 7 of 7
EC Number
General Information
Commentary
Reference
metabolism
substrates cellulose and xyloglucan show a stabilizing effect on the apparent transition midpoint temperature of the reduced, catalytically active enzyme. Oxidative auto-inactivation and destabilization are observed in the absence of a suitable substrate
physiological function
cellobiose dehydrogenase enhances cellulose degradation by coupling the oxidation of cellobiose to the reductive activation of copper-dependent polysaccharide monooxygenase that catalyzes the insertion of oxygen into C-H bonds adjacent to the glycosidic linkage; cellobiose dehydrogenase enhances cellulose degradation by coupling the oxidation of cellobiose to the reductive activation of copper-dependent polysaccharide monooxygenase that catalyzes the insertion of oxygen into C-H bonds adjacent to the glycosidic linkage; cellobiose dehydrogenase enhances cellulose degradation by coupling the oxidation of cellobiose to the reductive activation of copper-dependent polysaccharide monooxygenase that catalyzes the insertion of oxygen into C-H bonds adjacent to the glycosidic linkage
physiological function
enzyme introduces carboxyl groups primarily in surface-exposed crystalline areas of the cellulosic substrate. Cellulose nano-fibrils exposed on the surface are degraded into shorter and thinner insoluble fragments. Prior action of LPMO enables cellulases to attack otherwise highly resistant crystalline substrate areas and promotes an overall faster and more complete surface degradation
physiological function
isoforms LPMO9C and LPMO9F bind to nanocrystalline cellulose with high preference for the very same substrate surfaces that are also used by Hypocrea jecorina processive cellulase CBH I to move along during hydrolytic cellulose degradation. The bound LPMOs are immobile during their adsorbed residence time on cellulose. Treatment with LPMO results in fibrillation of crystalline cellulose, enhances the cellulase adsorption more than 2fold and increases enzyme turnover on the cellulose surface, boosting the hydrolytic conversion
physiological function
LPMO9A shows a strong synergistic effect with endoglucanase I with a 16fold higher release of detected oligosaccharides, compared to the oligosaccharides release of LPMO9A and endoglucanase I alone
physiological function
the enzyme produces both C1- and 4-oxidized products. The equilibrium between the two reducing end oxidized products, favoring the linear aldonic acid, may increase product inhibition, which would in turn reduce processive substrate turnover. In the case of action at the nonreducing end, oxidation appears to lower affinity with the nonreducing end specific cellulase, reducing product inhibition and potentially promoting processive cellulose turnover
physiological function
the oxidative activity of Cel61A displays a synergistic effect capable of boosting endo-1,4-beta-D-glucanase activity from Bacillus amyloliquefaciens, and thereby substrate depolymerization of soy cellulose, by 27%
Results 1 - 7 of 7