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1.14.99.56
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
745381
1.14.99.56
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 and more than 2fold enhances the cellulase adsorption. It also increased enzyme turnover on the cellulose surface, thus boosting the hydrolytic conversion
745866
1.14.99.56
physiological function
the enzyme prefers oxidation of products at C4, which lowers product binding affinity and thereby should enhance product release and processive hydrolytic turnover. Product inhibition resulting from binding of oxidized products is likely not significant
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740896
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