Glycosidases constitute the main machinery for the degradation of glycosidic bonds in nature. Their efficiency is a key issue in the processing of biomass for bioethanol production and they are also growing in importance as drug targets. By means of first-principles QM/MM simulations, we unravel the catalytic mechanism of a β-mannosidase of family 134 and show that the lysozyme fold can be co-opted to catalyze the hydrolysis of different polysaccharides in a mechanistically distinct manner. We also report the mechanism of a novel engineered β-glucosidase that allows β-stereoselective catalyst for glycoside synthesis.

Catalysis by natural and engineered glycosidases. An atomistic view from QM/MM simulations

254th National Meeting (2017)

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