The important roles that carbohydrates play in biology and medicine have stimulated a rapid expansion of the field of glycobiology.¹ The structures of glycoside hydrolases, the enzymes involved in the degradation of glycosidic bonds, are now being elucidated in molecular detail.² It is becoming increasingly accepted that only a complex interplay of electronic/structural properties can explain the perfect docking between the substrate and the enzyme. In this presentation, we will show how the conformational changes of one sugar unit of the carbohydrate affect the efficiency of these enzymes.³ The structure and dynamics of the enzyme-substrate complex will be investigated by means of ab initio QM/MM simulations.⁴

¹ Hurtley, S., Service, R., and Szuromi, P. (eds) Science 291, 2263–2502 (2000).

² Davies, G., and Henrissat, B. Structure 3, 853–859 (1995).

³ Planas, A. Biochim. Biochim. Acta 1543, 361–382 (2000).

⁴ Biarnés, X. Nieto, J., Planas, A., and Rovira, C. J. Biol. Chem. 281, 1432-1441 (2006).

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