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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/219212
Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
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The enzymatic breakdown of carbohydrates plays a critical role in several biological events and enables the development of sustainable processes to obtain bioproducts and biofuels. In this scenario, the design of efficient inhibitors for glycosidases that can act as drug targets and the engineering of carbohydrate-active enzymes with tailored catalytic properties is of remarkable importance. To guide rational approaches, it is necessary to elucidate enzyme molecular mechanisms, in particular understanding how the microenvironment modulates the conformational space explored by the substrate. Computer simulations, especially those based on ab initio methods, have provided a suitable atomic description of carbohydrate conformations and catalytic reactions in several glycosidase families. In this review, we will focus on how the active-site topology (pocket or cleft) and mode of cleavage (endo or exo) can affect the catalytic mechanisms adopted by glycosidases, in particular the substrate conformations along the reaction coordinate.
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ABRAHÃO BUENO MORAIS, Mariana, NIN HILL, Alba and ROVIRA I VIRGILI, Carme. Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes. Current Opinion in Chemical Biology. 2023. Vol. 74, num. 1-8. ISSN 1367-5931. [consulted: 12 of October of 2026]. Available at: https://hdl.handle.net/2445/219212