| Full text | |
| Author(s): |
Morais, Mariana Abrahao Bueno
;
Nin-Hill, Alba
;
Rovira, Carme
Total Authors: 3
|
| Document type: | Journal article |
| Source: | CURRENT OPINION IN CHEMICAL BIOLOGY; v. 74, p. 8-pg., 2023-03-15. |
| Abstract | |
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 con -for mations and catalytic reactions in several glycosidase fam-ilies. 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. (AU) | |
| FAPESP's process: | 18/22138-8 - Unveiling the calcium role on GH43 beta-xylosidases / alpha-L-arabinofuranosidases catalysis by QM/MM molecular dynamics methods |
| Grantee: | Mariana Abrahão Bueno de Morais |
| Support Opportunities: | Scholarships abroad - Research Internship - Post-doctor |