2026-04-13T04:00:28Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/2143072025-12-05T11:00:25Zcom_2072_1057col_2072_478907col_2072_478917col_2072_478933

00925njm 22002777a 4500 dc Coines, Joan author Cuxart Sanchez, Irene author Teze, David author Rovira i Virgili, Carme author 2024-07-04T14:55:29Z 2024-07-04T14:55:29Z 2022-01-24 2024-07-04T14:55:35Z Glycoside hydrolases and glycosyltransferases are the main classes of enzymes that synthesize and degrade carbohydrates, molecules essential to life that are a challenge for classical chemistry. As such, considerable efforts have been made to engineer these enzymes and make them pliable to human needs, ranging from directed evolution to rational design, including mechanism engineering. Such endeavors fall short and are unreported in numerous cases, while even success is a necessary but not sufficient proof that the chemical rationale behind the design is correct. Here we review some of the recent work in CAZyme mechanism engineering, showing that computational simulations are instrumental to rationalize experimental data, providing mechanistic insight into how native and engineered CAZymes catalyze chemical reactions. We illustrate this with two recent studies in which (i) a glycoside hydrolase is converted into a glycoside phosphorylase and (ii) substrate specificity of a glycosyltransferase is engineered toward forming O-, N-, or S-glycosidic bonds. Fosfats Pèptids Proteïnes Phosphates Peptides Proteins Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases