Shaping the Glycan Landscape: Hidden Relationships between Linkage and Ring Distortions Induced by Carbohydrate-Active Enzymes.

ABSTRACT: Carbohydrate-active enzymes (CAZymes) catalyze glycan remodeling by forming and cleaving glycosidic bonds. An often-observed aspect of their catalytic mechanisms, particularly in glycosidases, is monosaccharide ring distortion that brings the substrate from a stable solution conformation to a reactive state. To what extent this distortion is promoted by steric constraints in the enzyme's binding pocket or by more elusive dynamical effects associated with the glycan conformational flexibility is still a matter of debate. In our work, we quantify the conformational phase-space changes experienced by glycans upon CAZyme binding by means of enhanced-sampling molecular dynamics simulations. Our results reveal a novel correlation between torsional degrees of freedom along the glycosidic bonds an

SUBMITTER: Grothaus IL 

PROVIDER: S-EPMC12550843 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature