Glycosidases act by catalyzing the cleavage of glycosidic bonds, which link sugar molecules in polysaccharides, oligosaccharides, and glycoproteins. The catalytic mechanism typically involves the formation of a transient enzyme-substrate complex, followed by the stabilization of a high-energy transition state and the eventual release of the hydrolyzed products. This process often requires specific amino acid residues in the active site, such as aspartic acid, glutamic acid, or histidine, which facilitate proton transfer and stabilize the transition state.
