Glycoside hydrolases function by breaking the glycosidic bond between a carbohydrate and another molecule, which could be another carbohydrate, protein, lipid, or any other type of molecule. This is achieved through a mechanism that usually involves the formation of a glycosyl-enzyme intermediate. The catalytic process often includes two critical residues: one acts as a nucleophile and the other as an acid/base catalyst. The specificity of glycoside hydrolases towards their substrates is determined by the active site's shape and the arrangement of catalytic residues.
