Glycoside hydrolase

Glycoside hydrolase is a canonical name for a large and diverse class of enzymes that catalyze the hydrolysis (breakdown) of glycosidic bonds within carbohydrates or between a carbohydrate and a non-carbohydrate moiety[1][2][5][7]. These enzymes, which also include the terms glycosidase and glycosyl hydrolase, are present in all domains of life and have critical roles in carbohydrate digestion, nutrient uptake, processing of glycoproteins and glycolipids, lysosomal function, and biomass degradation[1][4][5][7]. Many glycoside hydrolases are clinically important: defects cause lysosomal storage disorders (e.g., Gaucher disease), and specific enzymes (such as glucosidase, galactosidase, and neuraminidase) are targeted for disease treatment[3][4]. Glycoside hydrolases are classified by sequence homology and substrate specificity into over 160 families (as curated by the CAZy database), and they utilize characteristic catalytic mechanisms (retaining or inverting the anomeric configuration) to cleave substrates[2][3][5][7]. This class of enzymes is also a major focus for drug and biotechnology development due to its central role in human health, disease, and industrial applications[2][3][7].

Other names

GlycosidaseGlycosyl hydrolaseGH (e.g., in family names such as "GH116")Glycoside hydrolases

Competitive inhibition of specific glycosidases (e.g., substrate mimetics inhibiting GBA1, GBA2); Enzyme replacement therapy (supplying deficient or defective enzyme); Pharmacological chaperoning (stabilizing misfolded enzyme)