Glycoside hydrolase (GH) (GH)

Glycosidases, also known as glycoside hydrolases, are a vast family of enzymes that catalyze the hydrolysis of glycosidic bonds in complex sugars and glycoconjugates. They are ubiquitous across all domains of life and play fundamental roles in the digestion of dietary carbohydrates, the lysosomal degradation of glycolipids and glycoproteins, and the post-translational processing of N-linked glycoproteins. In clinical practice, glycosidases are significant therapeutic targets for a variety of conditions. For example, alpha-glucosidase inhibitors like acarbose are used to manage Type 2 diabetes by delaying glucose absorption, while neuraminidase inhibitors like oseltamivir are used to treat influenza by preventing viral shedding. Furthermore, genetic deficiencies in specific lysosomal glycosidases lead to lysosomal storage disorders, such as Gaucher and Pompe diseases, which are managed through enzyme replacement therapies or pharmacological chaperones. Their critical involvement in metabolic pathways and cellular recognition makes them essential focal points for drug discovery and diagnostic monitoring. Beyond metabolism, aberrant glycosidase activity is also linked to cancer metastasis and inflammatory responses, expanding their potential as biomarkers and therapeutic targets.

Other names

GlycosidaseGlycohydrolaseCarbohydraseGlycosyl hydrolase

Competitive inhibition of the enzyme's active site to prevent the hydrolysis of glycosidic bonds; or enzyme replacement to restore catalytic activity in deficient states.