Lysosomal storage disorders
Deficiency of specific lysosomal glycosidases prevents glycan degradation and leads to substrate accumulation and disease.1
Glycome Atlas
protein
Also known as glycosidase, glycoside hydrolase, glycan-trimming enzymes
Plain-language answer
Glycosidases are enzymes that cut sugar chains apart. They remove sugars during glycan processing, recycle glycans in the lysosome, and let organisms harvest sugars from food and from each other.1
Trimming by glycosidases is a required editing step in building mature glycans, and inherited deficiencies of lysosomal glycosidases cause serious storage diseases. Gut bacteria use glycosidases to feed on mucus and dietary fiber.1
Technical detail
Glycosidases (glycoside hydrolases) catalyze hydrolysis of glycosidic linkages with defined anomeric and linkage specificity, functioning in ER/Golgi glycan processing, lysosomal degradation, and extracellular glycan catabolism.1
In the secretory pathway, glucosidases and mannosidases trim N-glycan precursors to enable maturation, while lysosomal exoglycosidases sequentially remove terminal sugars to degrade glycoconjugates for recycling.1
Microbial glycoside hydrolases release monosaccharides from host mucins and dietary polysaccharides, a key part of how the gut microbiota forages glycans.1
Human relevance
Deficiency of specific lysosomal glycosidases prevents glycan degradation and leads to substrate accumulation and disease.1
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References