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Glycosidase inhibitors, enzymes and substrates are tools for studying how glycans are broken down. Glycosidases remove sugars from glycoproteins, glycolipids and polysaccharides and shape N-glycan processing in the endoplasmic reticulum and Golgi apparatus. Kifunensine, an alkaloid, was reported in 1990 to inhibit glycoprotein processing mannosidase I, so N-glycans stay in high-mannose form. Peptide-N-glycosidase F (PNGase F) releases intact N-linked glycans from glycoproteins, as described in 1985. OGT2115 inhibits heparanase, the endo-β-glucuronidase that cleaves heparan sulfate chains. M-31850 inhibits β-hexosaminidase, and PFB-FDGlu is a fluorogenic substrate for glucocerebrosidase (GCase). Enzymes that cleave glucose residues have their own neighboring category, Glucosidase.
