Glucuronidase is a lysosomal glycosidase, a type of enzyme that removes carbohydrate groups from proteins. Glucuronidase exhibits both endo-glycosidase and exo-glycosidase activities, meaning that it can cleave monosaccharides from the middle of a chain or from the end.

Glycosylation is an interesting phenomenon that occurs in the endoplasmic reticulum (where carbohydrates are added to arginine groups via a process called N-linked glycosylation) and in the Golgi apparatus (where carbohydrates are added to serine/threonine groups via a process called O-linked glycosylation). This process is required for the appropriate folding of most proteins. Errors in glycosylation prevent many proteins from functioning properly.

Glucuronidase fits well into the lysosome's role as a recycling center for the cell.

An assay with beta-Glucuronidase (GUS assay) can find out, when and where a certain gene is transcribed.

Preparations of beta-Glucuronidase from the snail Helix pomatia, historically referred to by the trademark Glusulase, are used to digest the ascus of the yeast Saccharomyces cerevisiae after sporulation.

E. coli is among the few bacteria that can synthezise glucuronidase and therefore this trait is used to identify it.

Glucuronidase