Jump to: navigation, search
glucuronidase, beta
Other data
EC number3.2.1.31
LocusChr. 7 q22

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Glucuronidases are enzymes that separate glucoronic acid molecules from other molecules by cutting glycosidic bonds. They are thus classified as glycoside hydrolases that cleave glucuronides.

In eukaryotes, glucuronidase is located in lysosomes and plays an important role in recycling cellular components by cleaving glucuronide moieties 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.

Preparations of beta-glucuronidase from the snail Helix pomatia are commercially available and referred to by the trademark Glusulase. These enzymes preparations 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 this trait is commonly used to identify the bacterium.


Sly syndrome is an inherited disease in which a genetic defect leads to a deficiency in glucuronidase. This results in numerous symptoms because of the accumulation of complex carbohydrates in many tissues and organs of the body.

Use as reporter gene

In molecular biology, beta-glucuronidase is used as a reporter gene to monitor gene expression. Monitoring glucuronidase activity using a so-called GUS assay allows determination of the spatial and temporal expression of the gene being monitored. The beta-glucuronidase enzyme transforms certain substrates into colored or fluorescent products which can then be observed and measured.

External links