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β-Glucuronidase inhibitors block the glycosidase that removes glucuronic acid from glucuronide conjugates. In human cells the enzyme acts in lysosomes, where it helps degrade glycosaminoglycans such as heparan, dermatan and chondroitin sulfate. Inherited β-glucuronidase deficiency was reported in 1973 as a new mucopolysaccharidosis, now known as mucopolysaccharidosis type VII (Sly syndrome). Gut bacteria make their own β-glucuronidases, which free drugs and toxins from glucuronides excreted in bile. In a 2010 mouse study, inhibiting the bacterial enzyme reduced the intestinal toxicity of the anticancer drug irinotecan. Saccharolactone, also listed as D-Saccharic acid 1,4-lactone hydrate, is a classic inhibitor, and sanggenol A is a plant-derived one. Escherichia coli β-glucuronidase and the chromogenic substrate 4-nitrophenyl β-D-glucuronide support enzyme assays.
