DefinitionThis section has been translated automatically.
Enzyme class of ubiquitously occurring (animals, plants, fungi), mostly relatively unspecific hydrolases (this concerns mainly intestinal enzymes), which cleave glycosidic bonds into carbohydrates, glycoproteins and glycolipids. Glycosidases reversibly catalyse the hydrolytic cleavage of a glycosidic bond, whereby a sugar (glycone) and the so-called aglycone are released when a water molecule is consumed.
Examples of enzymes of the glycosidase type are amylases, disaccharidases (e.g. lactase = beta-galactosidase which cleaves lactose in the intestine, see alsolactose intolerance), cellulases (only cleave cellulose, e.g. rumen bacteria in ruminants), invertases. Such glycosidases (sensibly) mostly have a non-specific effect and hydrolyse a relatively broad spectrum of glycosides.
LiteratureThis section has been translated automatically.
- Brás NF et al (2014)Glycosidase inhibitors: a patent review (2008-2013). Expert Opinion Ther Pat 24:857-874.