BERGlykosylasen

BERGlykosylasen is a term used in some German-language literature to refer to enzymes that hydrolyze β-glycosidic bonds in glycosides and glycoconjugates. More broadly, these enzymes are grouped as β-glycosidases within the family of glycoside hydrolases (GH). They cleave the bond between a sugar and an aglycone or between two sugars when the anomeric carbon is in the beta configuration.

Function and general role: BERGlykosylasen catalyze the hydrolysis of a wide range of β-glycosidic substrates, releasing monosaccharides such as glucose or galactose and various aglycones. They participate in digestion (for example in the gut), plant and microbial carbohydrate metabolism, and processing of glycoconjugates in cells. Some act exo-wise, removing terminal glycosyl residues, while others act endo-wise on internal linkages.

Mechanism and structure: Most BERGlykosylasen use either a retaining or an inverting mechanism, depending on the GH family, with catalytic carboxylates (often glutamate residues) acting as acid/base and nucleophile. Structural families vary, but many enzymes possess catalytic domains belonging to known GH folds (including TIM-barrel and (β/α)8 structures) and can be modular, with additional carbohydrate-binding modules that enhance substrate recognition.

Examples and diversity: The most studied representatives include β-glucosidases, β-galactosidases, and β-xylosidases, found in bacteria, fungi, plants, and animals. Substrate specificity ranges from broad to highly selective.

Applications and relevance: BERGlykosylasen are used in biomass degradation, food processing, and biotechnological synthesis of glycosides. In humans, human β-glycosidases are essential lysosomal enzymes; deficiencies can cause storage diseases, underscoring medical relevance.