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4-Methylumbelliferyl β-D-glucopyranoside has been used as substrate: · in glucosylceramidase β enzyme activity assay in lysosome-enriched fractions from primary hippocampal neurons · in β-glucosidase assay during yeast fermentation · to assay glucocerebrosidase 1 (GBA1)-related glucosidase activity in macrophage cell line (RAW)

4-Methylumbelliferyl β-D-glucopyranoside is a synthetic enzymatic substrate for glycosidase. It has been used as substrate for the β- glucosidase from enterococci.

We report that simple glycoside donors can drastically shift the equilibria of glycosyltransferase-catalyzed reactions, transforming NDP-sugar formation from an endothermic to an exothermic process. To demonstrate the utility of this thermodynamic adaptability, we highlight the glycosyltransferase-catalyzed synthesis of 22 sugar nucleotides from simple aromatic sugar donors, as well as the corresponding in situ formation of sugar nucleotides as a driving force in the context of glycosyltransferase-catalyzed reactions for small-molecule glycodiversification. These simple aromatic donors also enabled a general colorimetric assay for glycosyltransfer, applicable to drug discovery, protein engineering and other fundamental sugar nucleotide-dependent investigations. This study directly challenges the general notion that NDP-sugars are ‘high-energy’ sugar donors when taken out of their traditional biological context.(From “Using simple donors to drive the equilibria of glycosyltransferase-catalyzed reactions”)