Enzyme Activity Measurement for Endo-β-N-Acetylglucosaminidases

Creative Enzymes is an industrial biotech company specialized in enzyme activity assays. We partner with diverse and unique customers to support their needs of early-stage research and process optimization. These years, Creative Enzymes has been chasing the highest grade of customer satisfaction, and improving its products, services and quality management constantly. Herein, we are excited to offer the most reliable enzymatic measurement for endo-β-N-acetylglucosaminidases.

Endo-β-N-acetylglucosaminidases (EC 3.2.1.96) are a group of enzymes that catalyze hydrolysis of the β-1,4-glycosidic linkage of the N,N’-diacetylchitobiose moiety in the core of asparagine-linked glycan of various glycoproteins and glycopeptides. Endo-β-N-acetylglucosaminidases can serve as useful tools for elucidating the functions of the oligosaccharides in glycoproteins because the enzymes can release oligosaccharides without causing damage to protein moieties. These enzymes are widely distributed in animals, plants, fungi, and bacteria. Several bacterial enzymes, such as Endo-H secreted by Streptomyces plicatus and Endo-F₁ secreted by Flavobacterium meningosepticum, were cloned and classified into glycoside hydrolase (GH) family 18. The other endo-β-N-acetylglucosaminidases are different from the enzymes of the GH18 family and are classified into the GH family 85. Endo-H is highly specific for hybrid and high-mannose glycans and does not process complex oligosaccharides. This enzyme requires α-Man-(1→3)- α-Man-(1→6)-ß-Man-(1→4)-ß-GlcNAc-(1→4)-GlcNAc-Asn as the minimum substrate for hydrolytic activity. Endo-F₁, has a similar substrate specificity to Endo-H and a high degree of sequence homology, including 32% identity at the amino acid sequence level. Endo-H is one of the most commonly used enzymatic reagents in glycoprotein research and is extensively used in studies of the structure and function of asparagine-linked oligosaccharides. Its selectivity for specific oligosaccharide structures, as well as the complexity of its glycoprotein substrates, makes it of particular interest for crystallographic analysis. Thus, the utilization promotes a strong demand for monitoring the activity of endo-β-N-acetylglucosaminidases.

Fortunately, Creative Enzymes makes the accurate activity assays available for endo-β-N-acetylglucosaminidases. Fully equipped with a skillful team of extraordinary enzymologists, state-of-the-art technology, and advanced instruments, we assure the performance of the activity test in a professional and timely manner. In the future, Creative Enzymes will continue the services as your trust-worthy partner.

Figure: The crystal structure of endo-beta-N-acetylglucosaminidase H from Streptomyces plicatus.
PDB: 1EDT