β-N-Acetylglucosaminidase from Streptococcus pneumoniae

β-N-Acetylglucosaminidase from Streptococcus pneumoniae has been used in the removal of O-linked sugars from inositol 1,4,5-trisphosphate (InsP3) receptor type I. It has also been used in coating PVDF strips for amelogenin trityrosyl motif peptide (ATMP) and keratin 5 binding studies.

β-N-Acetylglucosaminidase from Streptococcus pneumoniae is an extracellular glycosidase and has broad specificity over the β1-3 and β1-6 linkages present in mucins. It belongs to the glycoside hydrolase family 85 (GH85). Also called endo-β-N-acetylglucosaminidase, it cleaves at the asparagine residue of the di-N-acetylchitobiose structure in oligosaccharides and acts on fucosylated N-glycan core. Its deglycosylation functionality is exploited in studying functions of glycoproteins.

Specific for GlcNAc; not significantly active with GalNAc

This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates.

One unit will hydrolyze 1.0 μmole of p-nitrophenyl N-acetyl-β-D-glucosaminide to p-nitrophenol and N-acetyl-D-glucosamine per min at the pH 5 at 37 °C.

Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl