β-N-Acetylhexosaminidase, Streptococcus pneumoniae 

β-N-Acetylhexosaminidase, Streptococcus pneumoniae is a cell surface virulence factor of Streptococcus pneumoniae, which contains two synergistically acting GH20 domains (with higher activity in GH20-2). β-N-Acetylhexosaminidase, Streptococcus pneumoniae specifically recognizes and hydrolyzes substrates with β(1,2) glycosidic bonds via Trp-443 and Tyr-482 residues. β-N-Acetylhexosaminidase, Streptococcus pneumoniae catalyzes the hydrolysis of β(1,2)-linked N-acetylglucosamine groups and related disaccharides, and promotes persistent colonization of bacteria in the airway by modifying host defense molecules and releasing monosaccharides for bacterial growth. β-N-Acetylhexosaminidase, Streptococcus pneumoniae can be used in studies related to Streptococcus pneumoniae infection, acute pneumonia, otitis media and meningitis^[1][2].

β-N-Acetylhexosaminidase from Streptococcus pneumoniae specifically hydrolyzes β(1,2)-linked NAG-Man disaccharides; the Trp-443/Tyr-482 residues in the GH20-1 domain and the Trp-876/Tyr-914 residues in the GH20-2 domain are critical for this activity. Substitution of the tyrosine residues completely abolishes the hydrolytic activity against NAGβ(1,2) Man, and the tandem GH20-1&2 recombinant exhibits the highest activity toward this disaccharide (with a k_cat/K_m value of 38.70 min^-1mM^-1)^[2].
β-N-Acetylhexosaminidase from Streptococcus pneumoniae (10 mg/mL) contains a GH20-1 domain that adopts a conserved (β/α)₈ TIM barrel structure, with NAG bound to its active site. Substitution of Tyr with Cys-469 alters the conformation of NAG, resulting in lower enzymatic activity of GH20-1 than that of GH20-2^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Pretreatment of mice with β-N-Acetylhexosaminidase from Streptococcus pneumoniae (225 μg; administered intranasally; single dose 30 minutes prior to bacterial infection) reduces the colonization of S. pneumoniae D39 ΔbgaC mutant strain in the nasopharynx, lungs, and blood at 12 h post-infection^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9012-33-3

Liquid

Colorless to light yellow

[b-N-Acetylhexosaminidase, Streptococcus pneumoniae]

3.2.1.52

≥800 U/L

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Jeong J K, et al. Characterization of the Streptococcus pneumoniae BgaC protein as a novel surface β-galactosidase with specific hydrolysis activity for the Galβ1-3GlcNAc moiety of oligosaccharides[J]. Journal of bacteriology, 2009, 191(9): 3011-3023.

  [2]. Jiang YL, et al. Structural basis for the substrate specificity of a novel β-N-acetylhexosaminidase StrH protein from Streptococcus pneumoniae R6. J Biol Chem. 2011;286(50):43004-43012.