Skip to Content
Merck
All Photos(1)

Key Documents

A6805

Sigma-Aldrich

β-N-Acetylglucosaminidase from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

β-N-Acetyl-D-hexosaminide N-acetylhexosaminohydrolase, β-N-Acetylhexosaminidase

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

form

buffered aqueous solution

specific activity

≥80 units/mg protein

packaging

vial of ≥1.0 unit

foreign activity

β-galactosidase, α-mannosidase, α-fucosidase, neuraminidase, and proteases, none detected (Enzyme is expressed in glycosidase-free host.)

shipped in

wet ice

storage temp.

2-8°C

Gene Information

Streptococcus pneumoniae R6 ... lytB(934406)

Application

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.

Biochem/physiol Actions

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.

Unit Definition

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.

Physical form

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

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Cloning and Expression of the beta-N-Acetylglucosaminidase Gene from Streptococcus pneumoniae GENERATION OF TRUNCATED ENZYMES WITH MODIFIED AGLYCON SPECIFICITY
Clarke V, et al.
The Journal of Biological Chemistry, 270(15), 8805-8814 (1995)
Mutational studies on endo-beta-N-acetylglucosaminidase D which hydrolyzes core portion of asparagine-linked complex type oligosaccharides
Yamamoto S, et al.
Glycoconjugate Journal, 22(1-2), 35-42 (2005)
Remarkable transglycosylation activity of glycosynthase mutants of endo-D, an endo-beta-N-acetylglucosaminidase from Streptococcus pneumoniae
Fan SQ, et al.
The Journal of Biological Chemistry, 287(14), 11272-11281 (2012)
Regulation of the inositol 1, 4, 5-trisphosphate receptor type I by O-GlcNAc glycosylation
Rengifo J, et al.
The Journal of Neuroscience, 27(50), 13813-13821 (2007)
Amelogenin interacts with cytokeratin-5 in ameloblasts during enamel growth
Ravindranath R, et al.
The Journal of Biological Chemistry, 278(22), 20293-20302 (2003)

Articles

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service