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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

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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)

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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)
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)
Amelogenin interacts with cytokeratin-5 in ameloblasts during enamel growth
Ravindranath R, et al.
The Journal of Biological Chemistry, 278(22), 20293-20302 (2003)
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)
David J Vocadlo
Current opinion in chemical biology, 16(5-6), 488-497 (2012-11-14)
The addition of N-acetylglucosamine (GlcNAc) O-linked to serine and threonine residues of proteins is known as O-GlcNAc. This post-translational modification is found within multicellular eukaryotes on hundreds of nuclear and cytoplasmic proteins. O-GlcNAc transferase (OGT) installs O-GlcNAc onto target proteins

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.

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