» O-GlcNAcase

Catalogue No.:
PRO-E0255

LOT:
2008-0255

Source Organism:
Streptococcus pyogenes M1 GAS SF370

EC No.:
3.2.1.52

Synonyms:
Hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-β-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase; GlcNAcase; O-glycoprotein 2-acetamido-2-deoxy-β-D-glucopyranosidase

Nomenclature:
CAZy [GH84, glycoside hydrolase family 84], SPy1600

Specific Activity:
5.56 U/mg (pH 7.6; pNP-N-acetyl-β-D-glucosaminide (1 mM))

Accession No.:
NP_269657.1, Q99YP8

Molecular Weight:
67487.4 Da

Biological Function:
The expression of this enzyme is up-regulated during phagocytosis and thus a role in virulence is possible. As the enzyme is unlikely to be secreted, it is likely to be involved in the removal of GlcNAc from a variety of glycoconjugates that are imported into the bacterial cell during pathogenesis. Processing O-GlcNAc from endogenous group A streptococcal proteins within the host bacterium itself appears unlikely, given that no O-GlcNAc transferase-like sequence is present in the genome sequence of this strain. Its genomic organization strongly supports a role in glycan foraging, although given its up-regulation during phagocytosis a direct role in the deglycosylation of human O-GlcNAc proteins for the purpose of compromising the host cell machinery can not be ruled out (Sheldon et al. (2006) Biochem. J. 399, 241-247)

Comments:
The enzyme is only active against β-N-acetylglucosaminides and has no hyaluronidase activity. The enzyme also has been shown to remove O-GlcNAc from eukaryotic glycoproteins (Sheldon et al. (2006) Biochem. J. 399, 241-247). No activity is observed with β-N-acetylgalactosaminides