PRO-E0255
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More information| Catalogue No. | PRO-E0255 |
|---|---|
| EC | 3.2.1.52 |
| Synonyms | Hexosaminidase; ?acetylaminodeoxyhexosidase; N-acetyl-?-Dhexosaminidase; N-acetyl-?-hexosaminidase; ?hexosaminidase; ?-acetylhexosaminidinase; ?-D-N-acetylhexosaminidase; ?-N-acetyl-D-hexosaminidase; ?-Nacetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; ?-D-hexosaminidase; GlcNAcase; Oglycoprotein 2-acetamido-2-deoxy-?-D-glucopyranosidase |
| Nomenclature | CAZy [GH84 | glycoside hydrolase family 84] | SPy1600 |
| Specific Activity | 5.56 U/mg (pH 7.6; pNP-N-acetyl-?-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 OGlcNAc 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 ?-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 ?-N-acetylgalactosaminides |
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