Arthrobacter endo-β-N-acetylglucosaminidase (Endo-A), a member of glycoside hydrolase (GH) family 85, catalyses the hydrolysis and transglycosylation of asparagine-linked oligosaccharides of glycoproteins with retention of anomeric configuration. Glu-173 of Endo-A is a catalytically essential amino acid residue, and the corresponding residue is conserved in all GH family 85 members. The catalytic activity of Endo-A E173A mutant was rescued by the addition of sodium azide or sodium formate. Furthermore, the produced β-glycosyl azide (Man 5GlcNAc-β-N 3) retained the anomeric configuration, indicating that Glu-173 is the catalytic acid-base residue of Endo-A. This is the first identification of the catalytic residue for GH family 85 endo-β-N-acetylglucosaminidases.
|Number of pages||6|
|Journal||Journal of biochemistry|
|Publication status||Published - Sept 2007|
All Science Journal Classification (ASJC) codes
- Molecular Biology