Structural highlights
Function
PGDAE_HELPG Catalyzes the N-deacetylation of peptidoglycan (PG), an important mechanism that appears to confer lysozyme resistance and to mitigate host immune detection; this likely contributes to pathogen persistence in the host. The exact nature of the residue in PG that is deacetylated has not been determined. Is also able to catalyze the deacetylation of acetylated xylan, and, to a lesser extent, that of chitin and chitosan. Therefore, this enzyme might play a role during infection, considering that xylan-containing carbohydrate structures are among those commonly consumed by humans (By similarity). In vitro, does not show activity on N-acetylglucosamine (GlcNAc), chitotriose (GlcNAc3), some N-acetyl-dipeptides and allantoinase.[1]
References
- ↑ Shaik MM, Cendron L, Percudani R, Zanotti G. The Structure of Helicobacter pylori HP0310 Reveals an Atypical Peptidoglycan Deacetylase. PLoS One. 2011 Apr 29;6(4):e19207. PMID:21559431 doi:10.1371/journal.pone.0019207
