EC Number   |
General Information |
Reference |
|---|
   3.5.1.33 | malfunction |
in bone-marrow derived macrophages, N-acetylglucosamine deacetylase and O-acetylmuramic acid transferase double-deficient mutants demonstrate intracellular growth defects and increased induction of cytokine transcriptional responses that emanated from a phagosome and the cytosol. N-acetylglucosamine deacetylase deficient Listeria monocytogenes bacteria are sensitive to 0.05 mg/ml lysozyme, undergo increased bacteriolysis in the macrophage cytosol, induce AIM2-dependent pyroptosis and increased vacuolar and cytosolic cytokine signaling, demonstrate intracellular growth defects that are rescued in the absence of lysozyme M and in vivo defects that are not rescued in the absence of lysozyme M |
719589 |
| 3.5.1.33 | malfunction |
inactivation of the N-acetylglucosamine deacetylase gene leads to fully acetylated peptidoglycan, resulting in a lysozyme-sensitive phenotype |
-, 719610 |
| 3.5.1.33 | malfunction |
the pgdA-knockout strain shows a significant increase in aggregation/agglutination by salivary agglutinin |
712310 |
| 3.5.1.33 | physiological function |
N-acetylglucosamine deacetylase gene overexpression leads to an increased degree of peptidoglycan deacetylation, resulting in a lysozyme-resistant phenotype. N-Acetylglucosamine deacetylase does not confer any advantage in the persistence of Lactococcus lactis in the gastrointestinal tract and its ability to enhance host immune responses induced by delivered antigen in situ |
-, 719610 |
| 3.5.1.33 | physiological function |
PgdA is an active, metal-dependent CE4 esterase that plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin |
712310 |
