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Literature summary for 3.5.1.33 extracted from

  • Rae, C.S.; Geissler, A.; Adamson, P.C.; Portnoy, D.A.
    Mutations of the Listeria monocytogenes peptidoglycan N-deacetylase and O-acetylase result in enhanced lysozyme sensitivity, bacteriolysis, and hyperinduction of innate immune pathways (2011), Infect. Immun., 79, 3596-3606.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-glucosamine + H2O
-
 Listeria monocytogenes D-glucosamine + acetate
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 ?

Synonyms

Synonyms Comment Organism
Lmo0415
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 Listeria monocytogenes
Pgd
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 Listeria monocytogenes

General Information

General Information Comment Organism
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 Listeria monocytogenes