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Literature summary 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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.33 Listeria monocytogenes
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-
-
3.5.1.104 Listeria monocytogenes
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.5.1.33 Lmo0415
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 Listeria monocytogenes
3.5.1.33 Pgd
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 Listeria monocytogenes
3.5.1.104 Pgd
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 Listeria monocytogenes

General Information

EC Number General Information Comment Organism
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 Listeria monocytogenes
3.5.1.104 physiological function mutants lacking N-acetylglucosamine deacetylase Pgd and mutants in both Pgd and O-acetylmuramic acid transferase are attenuated approximately 2 and 3.5 logs, respectively, in vivo. In bone-marrow derived macrophages, the mutants demonstrate intracellular growth defects and increased induction of cytokine transcriptional responses that emanate from a phagosome and the cytosol. Mutants are lysozyme-sensitive and undergo bacteriolysis in the macrophage cytosol, resulting in AIM2-dependent pyroptosis. Each of the in vitro phenotypes is rescued upon infection of LysM macrophages. The addition of extracellular lysozyme to LysM macrophages restores cytokine induction, host cell death, and Listeria monocytogenes growth inhibition. This suggests that extracellular lysozyme can access the macrophage cytosol and act on intracellular lysozyme-sensitive bacteria Listeria monocytogenes