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Literature summary for 3.4.22.36 extracted from

  • Hsu, L.C.; Ali, S.R.; McGillivray, S.; Tseng, P.H.; Mariathasan, S.; Humke, E.W.; Eckmann, L.; Powell, J.J.; Nizet, V.; Dixit, V.M.; Karin, M.
    A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide (2008), Proc. Natl. Acad. Sci. USA, 105, 7803-7808.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
NOD2 NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in muramyl dipeptide-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
transient co-expression of of FALG-tagged NOD2, Myc-tagged caspase-1, and pro-interleukin-1beta in HEK293T cells allows muramyl dipeptide-induced pro-interleukin-1beta processing Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information defective Anthrax-induced interleukin-1beta secretion in Nod2-/- or caspase-1-/- macrophages, not due to decreased pro-interleukin-1beta expression, caspase-1 or NOD2 deficiencies do not exert a major effect on TNF-alpha secretion Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pro-interleukin-1beta + H2O Mus musculus caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells interleukin-1beta + ?
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
macrophage
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Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pro-interleukin-1beta + H2O caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells Mus musculus interleukin-1beta + ?
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?