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Literature summary extracted from

  • Fink, S.L.; Bergsbaken, T.; Cookson, B.T.
    Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms (2008), Proc. Natl. Acad. Sci. USA, 105, 4312-4317.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.83 E678C catalytically inactive Bacillus anthracis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.83 additional information Ca2+-free medium completely prevents mitogen-activated protein kinase kinase 3 proteolysis in anthrax lethal toxin-treated macrophages Bacillus anthracis
3.4.24.83 NH4Cl blocks mitogen-activated protein kinase kinase 3 proteolysis in anthrax lethal toxin-treated macrophages Bacillus anthracis
3.4.24.83 verapamil blocks mitogen-activated protein kinase kinase 3 proteolysis in anthrax lethal toxin-treated macrophages Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.36 additional information Mus musculus bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine ?
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Organism

EC Number Organism UniProt Comment Textmining
3.4.22.36 Mus musculus
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3.4.24.83 Bacillus anthracis
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.36 macrophage bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine Mus musculus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.36 additional information bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine Mus musculus ?
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 ?
3.4.24.83 mitogen-activated protein kinase kinase 1 + H2O
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 Bacillus anthracis ?
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 ?
3.4.24.83 mitogen-activated protein kinase kinase 3 + H2O
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 Bacillus anthracis ?
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 ?
3.4.24.83 additional information participates in the activation of caspase-1 Bacillus anthracis ?
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Synonyms

EC Number Synonyms Comment Organism
3.4.24.83 lethal factor
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 Bacillus anthracis