EC Number   |
Natural Substrates |
|---|
   3.4.24.83 | more |
an extremely polymorphic gene in the locus Nalp1b, is the primary mediator of mouse macrophage susceptibility to LeTx. LeTx-induced macrophage death requires caspase-1, which is activated in susceptible, but not resistant, macrophages after intoxication, suggesting that Nalp1b directly or indirectly activates caspase-1 in response to LeTx |
| 3.4.24.83 | more |
lethal factor acts directly on T and B lymphocytes, blocking antigen receptor-dependent proliferation, cytokine production and Ig production. In this manner, lethal factor mounts a broad-based attack on host-immunity, thus providing Bacillus anthracis with multiple mechanisms for avoiding protective host responses |
| 3.4.24.83 | more |
anthrax lethal factor cleaves and inactivates extracellular signal-regulated kinase kinases of the mitogen-activated protein kinase pathway in human dermal microvascular endothelial cells |
| 3.4.24.83 | more |
lethal toxin treatment of murine J774A.1 macrophages results in caspase-1 recruitment to the Nalp1b-containing complex, concurrent with processing of cytosolic caspase-1 substrates. Nalp1b belongs to the NLR family of intracellular surveillance proteins, which are able to recognize pathogen-associated molecular patterns, including lipopolysaccharide (LPS). Nalp1b and caspase-1 are able to interact with each other |
| 3.4.24.83 | more |
prevention of inflammatory response of immune system by preventing interleukin-8 expression: selective blocking of histone H3 phosphorylation at serine 10 and acetylation at lysine 14, H3 normally promotes the accessibility of NF-kappaB (transcription factor for inflammatory gene expression) to target promoters, the histone blocking is mitigated by cleaving mitogen-activated protein kinase kinase, thus preventing the activation of p38-mitogen-activated protein kinase and extracellular signal-regulated kinase |
| 3.4.24.83 | more |
lethal factor cleaves it substrates between P1 and P1 and has a broad specificity with preference toward hydrophobic residues, but not charged or branched residues. The most preferred residues are, from P1 to P3, Trp, Leu, Met, Tyr, Pro, and Leu |
| 3.4.24.83 | NACHT leucine-rich repeat and pyrin domain-containing protein 1B + H2O |
- |
| 3.4.24.83 | SKARRKKVYPYPXENFPPSTARPT + H2O |
- |
