3.4.24.83: anthrax lethal factor endopeptidase
This is an abbreviated version!
For detailed information about anthrax lethal factor endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.83
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3.4.24.83
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edema
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spore
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intoxication
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endosomal
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exotoxin
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metalloprotease
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inhalation
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inflammasome
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endocytosis
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toxin-induced
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anti-pa
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heptameric
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caspase-1
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sterne
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furin
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mapkks
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lt-induced
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tripartite
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diphtheria
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toxin-mediated
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spore-forming
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pyroptosis
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toxemia
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ring-shaped
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receptor-bound
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toxin-neutralizing
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zinc-dependent
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molecular biology
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cytolysis
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pa-binding
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medicine
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mkk
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bioterrorism
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diagnostics
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toxin-sensitive
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synthesis
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postexposure
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cell-binding
- 3.4.24.83
-
edema
- spore
-
intoxication
- endosomal
-
exotoxin
- metalloprotease
-
inhalation
- inflammasome
-
endocytosis
-
toxin-induced
-
anti-pa
-
heptameric
- caspase-1
- sterne
- furin
- mapkks
-
lt-induced
-
tripartite
- diphtheria
-
toxin-mediated
-
spore-forming
-
pyroptosis
- toxemia
-
ring-shaped
-
receptor-bound
-
toxin-neutralizing
-
zinc-dependent
- molecular biology
-
cytolysis
-
pa-binding
- medicine
- mkk
-
bioterrorism
- diagnostics
-
toxin-sensitive
- synthesis
-
postexposure
-
cell-binding
Reaction
Preferred amino acids around the cleavage site can be denoted BBBBxHx-/-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases =
Synonyms
anthrax lethal factor, anthrax lethal factor protease, anthrax lethal toxin, anthrax LF, anthrax toxin lethal factor, Bacillus anthracis lethal toxin, lethal factor, lethal factor of anthrax toxin, lethal toxin, LeTx, LF, LTx
ECTree
3.4.24.83 anthrax lethal factor endopeptidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.24.83 - anthrax lethal factor endopeptidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NACHT leucine-rich repeat and pyrin domain-containing protein 1B + H2O
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?
mitogen-activated protein kinase + H2O
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cleavage within N-terminus of MAPKKs
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?
mitogen-activated protein kinase + H2O
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inactivation of substrate
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?
additional information
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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
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?
additional information
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anthrax lethal factor cleaves and inactivates extracellular signal-regulated kinase kinases of the mitogen-activated protein kinase pathway in human dermal microvascular endothelial cells
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additional information
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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
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additional information
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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
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?
additional information
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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
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?
additional information
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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
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