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
results (
results (Substrates Products
Substrates Products on EC 3.4.24.83 - anthrax lethal factor endopeptidase
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SUBSTRATE 
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
(7-methoxycoumarin-4-yl)acetyl-AKVYPYPME-(2,4-dinitrophenyldiaminopropionic acid) + H2O
(7-methoxycoumarin-4-yl)acetyl-AKVYP + YPME-(2,4-dinitrophenyldiaminopropionic acid)
-
-
-
?
83 kDa full-length protective antigen + H2O
20 kDa N-terminal fragment of protective antigen + 63 kDa N-terminal fragment of protective antigen
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-
-
?
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide + H2O
?
-
-
-
?
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
AcG-Y-betaA-R-R-R-A-R-R-R-R-V-L-R-4-nitroanilide + H2O
AcG-Y-betaA-R-R-R-A-R-R-R-R-V-L-R + 4-nitroaniline
-
-
-
-
?
AcM-L-A-R-R-R-P-V-L-P-4-nitroanilide + H2O
AcM-L-A-R-R-R-P-V-L-P + 4-nitroaniline
-
-
-
-
?
AcR-R-R-R-V-L-R-4-methylcoumarin-7-amide + H2O
AcR-R-R-R-V-L-R + 7-amino-4-methylcoumarin
-
-
-
-
?
AcR-R-R-R-V-L-R-4-nitroanilide + H2O
AcR-R-R-R-V-L-R + 4-nitroaniline
-
-
-
-
?
dansyl-RDIRRITLFSLH
?
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i.e. S20D, substrate isolated from phage library
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-
?
Dsor1 kinase + H2O
?
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Dsor1 is a Drosophila mitogen-activated protein kinase kinase
-
-
?
fluorescein-QRRKKVYPYPME + H2O
fluorescein-QRRKKVYP + YPME
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i.e. LF15, peptide substrate isolated from second-iteration substrate phage library
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-
?
Hep kinase + H2O
?
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Hep (Hemipterous) is a Drosophila mitogen-activated protein kinase kinase
incubation of Hep with anthrax lethal factor generates a product of about 44 kDa
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?
Lic kinase + H2O
?
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Lic (Licorne) is a Drosophila mitogen-activated protein kinase kinase
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-
?
MEK2 + H2O
?
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mitogen-activated protein kinase kinase, cleavage between residues 10-11
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-
?
MKK3b + H2O
?
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mitogen-activated protein kinase kinase, cleavage between residues 26-27
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-
?
MKK4 + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 45-46 and 58-59
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-
?
MKK6b + H2O
?
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mitogen-activated protein kinase kinase, cleavage between residues 14-15
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-
?
MKK7beta + H2O
?
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mitogen-activated protein kinase kinase, cleavage between residues 44-45 and 76-77
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-
?
NACHT leucine-rich repeat and pyrin domain-containing protein 1B + H2O
?
-
-
-
?
NOD-like receptor protein-1 + H2O
?
lethal factor cleaves rat NOD-like receptor protein Nlrp1. Cleavage is required for toxin-induced inflammasome activation, interleukin IL-1beta release, and macrophage pyroptosis
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-
?
acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide + H2O
?
commercial substrate S-pNA
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-
?
MEK1 + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 8-9
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-
?
mitogen-activated protein kinase + H2O
?
-
-
-
-
?
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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substrate: MAPKK4, MAPKK6, MAPKK7, no substrate: MAPKK5
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-
?
mitogen-activated protein kinase + H2O
?
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substrate: MAPKK3, i.e. MKK3
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-
?
mitogen-activated protein kinase + H2O
?
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substrates: MAPKK1, MAPKK2
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-
?
mitogen-activated protein kinase + H2O
?
-
inactivation of substrate
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-
?
mitogen-activated protein kinase kinase + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase + H2O
?
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anthrax lethal toxin cleaves mitogen-activated protein kinase kinase/MEK/MAPKK 1-4 and 6, but not mitogen-activated protein kinase kinase 5 and 7 in murine neutrophils
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-
?
mitogen-activated protein kinase kinase 1 + H2O
?
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specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
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-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
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-
?
mitogen-activated protein kinase kinase 2 + H2O
?
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specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
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-
?
mitogen-activated protein kinase kinase 2 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 3 + H2O
?
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specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
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-
?
mitogen-activated protein kinase kinase 3 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
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-
?
mitogen-activated protein kinase kinase 4 + H2O
?
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specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 4 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 6 + H2O
?
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specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
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-
?
mitogen-activated protein kinase kinase 6 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 7 + H2O
?
-
specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 7 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
additional information
?
-
-
cleavage occurs within the N-terminal proline-rich regions of MAPKKs, consensus motifs
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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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participates in the activation of caspase-1
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-
?
additional information
?
-
-
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
?
-
the enzyme does not degrade mitogen-activated protein kinase kinase 7, Erk1/2, p38 and JNK1/2
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-
?
additional information
?
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the enzyme does not degrade mitogen-activated protein kinase kinase 7, Erk1/2, p38 and JNK1/2
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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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-
?
