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 (Metals Ions
Metals Ions on EC 3.4.24.83 - anthrax lethal factor endopeptidase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
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activation ability of divalent ions decreases in the follwing order: Zn2+ Ca2+ Mn2+ Mg2+, with Mg2+ completely unable to activate the enzyme
Co2+
Cu2+
Mn2+
Ni2+
Co2+ is capable to reactivate the apoprotein of lethal factor to a level comparable to that noted for the native zinc enzyme. Co2+-substituted lethal factor is not capable of killing RAW 264.7 murine macrophage-like cells
Zn2+
Co2+
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Co2+ is capable of directly replacing lethal factors active site Zn2+ to yield a hyperactive enzyme with 2fold higher kcat value and about 2.5fold increased catalytic efficiency
Co2+
Co2+ is capable to reactivate the apoprotein of lethal factor to a level comparable to that noted for the native zinc enzyme. Co2+-substituted lethal factor is not capable of killing RAW 264.7 murine macrophage-like cells
Cu2+
Cu2+-substituted lethal factor, prepared by direct exchange and by apoprotein reconstitution methodologies, displays a several-fold higher catalytic competence towards chromogenic and fluorogenic lethal factor substrates than native lethal factor. Cu2+ is bound tightly with a dissociation constant in the femtomolar range. The protein-bound metal ion is coordinated to two nitrogen donor atoms, suggesting that Cu2+ binds to both active site histidine residues. Cu2+-substituted lethal factor is capable of killing RAW 264.7 murine macrophage-like cells
Cu2+
replacement of Zn2+ by Cu2+ leads to an almost 30fold enhancement of the enzyme activity
Mn2+
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activation ability of divalent ions decreases in the follwing order: Zn2+ Ca2+ Mn2+ Mg2+, with Mg2+ completely unable to activate the enzyme
Mn2+
Co2+ is capable to reactivate the apoprotein of lethal factor to a level comparable to that noted for the native zinc enzyme. Co2+-substituted lethal factor is not capable of killing RAW 264.7 murine macrophage-like cells
Zn2+
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lethal factor along with its receptor-binding partner protective antigen, forms lethal toxin, a critical virulence factor for bacillus anthracis. Lethal factor is a Zn2+ protease
Zn2+
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activation ability of divalent ions decreases in the follwing order: Zn2+ Ca2+ Mn2+ Mg2+, with Mg2+ completely unable to activate the enzyme
Zn2+
content is 1 mole per mole of protein. Zinc content is retained upon acidification up to a pH value of 5.5. At pH 5.3, release of about 40% of zinc, and below pH 4.5, sharp increase in the release of zinc
Zn2+
Zn2+-substituted lethal factor is capable of killing RAW 264.7 murine macrophage-like cells
