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
-
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
- 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 (pH Range
pH Range on EC 3.4.24.83 - anthrax lethal factor endopeptidase
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pH RANGE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5.8
progressive further loss of activity. Biphasic loss of activity upon acidification
6.7
about 60% of maximum activity. Biphasic loss of activity upon acidification
7 - 8.5
the enzyme degrades R9LF-1 with maximum efficiency in the pH range of 7.0-8.5, which correlates well with the range of enzymatic activity with its native substrate
