Literature summary for 3.4.24.83 extracted from

Juris, S.J.; Melnyk, R.A.; Bolcome, R.E.; Chan, J.; Collier, R.J.
Cross-linked forms of the isolated N-terminal domain of the lethal factor are potent inhibitors of anthrax toxin (2007), Infect. Immun., 75, 5052-5058.

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Cloned(Commentary)

Cloned (Comment)	Organism
fusion protein between lethal factor and the catalytic domain of diphtheria toxin is expressed in Escherichia coli BL21(DE3) cells	Bacillus anthracis

Inhibitors

Inhibitors	Comment	Organism	Structure
C-terminal dimer of the protective antigen binding domain of anthrax lethal factor	-	Bacillus anthracis
C-terminal trimer of the protective antigen binding domain of anthrax lethal factor	-	Bacillus anthracis
N-terminal dimer of the protective antigen binding domain of anthrax lethal factor	-	Bacillus anthracis
N-terminal trimer of the protective antigen binding domain of anthrax lethal factor	-	Bacillus anthracis

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
mitogen-activated protein kinase + H2O	-	Bacillus anthracis	?	-	?

Synonyms

Synonyms	Comment	Organism
lethal factor	-	Bacillus anthracis

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Release 2023.1 (January 2023)