anthrax lethal factor endopeptidase

{{infobox enzyme

| Name = Anthrax lethal factor endopeptidase

| EC_number = 3.4.24.83

| CAS_number = 477950-41-7

| GO_code =

| image = 1PWU.png

| width =

| caption = Crystallographic structure of anthrax lethal factor (rainbow colored cartoon, N-terminus = blue, C-terminus = red) complexed with the inhibitor GM6001 (space-filling model, carbon = white, oxygen = red, nitrogen = blue).{{PDB|1PWU}}; {{cite journal |vauthors=Turk BE, Wong TY, Schwarzenbacher R, Jarrell ET, Leppla SH, Collier RJ, Liddington RC, Cantley LC | title = The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor | journal = Nat. Struct. Mol. Biol. | volume = 11 | issue = 1 | pages = 60–6 |date=January 2004 | pmid = 14718924 | doi = 10.1038/nsmb708 | s2cid = 39119275 }}

}}

Anthrax lethal factor endopeptidase ({{EC number|3.4.24.83}}, lethal toxin) is an enzyme that catalyzes the hydrolysis of mitogen-activated protein kinase kinases. This enzyme is a component of the lethal factor produced by the bacterium Bacillus anthracis. The preferred cleavage site can be denoted by BBBBxHxH, in which B denotes a basic amino acid Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid.{{cite journal |vauthors=Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC | title = Crystal structure of the anthrax lethal factor | journal = Nature | volume = 414 | issue = 6860 | pages = 229–33 |date=November 2001 | pmid = 11700563 | doi = 10.1038/n35101998 | url = https://deepblue.lib.umich.edu/bitstream/2027.42/62772/1/414229a0.pdf| hdl = 2027.42/62772 | s2cid = 9212908 | hdl-access = free }}