Anthrax lethal factor endopeptidase

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Anthrax lethal factor endopeptidase
1PWU.png
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).[1]
Identifiers
EC number 3.4.24.83
CAS number 477950-41-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Anthrax lethal factor endopeptidase (EC 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.[2]

References[edit]

  1. ^ PDB 1PWU; Turk BE, Wong TY, Schwarzenbacher R, Jarrell ET, Leppla SH, Collier RJ, Liddington RC, Cantley LC (January 2004). "The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor". Nat. Struct. Mol. Biol. 11 (1): 60–6. doi:10.1038/nsmb708. PMID 14718924. 
  2. ^ Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC (November 2001). "Crystal structure of the anthrax lethal factor". Nature 414 (6860): 229–33. doi:10.1038/n35101998. PMID 11700563.