Biology:Anthrax lethal factor endopeptidase
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| Anthrax lethal factor endopeptidase | |||||||||
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 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 | ||||||||
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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
- ↑ PDB: 1PWU; "The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor". Nat. Struct. Mol. Biol. 11 (1): 60–6. January 2004. doi:10.1038/nsmb708. PMID 14718924.
- ↑ "Crystal structure of the anthrax lethal factor". Nature 414 (6860): 229–33. November 2001. doi:10.1038/n35101998. PMID 11700563. https://deepblue.lib.umich.edu/bitstream/2027.42/62772/1/414229a0.pdf.
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