| EC |
3.4.24.83 |
| Accepted name: |
anthrax lethal factor endopeptidase |
| 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 |
| Other name(s): |
lethal toxin |
| Comments: |
From the bacterium Bacilus anthracis that causes anthrax. One of three proteins that are collectively termed anthrax toxin. Cleaves several MAP kinase kinases near their N-termini, preventing them from phosphorylating the downstream mitogen-activated protein kinases. In peptidase family M34. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 477950-41-7 |
| References: |
| 1. |
Pannifer, A.D., Wong, T.Y., Schwarzenbacher, R., Renatus, M., Petosa, C., Bienkowska, J., Lacy, D.B., Collier, R.J., Park, S., Leppla, S.H., Hanna, P. and Liddington, R.C. Crystal structure of the anthrax lethal factor. Nature 414 (2001) 229–233. [DOI] [PMID: 11700563] |
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| [EC 3.4.24.83 created 2003] |
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