KEGG   ENZYME: 3.4.24.83Help
Entry
EC 3.4.24.83                Enzyme                                 

Name
anthrax lethal factor endopeptidase;
lethal toxin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
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
Comment
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.
History
EC 3.4.24.83 created 2003
Orthology
K08645  
anthrax lethal toxin endopeptidase
Genes
BAR: 
BAH: 
BAI: 
BAX: 
BAL: 
BCX: 
Taxonomy
Reference
1  [PMID:11700563]
  Authors
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. 414 (2001) 229-33.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
477950-41-7

DBGET integrated database retrieval system