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Literature summary for 3.4.24.83 extracted from

  • Duesbery, N.S.; Webb, C.P.; Leppla, S.H.; Gordon, V.M.; Klimpel, K.R.; Copeland, T.D.; Ahn, N.G.; Oskarsson, M.K.; Fukasawa, K.; Paull, K.D.; Vande Woude, G.F.
    Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor (1998), Science, 280, 734-737.
    View publication on PubMed
Search for more literature for 3.4.24.83

Protein Variants

Protein Variants Comment Organism
E687C inactive Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
mitogen-activated protein kinase + H2O Bacillus anthracis inactivation of substrate ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 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 Bacillus anthracis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mitogen-activated protein kinase + H2O substrates: MAPKK1, MAPKK2 Bacillus anthracis ?
-
 ?
mitogen-activated protein kinase + H2O inactivation of substrate Bacillus anthracis ?
-
 ?