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Literature summary extracted from

  • Kong, Q.; Song, Y.; Mu, M.; Han, X.; Si, C.; Li, F.
    Effects of metalloprotease anthrax lethal factor on its peptide-based inhibitor R9LF-1 (2015), Mol. Cell. Biochem., 406, 293-299 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.83 expressed in Escherichia coli BL21 Star cells Bacillus anthracis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.83 In2LF i.e. Ac-Gly-Tyr-betaAla-(L-Arg)8-Val-Leu-Arg-CONHOH, competitive inhibitor Bacillus anthracis
3.4.24.83 R9LF-1
-
 Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.83 mitogen-activated protein kinase kinase + H2O Bacillus anthracis
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.83 Bacillus anthracis P15917
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.83 His-Trap HP nickel affinity column chromatography Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.83 In2LF + H2O
-
 Bacillus anthracis In2LF fragments
-
 ?
3.4.24.83 mitogen-activated protein kinase kinase + H2O
-
 Bacillus anthracis ?
-
 ?
3.4.24.83 R9LF-1 + H2O
-
 Bacillus anthracis svR9LF-1 + NH2OH
-
 ?

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.24.83 7 8.5 the enzyme degrades R9LF-1 with maximum efficiency in the pH range of 7.0-8.5, which correlates well with the range of enzymatic activity with its native substrate Bacillus anthracis