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Literature summary for 3.4.24.83 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)

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

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus anthracis P15917
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

pH Range

pH Minimum pH Maximum Comment Organism
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