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Literature summary extracted from

  • Zakharova, M.Y.; Kuznetsov, N.A.; Dubiley, S.A.; Kozyr, A.V.; Fedorova, O.S.; Chudakov, D.M.; Knorre, D.G.; Shemyakin, I.G.; Gabibov, A.G.; Kolesnikov, A.V.
    Substrate recognition of anthrax lethal factor examined by combinatorial and pre-steady-state kinetic approaches (2009), J. Biol. Chem., 284, 17902-17913.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.83 expression in Escherichia coli Bacillus anthracis

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.83 E687D mutation in metal-binding site, decrease in catalytic activity Bacillus anthracis
3.4.24.83 H690A mutation in metal-binding site, decrease in catalytic activity Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.83 0.0023
-
 fluorescein-QRRKKVYPYPME wild-type, pH 7.4, 37°C Bacillus anthracis
3.4.24.83 0.0174
-
 fluorescein-QRRKKVYPYPME mutant E687D, pH 7.4, 37°C Bacillus anthracis
3.4.24.83 0.042
-
 fluorescein-QRRKKVYPYPME mutant H690A, pH 7.4, 37°C Bacillus anthracis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.83 Ca2+ activation ability of divalent ions decreases in the follwing order: Zn2+ Ca2+ Mn2+ Mg2+, with Mg2+ completely unable to activate the enzyme Bacillus anthracis
3.4.24.83 Mn2+ activation ability of divalent ions decreases in the follwing order: Zn2+ Ca2+ Mn2+ Mg2+, with Mg2+ completely unable to activate the enzyme Bacillus anthracis
3.4.24.83 additional information Mg2+ is unable to activate Bacillus anthracis
3.4.24.83 Zn2+ activation ability of divalent ions decreases in the follwing order: Zn2+ Ca2+ Mn2+ Mg2+, with Mg2+ completely unable to activate the enzyme Bacillus anthracis

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.83 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 pre-steady-state kinetics of anthrax lethal factor proteolysis follows a four-step mechanism as follows: initial substrate binding, rearrangement of the enzyme-substrate complex, a rate-limiting cleavage step, and product release Bacillus anthracis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.83 dansyl-RDIRRITLFSLH i.e. S20D, substrate isolated from phage library Bacillus anthracis ?
-
 ?
3.4.24.83 fluorescein-QRRKKVYPYPME + H2O i.e. LF15, peptide substrate isolated from second-iteration substrate phage library Bacillus anthracis fluorescein-QRRKKVYP + YPME
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.24.83 0.01
-
 fluorescein-QRRKKVYPYPME mutant H690A, pH 7.4, 37°C Bacillus anthracis
3.4.24.83 0.1
-
 fluorescein-QRRKKVYPYPME mutant E687D, pH 7.4, 37°C Bacillus anthracis
3.4.24.83 0.52
-
 fluorescein-QRRKKVYPYPME wild-type, pH 7.4, 37°C Bacillus anthracis