Literature summary for 3.4.24.83 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus anthracis

Protein Variants

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

KM Value [mM]

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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
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
additional information	Mg2+ is unable to activate	Bacillus anthracis
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

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	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)

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

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)