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Literature summary for 3.4.24.83 extracted from

  • Lo, S.; Säbel, C.; Webb, M.; Walsby, C.; Siemann, S.
    High metal substitution tolerance of anthrax lethal factor and characterization of its active copper-substituted analogue (2014), J. Inorg. Biochem., 140, 12-22.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.073
-
 acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide pH 7.4, 22°C, apoprotein reconstituted in presence of Zn2+ Bacillus anthracis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Co2+ is capable to reactivate the apoprotein of lethal factor to a level comparable to that noted for the native zinc enzyme. Co2+-substituted lethal factor is not capable of killing RAW 264.7 murine macrophage-like cells Bacillus anthracis
Cu2+ Cu2+-substituted lethal factor, prepared by direct exchange and by apoprotein reconstitution methodologies, displays a several-fold higher catalytic competence towards chromogenic and fluorogenic lethal factor substrates than native lethal factor. Cu2+ is bound tightly with a dissociation constant in the femtomolar range. The protein-bound metal ion is coordinated to two nitrogen donor atoms, suggesting that Cu2+ binds to both active site histidine residues. Cu2+-substituted lethal factor is capable of killing RAW 264.7 murine macrophage-like cells Bacillus anthracis
Mn2+ Co2+ is capable to reactivate the apoprotein of lethal factor to a level comparable to that noted for the native zinc enzyme. Co2+-substituted lethal factor is not capable of killing RAW 264.7 murine macrophage-like cells Bacillus anthracis
Ni2+ Co2+ is capable to reactivate the apoprotein of lethal factor to a level comparable to that noted for the native zinc enzyme. Co2+-substituted lethal factor is not capable of killing RAW 264.7 murine macrophage-like cells Bacillus anthracis
Zn2+ Zn2+-substituted lethal factor is capable of killing RAW 264.7 murine macrophage-like cells Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis P15917
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.24
-
 pH 7.4, 22°C, apoprotein reconstituted in presence of Zn2+ Bacillus anthracis
7.12
-
 pH 7.4, 22°C, apoprotein reconstituted in presence of Cu2+ Bacillus anthracis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide + H2O commercial substrate S-pNA Bacillus anthracis ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
21.2
-
 acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide pH 7.4, 22°C, apoprotein reconstituted in presence of Cu2+ Bacillus anthracis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2900
-
 acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide pH 7.4, 22°C, apoprotein reconstituted in presence of Zn2+ Bacillus anthracis