thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of this hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability
the wild type enzyme and mutant enzyme K422R shows complete loss of activity after 15 min at 4°C, the mutant enzyme H391Y shows 36% loss of activity after 15 min at 4°C
thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of the hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability
almost complete loss of activity after 7 min. Addition of 1 M (NH4)2SO4 effectively stabilizes the enzyme agianst heat inactivation, retaining about 50% residual activity after incubation at 120 min
half-life: about 20 min, almost complete loss of activity after 120 min, native and recombinant enzyme, about 40% residual activity after 120 min incubation in presence of 1 M (NH4)2SO4
in N-tris[hydroxymethyl]methyl-2-aminoethane-sulfonic acid buffer, pH 7.9, 1% glycerol, 0.04 mM DTT, isozyme PKp: t1/2: 1.5 min, ADP and MgCl2 preserve activity over 10 min, isozyme PKc: at least 30 min
the wild type enzyme shows 56% loss of activity after 3 h at 37°C, the mutant enzyme K422R shows 80% loss of activity after 3 h at 37°C, the mutant enzyme H391Y shows 1% loss of activity after 3 h at 37°C
the wild type enzyme and mutant enzyme K422R show complete loss of activity after 10 min at 60°C, while mutant enzyme H391Y displays only 2% loss of activity after 10 min at 60°C