EC Number   |
General Stability |
Reference |
|---|
    1.1.1.42 | 3 M NaCl stabilizes the recombinant enzyme |
655604 |
| 1.1.1.42 | enzyme stability is mainly sensitive to cations and very little or not sensitive to anions. Divalent cations induce a strong shift of the active/inactive transition towards low salt concentration. Deactivation due to incubation of the enzyme at low NaCl concentrations is related to irreversible dissociation of the active dimeric species towards a monomer, which can be described as an extended inactive monomeric species |
727460 |
| 1.1.1.42 | instable in solutions of low ionic strength, stabilization by ammonium sulfate |
286749, 286782 |
| 1.1.1.42 | low molecular weight form of Acinetobacter calcoaceticus enzyme more heat stable than high molecular weight form |
286781 |
| 1.1.1.42 | Mg2+ stabilizes the enzyme during purification |
655035 |
| 1.1.1.42 | stabilization by dithiothreitol |
286788 |
| 1.1.1.42 | the activity of the enzyme treated with Escherichia coli isocitrate dehydrogenase kinase/phosphatase immediately decreases by 80% within 9 min |
760653 |
| 1.1.1.42 | the enzyme activity drops continuously per time during 500 min measurements with an average lost of 1.1% of enzyme activity per 10 min |
761784 |
| 1.1.1.42 | the inter-domain ionic network might be responsible for additional stabilization through a significant kinetic barrier in the unfolding pathway that can explain the larger difference observed between the folding and unfolding transitions of the wild type comparted to the mutant enzyme R211M |
727432 |
| 1.1.1.42 | with a residual amount of secondary structure |
727460 |
