EC Number   |
General Stability |
Reference |
|---|
    2.4.2.8 | 5-phospho-alpha-D-ribose 1-diphosphate stabilizes |
638391 |
| 2.4.2.8 | 5-phospho-alpha-D-ribose 1-diphosphate stabilizes against heat inactivation |
638393 |
| 2.4.2.8 | activation by substrate and product IMP destabilizes the enzyme, the unactivated ligand-free enzyme is more stable |
661691 |
| 2.4.2.8 | analysis of the stability of the variants in urea-induced unfolding experiments. Protein aggregation is taking place after dialysis or denaturant dilution, an indication of the existence of an irreversible phenomenon, precludes the derivation of thermodynamic state functions from the unfolding data. Nevertheless, the enzyme behaves as cooperative folding units when submitted to chemical denaturation, irreversible aggregation at 60°C within 10 min |
758845 |
| 2.4.2.8 | DTT and hypoxanthine stabilize |
638414 |
| 2.4.2.8 | glycerol or sucrose or dimethylsulfoxide stabilizes the purified enzyme at -70°C |
638396 |
