EC Number   |
General Stability |
Reference |
|---|
    2.7.4.9 | dissociation of the native dimeric species of the enzyme occurs at an urea concentration of around 4 M, leading to the accumulation of partially folded monomers that unfold totally at urea concentrations above 5.5 M |
645207 |
| 2.7.4.9 | dTDP and dTTP are effective as enzyme stabilizer |
645188 |
| 2.7.4.9 | midpoint transition is 3.0 M urea for the wild-type enzyme and 3.3 M for the G146A mutant enzyme |
645202 |
| 2.7.4.9 | the canonical enzyme is stable and its activity is not affected by the presence of NaCl |
759870 |
| 2.7.4.9 | the enzyme from outer mitochondrial membrane is unstable and loses activity rapidly, it also loses activity in the presence of a high concentration of NaCl |
759870 |
| 2.7.4.9 | the enzyme is very labile and can be stabilized for long periods of time by its substrate thymidine 5'-monophosphate in the presence of 2-mercaptoethanol |
645194 |
| 2.7.4.9 | the enzyme is very unstable and may be stabilized in the presence of 2-mercaptoethanol with dTMP, dTDP, or ADP but not with ATP, MgATP2- or mercaptoethanol alone |
645196 |
| 2.7.4.9 | the stability of the enzyme is maintained during purification by the constant presence of dTMP and 2-mercaptoethanol and by the elimination of substrate-destoying phosphatase activity |
645188 |
