EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.1.13.4 | 30 |
50 |
stable at |
749789 |
| 3.1.13.4 | 45 |
55 |
thermal stability and aggregation kinetic parameters, the aggregation is dominated by a first-order kinetics, increase in t0 and the decrease in k implies that Mg2+ can inhibit the rate of enzyme aggregation, overview. Cofactor Mg2+ is also important to PARN stability against inactivation induced by heat treatment, but promotes thermal aggregation at high temperatures. Mg2+ significantly decreases the rate but increases the aggregate size of the 54 kDa wild-type enzyme in a concentration-dependent manner. Effect of mutations on the Mg2+-dependent enzyme thermal aggregation, overview |
715205 |
| 3.1.13.4 | 49 |
- |
in the absence of Mg2+, the activity of PARN decreases continuously with increasing temperature |
679848 |
| 3.1.13.4 | 49 |
- |
inactivation of the four PARNs at 49°C, p74 is more stable than p54, p54 is equally stable than mutant p54DR3H, mutant p54DR3H is more stable than mutant p74DR3H |
677976 |
| 3.1.13.4 | 55 |
85 |
thermal denaturation of PARN in presence or absence of K+, overview |
749789 |
