EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    1.2.1.8 | -999 |
- |
mutant enzyme E103Q appears to be more heat labile than the wild-type enzyme. Mutant enzyme E103Q and wild-type enzyme are protected by NAD+ against thermal inactivation in a similar manner. Neither glycine betaine nor NaCl can afford protection against thermal inactivation in the mutant enzyme whereas some protection is observed in the wild-type enzyme |
655947 |
| 1.2.1.8 | 34.3 |
- |
apparent T50 mutant C439V |
672437 |
| 1.2.1.8 | 37 |
- |
apparent T50 mutant C439S |
672437 |
| 1.2.1.8 | 40 |
- |
loss of activity, activity is regained, when the heated enzyme is cooled to 30°C or lower |
390359 |
| 1.2.1.8 | 40 |
- |
pH 7.4, 0.01% 2-mercaptoethanol, 7 min, 50% loss of activity |
390342 |
| 1.2.1.8 | 43.6 |
- |
apparent T50 mutant C439A |
672437 |
| 1.2.1.8 | 45 |
- |
120 min, about 80% decrease of activity |
390350 |
| 1.2.1.8 | 46 |
- |
apparent T50 mutant C377A |
672437 |
| 1.2.1.8 | 47.2 |
59.9 |
thermal stability of the pkBADH-NAD+ complex in the presence of K+ shows a complete loss of the ellipticity signal and highly cooperative thermal transitions in each thermogram in the presence of each K+ concentration tested. In all tested conditions, the thermal denaturation is irreversible. The first derivative analysis from the pkBADH-NAD+ complex shows a peak with a (Tm)app value of 47.2°C, the addition of 25 mM K+ increased the (Tm)app to 59.9°C, while the addition of 50 mM or 100 mM K+ provokes changes in the (Tm)app to 55.9°C or 54.9°C, respectively. Binding of NAD+ to pkBADH causes a lower thermal stability of the enzyme |
763411 |
| 1.2.1.8 | 49.4 |
- |
apparent T50 mutant C353A |
672437 |
