EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    1.1.1.27 | -999 |
- |
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate |
678544 |
| 1.1.1.27 | -999 |
- |
protection against heat inactivation by 1 mM fructose 1,6-diphosphate, 1 mM ATP, 1 mM glucose 6-phosphate and increased levels of phosphate |
286433 |
| 1.1.1.27 | -999 |
- |
the enzyme from aerobic control muscle has a significantly higher melting temperature (greater thermal stability) compared to the anoxic enzyme form, suggesting that there is a structural difference between the two enzyme forms. Both anoxic and control LDH are most thermally stable around pH 7.6 although the difference in TM between pH 7.3 and pH 7.6 is not significant for the anoxic LDH |
740337 |
| 1.1.1.27 | -999 |
- |
very stable at room temperature, 4°C and 50°C |
667202 |
| 1.1.1.27 | 5 |
35 |
the mean Q10 value for all species is 1.8 |
668320 |
| 1.1.1.27 | 40 |
- |
half-life of wild-type is 50.4 h, of mutant N197D is 77.9 h |
761278 |
| 1.1.1.27 | 45 |
- |
20 min, about 10% loss of activity, isoenzyme A4 |
655268 |
| 1.1.1.27 | 45 |
- |
inactivation above, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments |
688389 |
| 1.1.1.27 | 46 |
- |
1 h, 25°C, 50% loss of activity, mutant enzyme with a deletion of 10 N-terminal amino acids |
654791 |
| 1.1.1.27 | 48 |
- |
30 min, stable up to |
678544 |
