EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.4.21.53 | -999 |
- |
loses DNA-binding ability, not ATP-dependent protease activity after heat-shock treatment |
29345 |
| 3.4.21.53 | -999 |
- |
the thermophilic nature of Lon protease is due to the special features of the enzyme activity regulation, the structure of ATPase domain, and the quaternary structure |
682848 |
| 3.4.21.53 | -999 |
- |
thermophilic nature of lon protease is due to special features of enzyme activity regulation, structure of ATPase domain, and quaternary structure |
682848 |
| 3.4.21.53 | 21 |
- |
rapid loss of activity in the absence of glycerol. ATP, AMP-PNP or ADP stabilizes, E. coli |
29360 |
| 3.4.21.53 | 30 |
- |
pure active Lon is unstable at 30°C |
653632 |
| 3.4.21.53 | 30 |
- |
the pure active lon is unstable at 30°C, presumably because it cleaves itself, but degradation is prevented by 1 mM ATP or AMP-PNP. These nucleotides stabilize both the individual subunits as well as the oligomeric enzyme, suggesting that stabilization required binding but not hydrolysis of ATP |
653632 |
| 3.4.21.53 | 30 |
37 |
can substitute for yeast protease at 30°C, but inable to maintain respiration at 37°C |
651853 |
| 3.4.21.53 | 37 |
- |
rapid denaturation, ATP, AMP-PNP or ADP stabilizes, E. coli |
29360 |
| 3.4.21.53 | 42 |
- |
1 h, 80% loss of activity, 3 mM ATP stabilizes, ADP or AMP less effectively, not Mg2+ |
29340 |
| 3.4.21.53 | 71.5 |
- |
melting temperature |
668468 |
