General Stability | Organism |
---|---|
unfolding of the enzyme in 8 M urea is strongly inhibited by high concentrations of NaCl | Priestia megaterium |
unstable at low ionic strength, in 67 mM phosphate buffer enzyme activity decreases to 80% within 5 hours at pH 6.5 and 0.01 mg/ml protein, reduction to 57% at 40 mM phosphate, high concentration of NAD inhibit dissociation | Priestia megaterium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Priestia megaterium | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
renaturation of enzyme denatured by urea, restores more than 90% of the original activity 60 min after dilution and after complete dialysis. Optimal temperature for refolding is 25°C | Priestia megaterium |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Priestia megaterium |
4 | - |
30 min, about 50% loss of activity | Priestia megaterium |
5 | 6.5 | 30 min, stable | Priestia megaterium |
7.3 | - |
30 min, about 50% loss of activity | Priestia megaterium |
7.5 | - |
30 min, about 95% loss of activity | Priestia megaterium |
9 | - |
- |
Priestia megaterium |