EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
---|
6.3.4.3 | -999 |
- |
NH4+ and K+, but not Na+ increase the thermostability |
1513 |
6.3.4.3 | -999 |
- |
the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ increases the denaturation temperature by 12°C and abolishes the cold lability of the enzyme |
1503 |
6.3.4.3 | -999 |
- |
thermolability is reduced by magnesium adenosine triphosphate and eliminated by the substrate analog folate pentaglutamate, suggesting that folate status may modulate impact of the variant R653Q |
698187 |
6.3.4.3 | 23 |
- |
the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase is more stable at 23°C than at 0°C |
1532 |
6.3.4.3 | 47 |
- |
transition at 47°C is due to the denaturation of a domain which binds MgATP2- and contains the synthetase active site |
1532 |
6.3.4.3 | 69 |
- |
in the absence of monovalent cation |
649939 |
6.3.4.3 | 70 |
- |
10 min stable |
1502 |
6.3.4.3 | 70 |
- |
rapid inactivation in absence of NH4Cl. In presence of 50 mM NH4Cl, about 50% loss of activity after 15 min and no more loss of activity thereafter |
1513 |
6.3.4.3 | 75 |
- |
rapid denaturation |
1502 |
6.3.4.3 | 79 |
- |
in the presence of 200 mM K+ |
649939 |