EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
---|
1.2.1.9 | -999 |
- |
effect of NADP+ on the thermostability and the irreversible thermal denaturation of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. The enzyme-NADP+ binary complex shows a strongly decreased thermal stability, with a difference of about 20°C between the temperatures of the thermal transition peak maxima of the complex and the free protein. GAPN thermal inactivation is considerably decelerated in the presence of NADP+ showing that the apparent change in stability of the active centre can be the opposite to that of the whole protein molecule. NADP+ can also reactivate the inactive GAPN species, obtained by heating of the apoenzyme below the thermal denaturation transition temperature. The mechanism provides GAPN the sufficient flexibility for the earlier observed profound active site reorganizations required during the catalytic cycle. The elevated thermal stability of the apoenzyme may, in turn, be important for maintaining a constant level of active GAPN |
741834 |
1.2.1.9 | -999 |
- |
hyperthermophilic |
288347 |
1.2.1.9 | -999 |
- |
phosphate binds to the enzyme, resulting in the formation of a GAPN-phosphate binary complex characterized by a strongly decreased thermal stability, with a difference of at least 15°C between the maximum temperature of the thermal transition peaks, phosphate binds to the substrate C-3 subsite. Glycerol-3-phosphate has similar effects in thermal stability |
656283 |
1.2.1.9 | 45 |
- |
10 min, inactivation above |
656781 |
1.2.1.9 | 45 |
- |
inactivation above |
288338 |
1.2.1.9 | 60 |
- |
6 min, 89% inactivation |
288341 |
1.2.1.9 | 70 |
- |
10 min, inactivation above |
657250 |
1.2.1.9 | 75 |
- |
10 min, complete inactivation |
656781 |
1.2.1.9 | 95 |
- |
10 min, complete inactivation |
657250 |