EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   1.4.1.3 | -999 |
- |
at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml. Only the oligomeric form is temperature resistant |
718955 |
| 1.4.1.3 | -999 |
- |
hGDH1: much slower heat inactivation processes in presence of 1 mM ADP or 3 mM L-Leu |
655582 |
| 1.4.1.3 | -999 |
- |
much slower heat inactivation processes in presence of 1 mM ADP or 3 mM L-Leu |
655582 |
| 1.4.1.3 | -999 |
- |
Q441R or S445L mutation makes the enzyme more resistant to thermal inactivation compared to wild-type, K450E or H454Y mutation makes the enzyme extremely heat-labile compared to wild-type |
699658 |
| 1.4.1.3 | -999 |
- |
the occurrence of specific substitutions and a possible role for N-epsilon-methylation of lysine residues are discussed in view of current hypotheses on the molecular basis of thermal adaptation of proteins |
719390 |
| 1.4.1.3 | 0 |
- |
complete loss of activity after 5 h, 20% glycerol protects from inactivation |
391615 |
| 1.4.1.3 | 5 |
- |
moderately stable above |
391615 |
| 1.4.1.3 | 25 |
- |
48 h, protein concentration of 0.2 mg/ml, stable |
679617 |
| 1.4.1.3 | 25 |
70 |
the thermostability of the enzyme at neutral pH is very high even at 70°C, but at acidic pH values, the dissociation of enzyme subunits produces the rapid enzyme inactivation even at 25°C, immobilized preparations, as well as the soluble enzyme, remain fully active after 24 h of incubation at 60°C and pH 7, the optimal glyoxyl agarose derivative obtained is fully stable at pH 4 and 25°C, retaining more than 90% of its activity after incubation at 45°C for 24 h at pH 4 and more than 75% of the activity after the same period at 50°C |
684650 |
| 1.4.1.3 | 37 |
- |
complete loss of activity |
391602 |
