EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    1.4.1.9 | -999 |
- |
- |
349660 |
| 1.4.1.9 | -999 |
- |
binding of NAD+ ioncreases thermostability. The interaction between NAD+ and Ser147 transduces a series of conformational changes that increases intermolecular interactions in the oligomer interface |
763749 |
| 1.4.1.9 | -999 |
- |
non-conserved residues Ala94 Tyr127, and the C-terminal region, are crucial for oligomeric thermostability |
763402 |
| 1.4.1.9 | -999 |
- |
residue Ala94 undergoes a hydrophobic interaction with Ala349 in a neighboring protomer. The side chain of Tyr127 undergoes hydrophobic interaction with Ile136 in the same subunit, and an electrostatic interaction with Arg364 in a neighboring protomer. Hydrophobic packing between protomers via domain I contributes to the high thermostability |
763749 |
| 1.4.1.9 | 25 |
- |
purified enzyme, fully stable at pH 5.0-11.0 |
725737 |
| 1.4.1.9 | 30 |
- |
10 mM potassium phosphate buffer, pH 7.4, 0.01% 2-mercaptoethanol, 1 mM EDTA, 1.0 M NaCl, stable for more than 6 months |
349682 |
| 1.4.1.9 | 30 |
- |
120 min, 85% residual activity |
763413 |
| 1.4.1.9 | 30 |
- |
2 months, 50% loss of activity in presence of 2.5 M NaCl |
656565 |
| 1.4.1.9 | 30 |
- |
half-life 72 h |
762918 |
| 1.4.1.9 | 35 |
- |
half-life 48 h |
762918 |
