EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    1.1.1.85 | -999 |
- |
- |
639160 |
| 1.1.1.85 | -999 |
- |
all mutant Bs3-isopropylmalateDHs and the wild-type enzyme are irreversibly inactivated by heat treatments. A linear correlation between thermal stability and hydrophobicity exists for those 3-isopropylmalateDHs containing position 253 residues with hydrophobic side chains |
687442 |
| 1.1.1.85 | -999 |
- |
APS IPMDH denatures significantly at temperatures above 60°C and completely and irreversible loses activity at 70°C within 1 min, Teq: 67°C |
684587 |
| 1.1.1.85 | -999 |
- |
high concentrations of KCl considerably protect the enzyme from irreversible thermal denaturation |
639131 |
| 1.1.1.85 | -999 |
- |
mutant enzyme L204F shows higher thermostability compared to wild-type enzyme, denaturation rates at 68°C and 70°C are slower for the mutant enzyme than for wild-type enzyme |
639157 |
| 1.1.1.85 | -999 |
- |
The thermal denaturation processes of wild-type and mutant enzymes are irreversible under the conditions used. Mutant M256F shows two-phase denaturation curve. The hydrophobic interactions at the subunit interface are critically important for the thermostability of dimeric enzyme. |
657230 |
| 1.1.1.85 | -999 |
- |
thermostabilization by LiCl, NaCl, KCl and to a lesser degree with RbCl, NH4Cl and CsCl |
639143 |
| 1.1.1.85 | -999 |
- |
time-dependent denaturation-renaturation experiments on IPMDH are presented. Unfolding occurs in a single first-order step with half-times of 1 h. The binding of Mn*IPM (the manganese complex of 3-isopropylmalate) markedly reduces the rates of unfolding. Refolding is a two-step or multistep first-order process involving an inactive intermediate. The restoration of the native structure and reactivation take place with a half-time of a few min |
685090 |
| 1.1.1.85 | -999 |
- |
two ancestral sequences of 3-isopropylmalate dehydrogenase (ancIPMDH-IQ and ancIPMDH-ML) are designed by an ancestral sequence reconstruction technique based on a phylogenetic analysis of extant homologous amino acid sequences. Genes encoding the designed sequences were artificially synthesized and expressed in Escherichia coli. The reconstructed enzymes were found to be slightly more thermally stable than the extant thermophilic homologue from Thermus thermophilus |
763696 |
| 1.1.1.85 | 0 |
- |
pH 8.3, half-life: 5 min |
639147 |
