EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
---|
2.4.2.28 | -999 |
- |
disulfide linkages play a key role in thermal stability |
637555 |
2.4.2.28 | -999 |
- |
high degree of thermal stability |
637529 |
2.4.2.28 | -999 |
- |
PfMTAP is a highly thermostable protein |
721717 |
2.4.2.28 | -999 |
- |
resistance to thermal inactivation is increased remarkably by addition of 5'-methylthioadenosine or phosphate |
637542 |
2.4.2.28 | -999 |
- |
the hexameric hyperthermophilic protein contains in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. All cysteine pairs and especially the CXC motif significantly contribute to the enzyme thermal stability |
731366 |
2.4.2.28 | -999 |
- |
the recombinant 5'-methylthioadenosine phosphorylase is less thermophilic and thermostable than the Sulfolobus solfataricus enzyme, since an incorrect positioning of disulfide bonds within the molecule generates structures less stable to thermal unfolding |
637549 |
2.4.2.28 | -999 |
- |
the recombinant enzyme, expressed in Escherichia coli, is less thermostable and thermophilic than the native enzyme due to incorrect positioning of disulfide bonds |
637549 |
2.4.2.28 | 4 |
- |
4h, 40% loss of activity |
723794 |
2.4.2.28 | 37 |
- |
4h, 90% loss of activity |
723794 |
2.4.2.28 | 40 |
55 |
15 min, stable |
637542 |