EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.6.5.3 | -999 |
- |
after a 6 h treatment at 80°C and 87°C, the residual activity is 80% and 54%, respectively; at 95°C the [3H]GDP-binding activity became one half of the initial activity after about 30 min. After 80 days at 25°C, a crude aEF-la preparation retained 50% of the maximum nucleotide-binding capacity |
724898 |
| 3.6.5.3 | -999 |
- |
domain 1 and domains 2+3 of both EF-Tu positively cooperate to heat-stabilize the GTPase center to attain optimal activity at alpha-helical regions of the G-domain |
667812 |
| 3.6.5.3 | -999 |
- |
thermal stability of the enzyme-GDP complex is significantly reduced when the GDP is replaced with guanyl-5'-yl imido diphosphate or in the presence of NaBr or NH4Cl |
678126 |
| 3.6.5.3 | 20 |
100 |
EF-1alpha denaturation profile at pH 4.0, the protonation state of the numerous Asp and Glu residues plays a critical role for the thermally denatured state of the enzyme, reversibility of the inter-conversion between the two denatured forms, overview |
691101 |
| 3.6.5.3 | 40 |
- |
about, melting point, recombinant enzyme |
756195 |
| 3.6.5.3 | 87 |
- |
half-denaturation of mutant enzyme G13A |
657934 |
| 3.6.5.3 | 87 |
- |
the enzyme isoform EF-1alpha retains 54% activity after 6 h at 87°C |
740115 |
| 3.6.5.3 | 87 |
96 |
half-inactivation time 99 min at 87°C, half-inactivation time 3.5 min at 96°C |
696496 |
| 3.6.5.3 | 91 |
- |
10 min, 50% inactivation of GDP binding ability, mutant enzyme G13A |
657934 |
| 3.6.5.3 | 92 |
- |
half-denaturation of wild-type enzyme |
657934 |
