Table 2.
Parameters describing thermodynamic and kinetic stabilities of human PGK1 WT and p.T378P enzymes. Data from [13,46].
| Chemical Denaturation | WT | p.T378P |
|---|---|---|
| Cm (M) | 2.43 ± 0.01 | 2.28 ± 0.06 |
| meq (kcal·mol−1·M−1) | 3.4 ± 0.2 | 1.5 ± 0.2 |
| ΔGU (kcal·mol−1) | 8.3 ± 0.5 | 3.5 ± 0.4 |
| Thermal denaturation | ||
| Tm (°C) | 52.8 ± 0.2 | 49.8 ± 0.4 |
| Ea (kcal·mol−1) | 191 ± 19 | 135 ± 12 |
| ΔH (kcal·mol−1) | 157 ± 18 | 127 ± 9 |
| Kinetic stability | ||
| Aggregation rate constant (kagg)(min−1) | 9 ± 5·10−7 | 1.6 ± 0.4·10−4 |
| Global unfolding rate constant (kunf(0M)) (min−1) | 0.09 ± 0.02 | 0.18 ± 0.04 |
| Proteolysis rate constant at high protease (k0) (min−1) | 0.11 ± 0.02 | 0.38 ± 0.01 |
| Proteolysis rate constant at low protease (k1) (min−1) | 0.27 ± 0.04 | 7.8 ± 0.5 |