Table 1.
Binding, kinetics and energetics of HIV-1 protease variants in complex with DRV. For each variant, the inhibition constant, Ki, Michaelis-Menten constant, KM, turnover number, kcat and mean protein-DRV van der Waals energy (from MD simulations), ΔEvdW, is reported. The enzyme catalytic efficiency, kcat/KM, is also reported.
| NL4–3 | KY | KY(V89L) | KY(M90L) | KY(DM) | |
|---|---|---|---|---|---|
| KM (μM) | 71.4 ± 6.8 | 74.4 ± 13.4 | ND* | 70.5 ± 30.0 | 77.0 ± 17.0 |
| kcat (s−1) | 1282.7 ± 0.06 | 220.6 ± 0.2 | ND | 47.7 ± 0.1 | 77.0 ± 0.01 |
| kcat / KM (μM−1s−1) |
17.1 ± 0.1 | 3.0 ± 0.2 | ND | 0.7 ± 0.4 | 1.0 ± 0.2 |
| Ki (nM) | < 0.005 | 7.0 ± 0.1 | 24.1 ± 1.0 | 2.4 ± 0.1 | 2.4 ± 0.1 |
| ∆EvdW
(kcal/mol) |
-58.5 ± 0.4 | -53.0 ± 0.5 | -52.3 ± 0.6 | -53.6 ± 0.6 | -53.9 ± 0.6 |
*
ND = Could not be determined