TABLE 1.
Pre-steady state RT kinetic parameters of WT and mutant HIV-1 RT enzymes determined by RQF method
| Enzyme | Kd.DNA | kpol | Kd.dATP | kpol/Kd.dATP | Ratioa (mutant/WT) |
|---|---|---|---|---|---|
| nm | s−1 | μm | μm−1 s−1 | ||
| WT | 16.3 ± 3.1 | 17.6 ± 1.2 | 6.5 ± 1.6 | 2.7 ± 0.8 | 1 |
| p66M184I/p51WT | 16.8 ± 3.3 | 17.7 ± 1.0 | 16.7 ± 3.1 | 1.1 ± 0.4 | 0.40 |
| p66E138K/p51E138K | 11.9 ± 3.3 | 28.1 ± 2.0 | 7.9 ± 1.8 | 2.9 ± 0.8 | 1.07 |
| p66E138K/M184I/p51E138K | 18.6 ± 2.6 | 19.8 ± 1.4 | 7.9 ± 1.6 | 3.2 ± 1.1 | 1.18 |
| p66M184I/p51E138K | 11.5 ± 3.1 | 17.3 ± 1.0 | 5.6 ± 1.1 | 3.1 ± 1.1 | 1.15 |
a The ratio represents -fold change in incorporation efficiencies (kpol/Kd.dNTP) by mutant enzyme compared with WT.