TABLE 2.
Pre-steady state RT kinetic parameters of WT and mutant HIV-1 RT enzymes determined by SF method
| Enzyme | kpol | K]d.dATP | kpol/Kd.dATP | Ratioa (mutant/WT) |
|---|---|---|---|---|
| s−1 | μm | μm−1 s−1 | ||
| WT | 12.5 ± 0.8 | 3.4 ± 0.8 | 3.7 ± 0.8 | 1 |
| p66M184I/p51WT | 12.7 ± 0.8 | 7.9 ± 1.2 | 1.6 ± 1.0 | 0.4 |
| p66E138K/p51E138K | 10.5 ± 0.7 | 4.0 ± 1.1 | 2.7 ± 0.9 | 0.73 |
| p66E138K/M184I/p51E138K | 12.6 ± 0.6 | 3.0 ± 0.3 | 4.2 ± 0.4 | 1.13 |
| p66M184I/p51E138K | 13.8 ± 0.8 | 3.4 ± 1.3 | 4.1 ± 1.6 | 1.10 |
a The ratio represents -fold change in incorporation efficiencies (kpol/Kd.dNTP) by mutant enzyme compared with WT.