Table 2.
Kinetic parameters of SFVmac PR-RTs for polymerization and DNA binding
| Enzyme | 1 K M (μM) | 1 V max (mM/min) | V max /K M (1/min) | 2 K D P/T (nM) |
|---|---|---|---|---|
| WT | 57 (±7) | 2.1 (±0.08) | 36.8 (±4.7) | 9.6 (±0.7) |
| K211I | 160 (±28) | 0.3 (±0.02) | 1.9 (±0.4) | 19.6 (±2.3) |
| I224T | 94 (±9) | 2.2 (±0.08) | 23.4 (±2.4) | 8.9 (±1.4) |
| S345T | 34 (±6) | 1.1 (±0.05) | 32.4 (±5.9) | 8.7 (±0.9) |
| E350K | 32 (±8) | 1.8 (±0.10) | 56.3 (±14.4) | 9.7 (±1.7) |
| mt2a | 252 (±39) | 0.5 (±0.04) | 2.0 (±0.3) | 7.8 (±1.2) |
| mt2b | 159 (±41) | 0.6 (±0.02) | 3.8 (±1.0) | 15.8 (±2.5) |
| mt2c | 9 (±3) | 2.5 (±0.10) | 277.8 (±92.6) | 17.2 (±2.1) |
| mt3 | 67 (±14) | 2.0 (±0.10) | 29.9 (±6.2) | 15.8 (±2.1) |
| mt4 | 110 (±11) | 1.3 (±0.05) | 11.8 (±1.3) | 9.5 (±1.6) |
1KM- and vmax-values were obtained by using the Michaelis-Menten equation to fit a curve to the data. 2KD-values were obtained as described previously [14] by using an equation for a two state model to fit a curve to the titration data. Standard errors are given in parenthesis.