TABLE 2.
Single turnover misincorporation opposite template A
Kinetic constants obtained from single turnover misincorporation experiments are listed for each enzyme (± S.E. of the fit).
| dNTP | Enzyme | kpol | Kd | kpolc/kpolia | Kdi/Kdca | Efficiencyb | Fold changec |
|---|---|---|---|---|---|---|---|
| s−1 | μm | μm−1 s−1 | |||||
| dTTP | WT | 46 ± 2 | 35 ± 5 | 1.3 | 55 | ||
| G231D | 13.1 ± 0.9 | 550 ± 70 | 2.4 × 10−2 | ||||
| dATP | WT | 0.025 ± 0.001 | 57 ± 10 | 1800 | 1.6 | 4.4 × 10−4 | 58 |
| G231D | 0.00250 ± 0.00007 | 330 ± 30 | 5200 | 0.60 | 7.6 × 10−6 | ||
| dCTP | WT | 0.079 ± 0.004 | 280 ± 40 | 580 | 8.0 | 2.8 × 10−4 | 110 |
| G231D | 0.0016 ± 0.0002 | 610 ± 110 | 8200 | 1.1 | 2.6 × 10−6 | ||
| dGTP | WT | 0.031 ± 0.002 | 84 ± 18 | 1500 | 2.4 | 3.7 × 10−4 | 93 |
| G231D | 0.00119 ± 0.00007 | 300 ± 50 | 11,000 | 0.55 | 4.0 × 10−6 |
a Subscript c denotes correct nucleotide; subscript i denotes incorrect nucleotide.
b Efficiency was calculated by dividing kpol by Kd for each condition.
c Fold change in efficiency (WT/G231D) is shown.