Table 2.
DNA-dependent ATPase activity of UvrD1–647. The ATPase activity of UvrD and UvrD1–647 were measured at a range of poly(dT) concentrations from 0 to 16 μM nucleotides. The data were plotted and used to calculate an apparent kcat for ATP hydrolysis and a KDNA (concentration of poly(dT) required for half-maximal ATPase rate) for the interaction of the proteins with DNA. The values shown are the averages of 3 independent experiments, with standard error.
| Helicase | kcat (s−1) | KDNA (μM nucleotides) |
|---|---|---|
| UvrD | 389.8 ± 6.3 | 0.54 ± 0.03 |
| UvrD1–647 | 497.5 ± 7.9 | 2.5 ± 0.1 |