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Kinetic analysis of YtkD triphosphatasea
| Substrate | Vmax (U/mg) | kcat (s−1) | Km (mM) | kcat/Km (s−1M−1) |
|---|---|---|---|---|
| dATP | 4.7 | 1.5 | 0.89 ± 0.27 | 1.6 × 103 |
| 8-oxo-dGTP | 3.1 | 0.96 | 0.43 ± 0.17 | 2.4 × 103 |
| dGTP | 2.4 | 0.74 | 0.16 ± 0.015 | 4.6 × 103 |
Vmax and Km were obtained from a nonlinear regression analysis. One unit of enzyme catalyzes the hydrolysis of 1 μmol of substrate/min.
