Table 1.
Kinetic rate constants for PPACK binding to thrombin wild-type and mutants.
| k12 (s−1) | k21 (s−1) | koff (s−1) | kon (μM−1s−1) | τ (ms) | E*:E | |
|---|---|---|---|---|---|---|
| wt | 56 ± 3 | 8.8 ± 0.3 | 0 ± 0 | 1.5 ± 0.1 | 15 ± 1 | 1:6 |
| S195A | 16 ± 1 | 3.8 ± 0.8 | 4.6 ± 0.2 | 2.1 ± 0.1 | 51 ± 3 | 1:4 |
| W215A | 51 ± 3 | 110 ± 10 | 0 ± 0 | 1.2 ± 0.1 | 6.2 ± 0.3 | 2:1 |
| E217A | — | — | 0 ± 0 | 0.070 ± 0.002 | — | — |
| E192A | 11 ± 1 | 19 ± 1 | 0 ± 0 | 1.0 ± 0.1 | 33 ± 2 | 2:1 |
| W215A/E217A | — | — | 0 ± 0 | 0.00019 ± 0.00001 | — | — |
Experimental conditions are: 400 mM ChCl, 50 mM Tris, 0.1% PEG8000, pH 8.0, at 15 °C.