Table 1.
Summary of kinetic parameters (±2 SD) for ProT activation by VWbp(1-263) from the hysteretic mechanism shown in Scheme 1, where KI is the dissociation constant for competitive product inhibition
| Parameters | d-Phe-Pip-Arg-pNA | Tosyl-Gly-Pro-Arg-pNA |
|---|---|---|
| Km (thrombin) | 2.5 ± 0.2 μM | 11.3 ± 0.3 μM |
| kcat (thrombin) | 77 ± 1 s−1 | 164 ± 1 s−1 |
| KD | 2.4 ± 0.1 μM | 2.2 ± 0.2 μM |
| Kcon (kC2/kC1) | 9 ± 1 | 9 ± 6 |
| kC1 | 0.0052 ± 0.0001 s−1 | 0.0053 ± 0.0004 s−1 |
| kC2 | 0.049 ± 0.005 s−1 | 0.047 ± 0.028 s−1 |
| Km | 0.6 ± 0.2 μM | 6 ± 4 μM |
| kcat | 95 ± 1 s−1 | 50 ± 1 s−1 |
| KI | 2.2 ± 0.3 μM | 30 ± 20 μM |