Michaelis-Menten constants kcat and Km and the catalytic efficiencies (kcat/Km) of VWF115 and VWF115(1606A) proteolysis by wild-type ADAMTS13 and ADAMTS13 VR3B variants derived from kinetic analysis from the initial rates of substrate proteolysis
| . | Michaelis-Menten constants (WT ADAMTS13) . | Fold difference . | |
|---|---|---|---|
| VWF115 . | VWF115 (M1606A) . | ||
| Km, μM | 0.65 | 2.9 | 4.6 |
| kcat, s−1 | 0.52 | 0.16 | 3.3 |
| kcat/Km, ×105 M−1s−1) | 8.21 | 0.55 | 15 |
| . | Michaelis-Menten constants (WT ADAMTS13) . | Fold difference . | |
|---|---|---|---|
| VWF115 . | VWF115 (M1606A) . | ||
| Km, μM | 0.65 | 2.9 | 4.6 |
| kcat, s−1 | 0.52 | 0.16 | 3.3 |
| kcat/Km, ×105 M−1s−1) | 8.21 | 0.55 | 15 |