Table 3. Summary of kinetic values for cleavage of P1 aspartate and glutamate by caspases-3 and -7.
|
D/E ratio |
||||||||
|---|---|---|---|---|---|---|---|---|
| Caspase | Substrate | Vmax (uM/s) | KM (uM) | kcat (1/s) | kcat/KM (1/(Ms)) | KM (uM) | kcat (1/s) | kcat/KM (1/(Ms)) |
| 3 | D | 5.3 (0.16) | 57.9 (5.6) | 355.73 | 6.14E+06 | 3.55 | 8.15 | 2.29 |
| 3 | E | 0.65 (0.04) | 16.3 (3.8) | 43.65 | 2.68E+06 | |||
| 7 | D | 2.6 (0.05) | 49.4 (3.1) | 173.80 | 3.52E+06 | 0.37 | 0.79 | 2.14 |
| 7 | E | 3.3 (0.06) | 133.8 (6.3) | 219.93 | 1.64E+06 | |||
The values for Vmax and KM with standard errors are reported from triplicate measurements on three biological replicates. The ratio of kcat/KM for P1 aspartate/P1 glutamate is just over twofold for both caspases-3 and -7