Table 1.
Enzymatic activity assay (Michaelis-Menten analysis).
| kcat (s−1) | Km (µM) | kcat/Km (µM−1s−1) | N | |
|---|---|---|---|---|
| TCPTP | ||||
| TCPTPCAT | 34.0 ± 0.9 | 24.8 ± 2.0 | 1.4 ± 0.1 | 9 |
| TCPTPC-term | 23.7 ± 0.5 | 17.9 ± 1.1 | 1.3 ± 0.1 | 12 |
| TCPTPL1 | 19.3 ± 0.8 | 21.0 ± 2.7 | 0.9 ± 0.1 | 12 |
| TCPTP | 12.2 ± 0.2 | 12.4 ± 0.6 | 1.0 ± 0.1 | 9 |
| ITGA1 (saturated) | ||||
| TCPTPCAT + ITGA1_TR | 31.1 ± 0.7 | 23.0 ± 1.6 | 1.3 ± 0.1 | 9 |
| TCPTP + ITGA1_FCT | 26.6 ± 0.8 | 20.2 ± 1.9 | 1.3 ± 0.1 | 9 |
| TCPTP + ITGA1_TR | 26.2 ± 0.6 | 15.9 ± 1.3 | 1.6 ± 0.1 | 9 |
pEGFR peptide-1, derived from the cytoplasmic tail of EGFR, was used as a substrate. Calculated kinetic parameters are presented as the mean of nine or twelve independent reactions (n = 9 or n = 12; mean ± standard error, SE; explicit n number for individual analysis is shown in the column under the header ‘N’). Source data are provided as a Source Data file.