ATPase properties of KIF17M-490
| Constructs | ATPase activity | Gliding | |||
| kcat | K0.5, MT | Velocity | Motile MT | No. of MT observed | |
| s−1 | µM | µm/s | % | ||
| KIF17 M-490 | 13.6 ± 1.8 | 1.3 ± 0.1 | 0.47 ± 0.02 | 11.6 ± 0.9 | 247 |
| KIF17 M-490 + KIF17-tail | 3.9 ± 0.7 | 0.4 ± 0.3 | ND | ND | 252 |
| KIF17 M-490 + EB1 | 16.6 ± 1.2 | 0.7 ± 0.3 | 0.51 ± 0.03 | 16.6 ± 1.3 | 251 |
| Constructs | ATPase activity | Gliding | |||
| kcat | K0.5, MT | Velocity | Motile MT | No. of MT observed | |
| s−1 | µM | µm/s | % | ||
| KIF17 M-490 | 13.6 ± 1.8 | 1.3 ± 0.1 | 0.47 ± 0.02 | 11.6 ± 0.9 | 247 |
| KIF17 M-490 + KIF17-tail | 3.9 ± 0.7 | 0.4 ± 0.3 | ND | ND | 252 |
| KIF17 M-490 + EB1 | 16.6 ± 1.2 | 0.7 ± 0.3 | 0.51 ± 0.03 | 16.6 ± 1.3 | 251 |
ATPase activity of KIF17M-490 in the absence and presence of KIF17-tail or EB1. Data (Fig. S1 A) were fit to a Michaelis–Menton equation to determine kcat and K0.5, MT. Data represent the mean of nine independent experiments at three different MT concentrations ± SEM. kcat refers to the rate of ATP hydrolysis per kinesin dimer. K0.5, MT refers to the concentration of polymerized tubulin to half-maximally stimulate ATPase activity. Errors are ± SEM.