Table 1. Kinetic and affinity data of monomeric Kinesin-1,–3, and −5 compared to MKLP2-MD.
A summary of steady state ATPase activities and MT affinities of monomeric Kin1 (Atherton et al., 2014; Woehlke et al., 1997; Hackney, 1988; Gilbert et al., 1995; Ma and Taylor, 1995; Rosenfeld et al., 1996; Nitta et al., 2004; Gigant et al., 2013), whose structures were used to compared with MKLP2, as well as Kin3 (Nitta et al., 2004). Kin5’s MT-stimulated ATPase activity has similar values as MKLP2 (Cochran et al., 2004; Cochran et al., 2006).
| Monomeric motor | MT-stimulated ATPase | MT affinity; Kd (μM) | ||||
|---|---|---|---|---|---|---|
| K0.5, MT (μM) | kcat (S−1) | ADP | NN | ADP.AlFx | AMPPNP | |
| MKLP2-MD | 1.07 ± 0.18 | 4.38 ± 0.20 | 0.363 ± 0.057 | 0.043 ± 0.002 | 0.355 ± 0.073 | 0.043 ± 0.035 |
| Kin1 (Kif5a/b) | 12.7 ± 4.0 (Atherton et al., 2014) 26.0 ± 5.8 (Rosenfeld et al., 1996) |
34.2 ± 5.7 (Atherton et al., 2014) 43.6 ± 7.8 (Rosenfeld et al., 1996) 50.3 ± 1.6 (26) |
20.8 ± 2.4 (Rosenfeld et al., 1996) 2.0 ± 0.3 (Gigant et al., 2013) |
n.a. | 1.4 ± 0.2 (Rosenfeld et al., 1996) 0.3 ± 0.006 (Gigant et al., 2013) |
1.1 ± 0.1 (Rosenfeld et al., 1996) 0.045 ± 0.012 (Gigant et al., 2013) |
| Kin3 (Kif1a) | 0.0537 ± 0.0057 (Atherton et al., 2014) | 43.4 ± 1.0 (Atherton et al., 2014) | 0.0068 ± 0.0025 (Nitta et al., 2004) | n.a. | 0.0059 ± 0.0015 (Nitta et al., 2004) | 0.0042 ± 0.0013 (Nitta et al., 2004) |
| Kin5 (Eg5) |
4.5 (Cochran et al., 2004) 0.29 ± 0.02 (Cochran et al., 2006) |
2.9 (Cochran et al., 2004) 5.5 ± 0.1 (Cochran et al., 2006) |
n.a. | n.a. | n.a. | n.a. |
n.a.: not available.