Table 1.
Summary of kinetic parameters measured from in vitro motility, actin-activated S1 ATPase, single molecule binding, and stopped-flow spectroscopy assays.
Kinetic parameters with and without sucrose
| ||
---|---|---|
Sucrose: | 0 mM | 880 mM |
V, μm·s−1 | 2.05 ± 0.3 (3) | 0.43 ± 0.2 (3) |
D actin, μm2·s−1 | 0.72 ± 0.02 | 0.54 ± 0.02 |
kcat*, min−1 | 75 ± 13 (2) | 15 ± 1 (2) |
Km *, μM | 33 ± 2 (2) | 9 ± 1 (2) |
ρ·katt(−ATP) †, s−1 | 0.72 ± 0.02 | 0.21 ± 0.02 |
ρ·katt(+ATP) †, s−1 | 0.97 ± 0.08 | 0.14 ± 0.01 |
katt(−ATP) ‡, μM−1·s−1 | 2.41 ± 0.08 | 0.48 ± 0.01 |
kdet(−ATP) ‡, s−1 | 0.13 ± 0.06 (2) | 0.11 ± 0.03 (2) |
kdet(−ATP) †, s−1 | 1.3 ± 0.2 | 1.0 ± 0.1 |
kT ‡, μM−1·s−1 | 2.1 ± 0.1 | 1.3 ± 0.1 |
KADP ‡, μM | 217 ± 30 | 244 ± 33 |
Ea(att) ‡, kJ·mol−1 | 50 ± 2 | 68 ± 5 |
Ea(det) ‡, kJ·mol−1 | 24 ± 3 | 28 ± 3 |
Steady-state ATPase assays performed at 700 mM sucrose.
SiMBA
Stopped-Flow
N values are in parenthesis.
Errors with (N) are ± SD. All other errors are SEM to a fit.