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. Author manuscript; available in PMC: 2015 Jun 15.
Published in final edited form as: Arch Biochem Biophys. 2013 Dec 25;0:74–82. doi: 10.1016/j.abb.2013.12.012

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.