Table 1.
Summary of kinetic parameters
kbasal, ATPase activity in the absence of actin; vmax, maximum actin-activated ATPase activity; Kapp, concentration of actin at one-half vmax. vmax and Kapp were estimated from hyperbolic fits. vmax (60 μm), actin-activated ATPase rate at 60 μm F-actin; kcat/Kapp, catalytic efficiency; k−ADfast and k−ADslow, rate constants of the ADP release from acto-myosin; k−Pi, rate constant of Pi release at 20 μm F-actin concentration.
Parameter | S1f | S1f cgmRLC | S1f MLC2v | S1s | S1s cgmRLC | S1s MLC2B |
---|---|---|---|---|---|---|
kbasal (s−1) | 0.04 ± 0.01 | 0.06 ± 0.01 | 0.04 ± 0.01 | 0.05 ± 0.01 | 0.55 ± 0.01 | 0.04 ± 0.01 |
vmax (fit) (s−1) | 3.5 ± 1 | 2.5 ± 0.1 | 1.0 ± 0.3 | 0.5 ± 0.2 | 0.6 ± 0.1 | 0.1 ± 0.1 |
vmax (60 μm) (s−1) | 0.66 ± 0.01 | 0.52 ± 0.2 | 0.30 ± 0.02 | 0.14 ± 0.01 | 0.62 ± 0.01 | 0.09 ± 0.01 |
Kapp (fit) (μm) | 278 ± 96 | 244 ± 10 | 142 ± 54 | 208 ± 91 | 22 ± 3 | 39 ± 4 |
kcat/Kapp (10−3 μm−1 s−1) | 10 | 11 | 4 | 2 | 4 | 2 |
k−ADfast (s−1) | > 500 | > 500 | > 500 | 54 ± 3 | 61 ± 1 | 60 ± 3 |
k−ADslow (s−1) | 4 ± 1 | 5 ± 1 | 3 ± 1 | |||
k−Pi (20 μm) (s−1) | 0.18 ± 0.01 | 0.29 ± 0.01 | 0.07 ± 0.01 | 0.05 ± 0.01 | 0.17 ± 0.01 | 0.03 ± 0.01 |