Table 2.

EMD 57033-mediated changes in the kinetic behavior of β-cardiac myosin

DOI: http://dx.doi.org/10.7554/eLife.01603.010

	Control	25 µM EMD 57033	∼Change (−fold)
KM(Actin)	36. 8 ± 2.67 µM	3. 6 ± 0.8 µM	10
kcat	0. 12 ± 0.02 s−1	0.19 ± 0.02 s−1	1.6
kcat/KM(Actin)*	0.00326 µM−1 s−1	0.0528 µMv1 s−1	16
kcat/KM(Actin)†	0.00193 µM−1 s−1	0.0304 µM−1 s−1	15.8
K1k+2	0.19 ± 0.02 µM−1s−1	0.65 ± 0.04 µM−1s−1	3.4
k+2	46 ± 3 s−1	174 ± 7 s−1	3.8
k+3 + k−3	1.9 ± 0.2 s−1	24.5 ± 1.9 s−1	12.9
k+4‡	0.09 ± 0.01 s−1	0.15 ± 0.01 s−1	1.7
k−D	0.15 ± 0.03 s−1	0.16 ± 0.04 s−1	n.a.
k−AD	25.5 ± 3 s−1	26.9 ± 4 s−1	n.a.
Ea	47 ± 4 kJ mol−1	31 ± 3 kJ mol−1	1.5

^*The apparent second order rate constant for actin binding (k_cat/K_M(Actin)) was obtained from the calculated ratio of both values.

^†k_cat/K_M(Actin) was obtained from the initial slope of the steady-state ATPase activity vs the F-actin plot.

^‡Measured at F-Actin concentration of 25 µM and 25 µM ATP.