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. Author manuscript; available in PMC: 2017 Dec 22.
Published in final edited form as: Biochemistry. 2010 May 4;49(17):3695–3702. doi: 10.1021/bi902211w

Table 1.

Kinetic Parameters of the Phosphorylated and Unphosphorylated huM3MD ATPase Cycle

signal/method p-myosin IIIA up-myosin IIIAa
steady state
Vo (s−1) 0.07±0.02 0.05
Vmax (s−1) 1.6±0.2 0.54
Kactin (μM) 10.3±3.2 0.13
ATP binding
K1k+2 (μM−1 s−1) mant-ATP 0.20± 0.01 14
k−2 (s−1) 0.05±0.02 0.2
K1k+2 (μM−1 s−1) mant-ATP 0.13±0.01 0.16
k−2 (s−1) 0.65±0.2 7.4
ATP hydrolysis
k+3 + k−3 (s−1) quenched-flow 3.7 ±0.4 0.15
phosphate release
k+4obs (s−1) MDCC-PBP 0.36±0.01 0.14–0.16
k+4obs (s−1) 70± 24 1.14–1.26
ADP binding
k+5 (s−1) mant-ADP cold chase 8.6±0.6 6.5
k−5 (μM−1 s−1) mant-ADP binding 0.87±0.03 0.4
k+5 (s−1) mant-ADP cold chase 8.1±0.06 6.2
k−5 (μM−1 s−1) mant-ADP binding 0.56±0.03 0.58
actin binding
k−6 (μM−1 s−1) light scattering 0.54±0.03 29.8
k+6 (s−1) light scattering 0.13±0.02 2.3
K6 (nM) 240 68.8
k−8 (μM−1 s−1) light scattering 92.9
k+8 (s−1) light scattering 8.6
K8 (μM) 0.09
k−10 (μM−1 s−1) light scattering 0.14±0.02 23.8
k+10 (s−1) light scattering 0.15±0.02 2
K10 (nM) 1071 71.4
a

From ref 1.