Table 1.

Kinetic parameters comparison between Myo19-3IQ and Myo^W140V-3IQ.

Parameter	Value
	Myo19-3IQ5	Myo19-3IQW140V
Steady-state ATPase parameters
k cat (s−1 head−1)	3.1 ± 0.1	4.1 ± 0.4
K ATPase (µM)	11.6 ± 1.2	56.7 ± 10.9
v o (s−1)	0.06 ± 0.02	0.10 ± 0.05
ATP binding
1/K′1T (µM)	476 ± 116	758 ± 217
K′+2T (s−1)	1003 ± 26	381 ± 72
K′1T K′+2T (μM−1s−1)	2.17 ± 0.8	0.5 ± 0.2
K′−2T (s−1)	≈0	1.4 ± 0.3
k +α (s−1)	17.5 ± 0.3	29.3 ± 4.3
k-α (s−1)	2.6 ± 1.1	10.1 ± 6.0
K α 3	6.8 ± 1.6	2.9 ± 1.3
ADP binding
K′-1D (s−1)	9.3 ± 0.3	12.7 ± 1.5
1/KD,overall (µM)	0.13 ± 0.04	1.6 ± 0.3

Conditions: 20 mM MOPS, pH 7.3, 50 mM KCl, 2 mM MgCl₂, 0.2 mM EGTA, 1 mM DTT, 25 °C. ¹Calculated parameter from rates or/and equilibrium constants. ²Calculated parameters from y-intercept. ³The equilibrium constant for isomerization, K _α, is define as K _α = k _{+ α/} k _−α. ⁴Calculated parameters from k- _α = k _{+ α/} K _α. ⁵Reported in (Usaj & Henn, parallel submission).