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. 2012 Jun 1;23(11):2057–2065. doi: 10.1091/mbc.E12-02-0120

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© 2012 Wang et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 2: — Actin-stimulated MgATPase activity and actin sliding velocity of control (PwMhc2) and IBM-3 mutant (E701K) myosin. (A) ATPase activity of control and mutant myosin was determined in the absence and in the presence of F-actin. For the determination of V_max and K_m (Table 3), basal Mg-ATPase activities obtained in the absence of actin were subtracted from all data points. The data were fitted with the Michaelis–Menten equation to determine V_max and K_m (actin). The ratio of V_max/K_m from all assays was used to determine catalytic efficiency. CaATPase, MgATPase, actin-stimulated MgATPase activity, and the V_max/K_m ratio were significantly reduced (p < 0.001), whereas K_m was significantly enhanced (p < 0.05) in mutant relative to control myosin (Table 3). (B) Actin sliding velocity stimulated by IBM-3 mutant (E701K) myosin was significantly reduced (p < 0.001) compared with that of control myosin. Our data suggest that the IBM-3 mutation depresses the enzymatic activity of the molecular motor.