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The substructure of myosin and the reaction mechanism of its adenosine triphosphatase

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Summary

This review summarizes recent studies on the structure and function of myosin, and attempts to survey them critically. Merits and demerits of our original reaction mechanism of myosin-ATPase and its simplified variant proposed byTaylor et al. are described.

Recent studies on the substructure of the myosin molecule and the reaction mechanism of the myosin-ATP system strongly suggest that the myosin molecule has two nonidentical heads. Various lines of evidence are also presented for the mechanism that ATP is hydrolyzedvia two different routes: one is the simple hydrolysis through the myosin-ATP complex, and the other is the one through the reactive myosin-phosphate-ADP complex. Our recent studies clearly demonstrate that F-actin accelerates markedly de-composition of the reactive myosin-phosphate-ADP complex. The molecular mechanism of this acceleration is analyzed by use of transient enzyme kinetic methods.

Finally, the reaction mechanism of the myosinactin-ATP system is discussed in relation with the molecular mechanisms of the three fundamental steps in muscle contraction, i.e., the binding of the projections from myosin filaments with actin filaments, sliding of actin filaments past myosin filaments with movement of the projections, and detachment of the projections from actin filaments.

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  1. Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka, Japan

    Yuji Tonomura & Akio Inoue

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  1. Yuji Tonomura
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  2. Akio Inoue
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Tonomura, Y., Inoue, A. The substructure of myosin and the reaction mechanism of its adenosine triphosphatase. Mol Cell Biochem 5, 127–143 (1974). https://doi.org/10.1007/BF01731376

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