ATPase (cardiac specific myosin)
Myosin (EC 220.127.116.11) and p97 (also known as Cdc48 or valosin containing protein (VCP; EC 18.104.22.168)) are both ATPases involved in cellular and subcellular movement. Myosin is an ATPase that converts chemical energy into directed movement via its cyclic interactions with actin filaments in all eukaryotic cells and can be viewed as a molecular motor. Although this protein comes in many shapes and sizes, all known myosin superfamily members show widely conserved regions: the myosin head is commonly subdivided into the motor domain, which is the actin activated ATPase, and the lever arm, which is an extended helix containing a variable number of consensus calmodulin or calmodulin-like light chain binding sites; this is followed by a region of coiled coil in two-headed myosins and may contain sequences that act as elements for protein folding; last is the targeting domain, which binds the myosin to its cellular target. More than 35 classes of myosin have been discovered, 13 of which are represented in humans. CK 1827452 (Axon 1835), is an agent that directly activates myosin, for use in the treatment of heart failure.
ATPases listed: ATPase (cardiac specific myosin), ATPase (p97), ATPase (H+/K+), ATPase (Na+/K+)
 I. Rayment. The Structural Basis of the Myosin ATPase Activity. J. Biol. Chem. 1996, 271, 15850-15853.
 H.L. Sweeney, A. Houdusse. Structural and Functional Insights into the Myosin Motor Mechanism. Annu. Rev. Biophys. 2010, 39, 539-557.