Myosin adenosine triphosphatase activity

Sreter, F. A., Seidel, J. C., and Gergely, J., Studies on myosin from red and white skeletal muscles of the rabbit. I. Adenosine triphosphatase activity. J. Biol. Chem. 241, 5772-5776 (1966). 

Caldesmon is a cytoplasmic protein with two isoform classes, one of which is found predominantly in smooth muscle cells and other cell types with partial myogenic differentiation. High-molecular-weight isoforms with molecular weights between 89 and 93 kD are capable of binding to actin, tropomyosin, calmodulin, myosin, and phospholipids, and they function to counteract actin-tropomyosin-activated myosin adenosine triphosphatase (ATPase). As such, they are mediators for the inhibition of calcium-dependent smooth muscle contraction." ... 

Onishi H, Suzuki H, Nakamura K, Takahashi K, Watanabe S (1978) Adenosine triphosphatase activity and thick filament formation of chicken gizzard myosin in low salt media. J Biochem (Tokyo) 83 835-847... 

Calcium stimulates myosin-adenosine triphosphatase (ATPase) activity. 

Preparation of an immobilized form of myosin and characterization of the adenosine triphosphatase activity generated... 

Flock and Bollman (62,53), using myosin adenosine triphosphatase (ATPase) as a tool for differentiating between the two labile groups of ATP, have found, in experiments lasting one hour, a higher P concentration in the terminal phosphate group than in the second phosphate group (Table II). After the lapse of one day, the specific activity of the two... 

Contraction of muscle follows an increase of Ca " in the muscle cell as a result of nerve stimulation. This initiates processes which cause the proteins myosin and actin to be drawn together making the cell shorter and thicker. The return of the Ca " to its storage site, the sarcoplasmic reticulum, by an active pump mechanism allows the contracted muscle to relax (27). Calcium ion, also a factor in the release of acetylcholine on stimulation of nerve cells, influences the permeabiUty of cell membranes activates enzymes, such as adenosine triphosphatase (ATPase), Hpase, and some proteolytic enzymes and facihtates intestinal absorption of vitamin B 2 [68-19-9] (28). 

The magnitudes of entropies of activation have provided valuable information regarding the details of the interactions between enzymes and substrates. The process of muscular contraction involves an interaction between the muscle enzyme myosin and adenosine triphosphate (ATP). Myosin is an enzyme which catalyzes the hydrolysis of ATP, a process which we have seen (p. 246) to be more exergonic than is the case for many other phosphates, and this hydrolysis contributes energy for contraction. Because of its catalytic action, myosin is also referred to as adenosine triphosphatase (ATP-ase). When the activated complex is formed from ATP ase and its substrate ATP, the entropy of activation is about 41 cal K" mol under approximately normal physiological conditions. We saw on p. 400, on the basis of a very simple electrostatic theory of AS values for ionic reactions in aqueous solution, that there will be a positive contribution of about 10 cal mol for each unit of the product [ [ % ( The long myosin molecules bear a series of positive... 

This enzyme activity has been observed in myosin and actomyosin, mitochondria, microsomes, and cell membranes. In some cases magnesium ions function as an activator, in others calcium ions, and in still others, both calcium and magnesium are requited. Another form of adenosine-triphosphatase is stimulated by sodium and potassium ions and is inhibited by ouabain. Some forms of the enzyme can hydrolyse inosine triphosphate and other nucleoside-5 -triphosphates. The substrate specificity may depend upon the activating divalent cation and on the presence of monovalent cations. These enzymes are probably important components of a system responsible for facilitating cation transfer in membranes. They should not be confused with adenosine triphosphate pyrophosphatase E.C. 3.6.1.8. 

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