Temperature-dependent transitions of the myosin-product intermediate at 10 degrees during Mn(II)-ATP hydrolysis by myosin from rabbit psoas muscle.
The initial burst of Pi liberation during the hydrolysis of Mn(II)-ATP by heavy meromyosin from rabbit psoas muscle was investigated. Below 10 degrees, the initial burst of Pi liberation was inhibited by the pre-addition of ADP without any change in the steady-state activity, but it was not inhibited above 10 degrees. The burst size was about one mole per mole of heavy meromyosin. The initial burst of Pi liberation in Mg-ATP hydrolysis at 8 degrees, however, was not inhibited by the pre-addition of ADP. These results, obtained with psoas muscle heavy meromyosin, were almost the same as those obtained with heavy meromyosin from rabbit leg and back muscles (Hozumi and Tawada (1975) Biochim. Biophys. Acta 376, 1-12) and, therefore, indicate that in Mn-ATP above 10 degrees there is at the burst site a predominant myosin -product complex generated by ATP hydrolysis. Similarly, below 10 degrees there is a myosin-product complex identical with the one generated by adding ADP (and Pi) to myosin.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D011817:Rabbits; D013696:Temperature
D008345:Manganese; D000251:Adenosine Triphosphatases; D009218:Myosins; D008274:Magnesium