N-terminal region of gizzard myosin heavy chain is critical for the ATPase activity.
Two different HMM species of gizzard myosin were prepared under conditions such that the phosphorylation of light chain was fully maintained. They were different in the N-terminal structure of the heavy chain but not in the light chain composition. A significant decrease in the Mg2+-ATPase activity was observed in one class of HMM which was proteolytically cleaved intramolecularly at site 1, 5 K daltons from the masked N terminus. Another class of HMM without the cleavage at site 1 showed ATPase activity similar to that of myosin. The decrease in ATPase activity was not caused by denaturation since similar amounts of initial burst of Pi liberation were observed with both HMMs and myosin. Kinetic and substructure analyses of HMM revealed that the activity change depended solely on the cleavage at site 1. The N-terminal region of gizzard myosin heavy chain may thus have an important role in maintaining the active site structure.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D005895:Gizzard, Avian / Q000201:enzymology*; D015879:Myosin Subfragments / Q000032:analysis; D009218:Myosins / Q000032:analysis*; D009994:Osmolar Concentration; D010766:Phosphorylation; D013329:Structure-Activity Relationship
D000596:Amino Acids; D015879:Myosin Subfragments; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins