Inhibition of E coli ATPase activity by a troponin component, TN-I, and by mitochondrial ATPase inhibitor.
The enzymic activity of Mg2+- or Ca2+-stimulated ATPase from Escherichia coli was inhibited by one of the troponin components, TN-I, and by mitochondrial ATPase inhibitor (F1-inhibitor). The inhibitory ability of component TN-I against Mg2+-stimulated AtPase activity was lost after digestion of component TN-I with trypsin. The Mg2+-stimulated ATPase activity inhibited by component TN-I was completely restored by the addition of another troponin component TN-C.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008929:Mitochondria, Heart / Q000502:physiology*; D009124:Muscle Proteins / Q000494:pharmacology*; D010086:Oxidative Phosphorylation Coupling Factors / Q000494:pharmacology*; D014336:Troponin / Q000494:pharmacology*
D009124:Muscle Proteins; D010086:Oxidative Phosphorylation Coupling Factors; D014336:Troponin; D000251:Adenosine Triphosphatases; D000252:Calcium-Transporting ATPases; D008274:Magnesium