[Esterase activity of the mitochondria oligomycin-sensitive ATPase complex].
It was found that mitochondrial oligomycin-sensitive ATPase (OS-ATPase) possesses the esterase activity with respect to some carboxylic acid esters with phenols and arylalcane alcohols. The substrate specificity of the esterase found was studied. The effects of some inhibitors and activators of ATPase on the enzyme activity were demonstrated. It was found that ADP inhibits the enzyme from submitochondrial particles containing factor F1 and does not inhibit the enzyme from the particles devoid of this factor. The data obtained suggest that esterase is localized in the hydrophobic part of the oligomycin-sensitive ATPase complex and are indicative of the functional interrelationship between the esterase and ATPase activities.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002417:Cattle; D066298:In Vitro Techniques; D008929:Mitochondria, Heart / Q000201:enzymology*; D009840:Oligomycins / Q000494:pharmacology*; D010086:Oxidative Phosphorylation Coupling Factors; D013367:Submitochondrial Particles / Q000201:enzymology; D013379:Substrate Specificity
D009840:Oligomycins; D010086:Oxidative Phosphorylation Coupling Factors; D000255:Adenosine Triphosphate; D002265:Carboxylic Ester Hydrolases; D000251:Adenosine Triphosphatases
Esteraznaia aktivnost' kompleksa oligomitsinchuvstvitel'noĭ ATPazy mitokhondriĭ.