Partial characterization of a soluble ATPase from pea cotyledon mitochondria.
A partially purified soluble ATPase (ATP phosphohydrolase, EC 3.6.1.3) from pea cotyledon mitochondria was characterized. Inhibition patterns with azide, NaF, and cold, and a stimulation by 2,4-dinitrophenol were typical of F1-ATPases from mammalian mitochondria. The enzyme hydrolysed GTP, ITP, and ATP, but not CTP, UTP, ADP, or IDP. ATPase and ITPase activities were strongly inhibited by ADP and to a lesser extent by IDP. Distinctive properties of the pea mitochondrial enzyme were activation by high concentrations of CaCl2 and stimulation by NaCl.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D001386:Azides / Q000494:pharmacology; D002413:Cations, Divalent; D003080:Cold Temperature; D004355:Drug Stability; D004789:Enzyme Activation; D007292:Inosine Nucleotides / Q000494:pharmacology; D008928:Mitochondria / Q000201:enzymology*; D010944:Plants / Q000201:enzymology*; D012265:Ribonucleotides; D013329:Structure-Activity Relationship
D001386:Azides; D002413:Cations, Divalent; D007292:Inosine Nucleotides; D012265:Ribonucleotides; D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases