Steady-state kinetics of F1-ATPase. Mechanism of anion activation.
The kinetic behaviour of the ATPase activity of beef heart F1 depends largely on the exposure of the enzyme to some anionic ligands such as sulphate and/or EDTA. F1 prepared in the presence of such anions exhibited a triphasic kinetic pattern whereas F1 from which those anions were removed by dialysis exhibited only two Km values for ATP. Conversely to what has been previously reported, bicarbonate did not linearize F1-ATPase kinetics. Moreover, anion activation cannot be simply explained by promotion of ADP release but mainly by an increase in affinity of the third catalytic site for ATP.
Roveri
O A
OA
Calcaterra
N B
NB
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D000838:Anions / Q000494:pharmacology*; D001639:Bicarbonates / Q000494:pharmacology; D002417:Cattle; D003956:Dialysis; D004492:Edetic Acid / Q000494:pharmacology; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013431:Sulfates / Q000494:pharmacology
D000838:Anions; D001639:Bicarbonates; D013431:Sulfates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D006180:Proton-Translocating ATPases