Steady‐state kinetics of F1‐ATPase

FEBS Letters

Calcaterra, Nora B.¹  Roveri, Oscar A.¹ 

[1] Centra de Estudios Fotosintéticos y Bioquímicos (CONICET, Fund. M.Lillo and Universidad Nacional de Rosario), Suipacha 531, 2000 Rosario, Argentina

关键词: F1-ATPase;    Mitochondrial ATPase;    Anion activation;    Hysteretic enzyme;    Steady-state kinetics;    (Beef heart);   

DOI  :  10.1016/0014-5793(85)80056-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 K _m values for ATP. Conversely to what has been previously reported, bicarbonate did not linearize F₂-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.

【 授权许可】

Unknown