Steady‐state rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic site

FEBS Letters

Milgrom, Ya.M.¹  Murataliev, M.B.¹ 

[1] A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, 119899 Moscow, USSR

关键词: F1-ATPase;    Single-site catalysis;    Active site;    Equilibrium constant;   

DOI  :  10.1016/0014-5793(87)81557-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Under the conditions of ATP regeneration and molar excess of nucleotide-depleted F₁-ATPase the enzyme catalyses steady-state ATP hydrolysis by the single catalytic site. Values ofK_m = 10⁻⁸ M and V_m = 0.05 s⁻¹ for the single-site catalysis have been determined. ADP release limits single-site ATP hydrolysis under steady-state conditions. The equilibrium constant for ATP hydrolysis at the F₁-ATPase catalytic site is ⩽ 0.7.

【 授权许可】

Unknown