Section 42
Chapter 41,431

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

Milgrom YaM; Murataliev, M.B.

Febs Letters 212(1): 63-67


ISSN/ISBN: 0014-5793
PMID: 2879744
DOI: 10.1016/0014-5793(87)81557-0
Accession: 041430963

Download citation:  

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 of Km = 10(-8) M and Vm = 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 less than or equal to 0.7.

PDF emailed within 0-6 h: $19.90