| Value |
3.3
%
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Tomashek JJ, Glagoleva OB, Brusilow WS. The Escherichia coli F1F0 ATP synthase displays biphasic synthesis kinetics. J Biol Chem. 2004 Feb 6 279(6):4465-70 DOI: 10.1074/jbc.M310826200 p.4469 left columnPubMed ID14602713
|
| Primary Source |
[18] Etzold C, Deckers-Hebestreit G, Altendorf K. Turnover number of Escherichia coli F0F1 ATP synthase for ATP synthesis in membrane vesicles. Eur J Biochem. 1997 Jan 15 243(1-2):336-43.PubMed ID9030757
|
| Method |
Luciferase assay. Primary source abstract: " In parallel, the amount of F0F1 complexes present in membrane vesicles was determined by immunoquantitation to be 3.3 +/- 0.3% of the membrane protein for cells grown in rich medium and 6.6 +/- 0.3% for cells grown in minimal medium with glycerol as sole carbon and energy source." |
| Comments |
P.4467 right column bottom paragraph: "Previously, Etzold et al. (primary source) used the luciferase assay to measure the turnover number of the ATP synthase during synthesis by membrane vesicles of E. coli. They measured ATP synthesis rates of ∼0.060-0.10 μmol/min/mg of membrane protein at room temperature and 0.20 μmol/min/mg of membrane protein at 37 °C. They found that F1F0 makes up 3.3% of the E. coli membrane proteins, giving a turnover number of 13-33 s^-1, considerably lower than those of other F-type ATPase complexes measured under optimal conditions." |
| Entered by |
Uri M |
| ID |
115176 |