| Value |
270
ATP/s
Range: ±40 ATP/s
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Szenk M, Dill KA, de Graff AMR. Why Do Fast-Growing Bacteria Enter Overflow Metabolism? Testing the Membrane Real Estate Hypothesis. Cell Syst. 2017 Aug 235(2):95-104. doi: 10.1016/j.cels.2017.06.005. p.97 box 1 2nd paragraph, p.98 right column top paragraph & p.101 left column 3rd paragraphPubMed ID28755958
|
| Primary Source |
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
|
| Comments |
p.97 box 1 2nd paragraph: "The surface efficiency of the electron transport chain-dependent part can be estimated from experimental electron transport chain protein structures, abundances, and kinetics (Valgepea et al., 2013, and primary source). Normalizing abundances to the terminal ATP synthase, an estimated 84 nm^2 of electron transport chain is required to generate 270 ± 40 ATP/s, the maximum speed of ATP synthase (primary source), resulting in a surface efficiency of only 3 ± 1 ATP/s/nm^2 (Tables S1B and S1D). The electron transport chain stoichiometry shown in the table below represents averages across growth rates (Valgepea et al., 2013) (Table S1B)." |
| Entered by |
Uri M |
| ID |
114701 |