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Literature summary for 7.1.2.2 extracted from
- Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase (2009), J. Biol. Chem., 284, 17457-17464.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type FoF1 and subunit epsilon mutant EFoF1 in Escherichia coli strain RA1 | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of a EFoF1 mutant lacking the C-terminal domain of the epsilon subunit, the mutant shows severalfold lower turnover numbers and higher Michaelis constants compared to the wild-type enzyme in ATP synthesis driven by acid-base transition, overview. The dependence of the activities of FoF1 wild-type and FoF1 DELTAepsilon on various combinations of DELTApH and DELTAPsi is similar | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the epsilon subunit of FoF1-ATP synthase inhibits the FoF1 ATP hydrolysis activity. The inhibitory effect is modulated by the conformation of the C-terminal alpha-helices of epsilon, and the extended but not hairpin-folded state is responsible for inhibition | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, wild-type and mutant enzymes, overview | Escherichia coli | |
| 0.025 | - |
ADP | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli |  |
| 0.052 | - |
ATP | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 0.078 | - |
ATP | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 0.1 | - |
ADP | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 3.2 | - |
phosphate | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 4.2 | - |
phosphate | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Escherichia coli | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | Escherichia coli | - |
ADP + phosphate + H+/out | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type enzyme and subunit epsilon mutant EFoF1 from Escherichia coli strain RA1 | Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] | model of mechanochemical coupling, overview | Escherichia coli |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| reconstitution of purified recombinant mutant EFoF1 into liposomes using L-alpha-phosphatidylcholine from soybean suspended in 10 mM HEPES-NaOH, 5 mM MgSO4, and 1 mM KCl, pH 7.5 | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
measurement of ATP synthesis driven by acid-base transition and the K+-valinomycin diffusion potential, wild-type and mutant enzymes, overview | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | - |
Escherichia coli | ADP + phosphate + H+/out | - |
r | |
| ATP + H2O + H+/in | the epsilon subunit of FoF1-ATP synthase inhibits the FoF1 ATP hydrolysis activity. The rate-limiting step in ATP synthesis is unaltered by the C-terminal domain of epsilon | Escherichia coli | ADP + phosphate + H+/out | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the epsilon subunit has a molecular mass of 14 kDa and a two-domain structure consisting of an N-terminal 10-stranded beta-sandwich and two C-terminal alpha-helices | Escherichia coli |
| multimer | subunit composition of bacterial F1 and Fo is alpha3beta3gammadeltaepsilon and ab2c10-15, respectively, and the gammaepsilonc10-15 complex rotates against the alpha3beta3deltaab2 complex in FoF1. The epsilon subunit has a molecular mass of 14 kDa and a two-domain structure consisting of an N-terminal 10-stranded beta-sandwich and two C-terminal alpha-helices | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FoF1-ATP synthase | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 16 | - |
ADP | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 20 | - |
phosphate | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 55 | - |
ADP | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 66 | - |
phosphate | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 285 | - |
ATP | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 539 | - |
ATP | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
ATP hydrolysis activity assay at | Escherichia coli |
| 7.5 | 8.8 | ATP synthesis activity assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | FoF1-ATP synthase is an enzyme that is responsible for ATP synthesis during oxidative phosphorylation and photosynthesis. FoF1 is a complex of two rotary motors F1 and Fo, and the ATP synthesis/hydrolysis reaction that is reversibly catalyzed by F1 is coupled with proton transport across membrane-embedded Fo | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 4.8 | - |
phosphate | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 21 | - |
phosphate | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 160 | - |
ADP | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 2200 | - |
ADP | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 3800 | - |
ATP | recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
| 10000 | - |
ATP | recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication | Escherichia coli | |
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