Cloned (Comment) | Organism |
---|---|
expression of wild-type FoF1 and subunit epsilon mutant EFoF1 in Escherichia coli strain RA1 | Escherichia coli |
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 | 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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Escherichia coli | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type enzyme and subunit epsilon mutant EFoF1 from Escherichia coli strain RA1 | Escherichia coli |
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 (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 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 | 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 | 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 | Comment | Organism |
---|---|---|
FoF1-ATP synthase | - |
Escherichia coli |
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 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 | 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 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 |