Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Lauryldimethylamine oxide | LDAO, stimulates F1-ATPase | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes complex in strain DK8 | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
aR210A/aN214R | site-directed mutagenesis, the subunit a mutant supports proton conduction onyl through EF1-depleted EFo, but not in EfoEF1, nor ATP-driven proton pumping | Escherichia coli |
cD61N/cM65D | site-directed mutagenesis, the subunit c mutant grows on succinate, retains the ability to synthesize ATP, and supports passive proton conduction, but not ATP hydrolysis-driven proton pumping, overview | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Dicyclohexylcarbodiimide | DCCD | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | bound | Escherichia coli | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | Escherichia coli | the enzyme complex can pump protons in the reverse direction driven by ATP hydrolysis generating a ion-motive force, the F1 domain, comprising subunits alpha3beta3gammadeltaepsilon and possessing the nucleotide binding site, is responsible for the ATP hydrolysis upon detachment from the Fo domain | ADP + phosphate + H+/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | - |
Escherichia coli | ADP + phosphate + H+/out | - |
? | |
ATP + H2O + H+/in | the enzyme complex can pump protons in the reverse direction driven by ATP hydrolysis generating a ion-motive force, the F1 domain, comprising subunits alpha3beta3gammadeltaepsilon and possessing the nucleotide binding site, is responsible for the ATP hydrolysis upon detachment from the Fo domain | Escherichia coli | ADP + phosphate + H+/out | - |
? |
Synonyms | Comment | Organism |
---|---|---|
F1-ATPase | - |
Escherichia coli |
FoF1 ATP synthase | - |
Escherichia coli |