EC Number   |
Natural Substrates |
|---|
    7.1.2.2 | ADP + phosphate + 4 H+[side 2] |
- |
| 7.1.2.2 | ADP + phosphate + 4 H+[side 2] |
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed |
| 7.1.2.2 | ADP + phosphate + 4 H+[side 2] |
the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis |
| 7.1.2.2 | ADP + phosphate + H+ |
couples the H+-translocation driven by an electrochemical potential of H+ to the synthesis of ATP from ADP and phosphate. ATPase in photosynthetic bacteria and strict aerobes seems to function strictly as the ATP-synthetase of photophosphorylation or oxidative phosphorylation |
| 7.1.2.2 | ADP + phosphate + H+ |
terminal enzyme in oxidative phosphorylation |
| 7.1.2.2 | ADP + phosphate + H+/out |
- |
| 7.1.2.2 | ADP + phosphate + H+/out |
the enzyme cannot synthesize ATP in the dark, but may catalyze futile ATP hydrolysis reactions |
| 7.1.2.2 | ADP + phosphate + H+/out |
the enzyme synthesizes ATP at the expense of a proton gradient |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] |
- |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] |
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed |
