EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
7.1.2.2 | 2'-deoxy-ATP + H2O |
- |
Enterococcus faecalis |
2'-deoxy-ADP + phosphate + H+/out |
- |
? |
7.1.2.2 | ADP + phosphate + 4 H+[side 2] |
- |
Escherichia coli |
ATP + H2O + 4 H+[side 1] |
- |
r |
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 |
Paracoccus denitrificans |
ATP + H2O + 4 H+[side 1] |
- |
r |
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 |
Escherichia coli |
ATP + H2O + 4 H+[side 1] |
- |
r |
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 |
Paracoccus denitrificans 1222 |
ATP + H2O + 4 H+[side 1] |
- |
r |
7.1.2.2 | ADP + phosphate + H+ |
- |
Spinacia oleracea |
ATP + H2O |
- |
r |
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 |
Bacteria |
ATP + H2O |
- |
r |
7.1.2.2 | ADP + phosphate + H+ |
terminal enzyme in oxidative phosphorylation |
Bos taurus |
ATP + H2O |
- |
r |
7.1.2.2 | ADP + phosphate + H+ |
low rates of ATP synthesis |
[Clostridium] paradoxum |
ATP + H2O |
- |
? |
7.1.2.2 | ADP + phosphate + H+ |
low rates of ATP synthesis |
[Clostridium] paradoxum DSM 7308 |
ATP + H2O |
- |
? |