EC Number   |
Reaction |
Reference |
|---|
    7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
ATP synthase uses a unique rotary mechanism to couple ATP synthesis and hydrolysis to transmembrane proton translocation. As part of the synthesis mechanism, the torque of the rotor has to be converted into conformational rearrangements of the catalytic binding sites on the stator to allow synthesis and release of ATP. The gamma subunit of the rotor plays a central role in the energy conversion. The N-terminal helix alone is able to fulfill the function of full-length gamma in ATP synthesis as long as it connects to the rest of the rotor. This connection can occur via the epsilon subunit. No direct contact between epsilon and the gamma ring seems to be required. The epsilon subunit of the rotor exists in two different conformations during ATP synthesis and ATP hydrolysis. Reaction mechanism, overview |
712383 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
catalytic mechanism of the enzyme complex |
686272 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
mechanism of proton conduction through F0, and the catalytic mechanism of F1 |
210247, 210248 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
model of mechanochemical coupling, overview |
712371 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
reaction mechanism and structure-fucntion analysis, overview |
712416 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview |
-, 711288 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
structure-function relationship from F1 crystal structure in the stable conformational state, catalytic mechanism, F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state, betaDP is the catalytically active form, overview |
-, 700972 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
substrate modulation of multi-site activity of F1 is due to the substrate binding to the second catalytic site, bi-site catalytic mechanism, effects of Mg2+, overview |
711178 |
| 7.1.2.2 | ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] |
X-ray structure is compatible with a catalytic mechanism in which all three F1-ATPase catalytic sites must fill with MgATP to initiate steady-state hydrolysis |
210260 |
