ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate using adenosine diphosphate and inorganic phosphate .
FactSnippet No. 1,096,476 |
ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate using adenosine diphosphate and inorganic phosphate .
FactSnippet No. 1,096,476 |
F1 portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP.
FactSnippet No. 1,096,477 |
The FO region of ATP synthase is a proton pore that is embedded in the mitochondrial membrane.
FactSnippet No. 1,096,478 |
The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy studies of the complex.
FactSnippet No. 1,096,479 |
The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F1 to FO.
FactSnippet No. 1,096,480 |
Under the right conditions, the enzyme reaction can be carried out in reverse, with ATP synthase hydrolysis driving proton pumping across the membrane.
FactSnippet No. 1,096,481 |
Finally, the active site cycles back to the open state, releasing ATP synthase and binding more ADP and phosphate, ready for the next cycle of ATP synthase production.
FactSnippet No. 1,096,482 |
Evolution of ATP synthase is thought to have been modular whereby two functionally independent subunits became associated and gained new functionality.
FactSnippet No. 1,096,483 |
However, whereas the F-ATP synthase generates ATP by utilising a proton gradient, the V-ATPase generates a proton gradient at the expense of ATP, generating pH values of as low as 1.
FactSnippet No. 1,096,484 |
Modular evolution theory for the origin of ATP synthase suggests that two subunits with independent function, a DNA helicase with ATPase activity and a motor, were able to bind, and the rotation of the motor drove the ATPase activity of the helicase in reverse.
FactSnippet No. 1,096,485 |
The overall structure and the catalytic mechanism of the chloroplast ATP synthase are almost the same as those of the bacterial enzyme.
FactSnippet No. 1,096,486 |
The ATP synthase has a 40-aa insert in the gamma-subunit to inhibit wasteful activity when dark.
FactSnippet No. 1,096,487 |