12 Facts About ATP synthase


ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate using adenosine diphosphate and inorganic phosphate .

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F1 portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP.

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The FO region of ATP synthase is a proton pore that is embedded in the mitochondrial membrane.

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The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy studies of the complex.

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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.

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Under the right conditions, the enzyme reaction can be carried out in reverse, with ATP synthase hydrolysis driving proton pumping across the membrane.

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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.

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Evolution of ATP synthase is thought to have been modular whereby two functionally independent subunits became associated and gained new functionality.

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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.

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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.

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The overall structure and the catalytic mechanism of the chloroplast ATP synthase are almost the same as those of the bacterial enzyme.

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The ATP synthase has a 40-aa insert in the gamma-subunit to inhibit wasteful activity when dark.

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