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Literature summary for 7.1.2.2 extracted from
- Torque generation and elastic power transmission in the rotary FOF1-ATPase (2009), Nature, 459, 364-370.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| asymmetric crystal structure of bovine mitochondrial F1 | Bos taurus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Escherichia coli | 16020 | - |
| membrane | - |
Bos taurus | 16020 | - |
| mitochondrion | - |
Bos taurus | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli |  |
| Mg2+ | required | Bos taurus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | Escherichia coli | FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity | ADP + phosphate + H+/out | - |
r | |
| ATP + H2O + H+/in | Bos taurus | FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity | ADP + phosphate + H+/out | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity | Escherichia coli | ADP + phosphate + H+/out | - |
r | |
| ATP + H2O + H+/in | FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity | Bos taurus | ADP + phosphate + H+/out | - |
r | |
| ATP + H2O + H+/in | nucleotide binding structure, nucleotide occupancy of the catalytic sites, overview | Escherichia coli | ADP + phosphate + H+/out | - |
r | |
| ATP + H2O + H+/in | nucleotide binding structure, nucleotide occupancy of the catalytic sites, overview | Bos taurus | ADP + phosphate + H+/out | - |
r | |
| additional information | structure-function analysis, overview | Bos taurus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | F1 is a rotary chemical motor and generator, structure modelling, overview | Escherichia coli |
| More | F1 is a rotary chemical motor and generator, structure modelling, overview | Bos taurus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP synthase | - |
Escherichia coli |
| ATP synthase | - |
Bos taurus |
| FoF1-ATPase | - |
Escherichia coli |
| FoF1-ATPase | - |
Bos taurus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme is an essential machine of the power stations of the cell. In principle, it can operate in either direction, to synthesize ATP at the expense of ion flow, or to drive ion flow while hydrolysing ATP, although this sometimes occurs only in the forward direction | Escherichia coli |
| physiological function | the enzyme is an essential machine of the power stations of the cell. In principle, it can operate in either direction, to synthesize ATP at the expense of ion flow, or to drive ion flow while hydrolysing ATP, although this sometimes occurs only in the forward direction | Bos taurus |
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