Protein Variants | Comment | Organism |
---|---|---|
E190D | the mutation in the beta-subunit reduces the ATP hydrolysis | Bacillus sp. (in: Bacteria) |
R84C/E190D/E391C | incorporating of a single copy of the mutant beta-subunit to construct the chimera F1, alpha3beta2beta(E190D/E391C)gamma(R84C) which shows slowed ATP hydrolysis | Bacillus sp. (in: Bacteria) |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
adenosine-5'-(beta,gamma-imino)-triphosphate | inhibits F1 rotation | Bacillus sp. (in: Bacteria) | |
azide | inhibits F1 rotation | Bacillus sp. (in: Bacteria) |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Bacillus sp. (in: Bacteria) | 16020 | - |
mitochondrion | - |
Bacillus sp. (in: Bacteria) | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | Bacillus sp. (in: Bacteria) | - |
ADP + phosphate + H+/out | - |
? | |
ATP + H2O + H+/in | Bacillus sp. (in: Bacteria) PS3 | - |
ADP + phosphate + H+/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus sp. (in: Bacteria) | - |
- |
- |
Bacillus sp. (in: Bacteria) PS3 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Bacillus sp. (in: Bacteria) |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | - |
Bacillus sp. (in: Bacteria) | ADP + phosphate + H+/out | - |
? | |
ATP + H2O + H+/in | F1-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the gamma-subunit against the alpha3beta3 ring, betaDP is the catalytically active form | Bacillus sp. (in: Bacteria) | ADP + phosphate + H+/out | - |
? | |
ATP + H2O + H+/in | - |
Bacillus sp. (in: Bacteria) PS3 | ADP + phosphate + H+/out | - |
? | |
ATP + H2O + H+/in | F1-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the gamma-subunit against the alpha3beta3 ring, betaDP is the catalytically active form | Bacillus sp. (in: Bacteria) PS3 | ADP + phosphate + H+/out | - |
? | |
additional information | structure-function relationship of the R84C/E190D/E391C mutant enzyme, overview | Bacillus sp. (in: Bacteria) | ? | - |
? | |
additional information | structure-function relationship of the R84C/E190D/E391C mutant enzyme, overview | Bacillus sp. (in: Bacteria) PS3 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structure analysis F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state | Bacillus sp. (in: Bacteria) |
Synonyms | Comment | Organism |
---|---|---|
F1-ATPase | - |
Bacillus sp. (in: Bacteria) |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Bacillus sp. (in: Bacteria) |