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Literature summary for 7.1.2.2 extracted from
- Biochemistry and genetics of bacterial H+-translocating ATPase (1981), Curr. Top. Bioenerg., 11, 35-106.
No PubMed abstract available
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Aurovertin | - |
Bacteria |  |
| Aurovertin | - |
Escherichia coli | |
| N,N'-dicyclohexylcarbodiimide | - |
Bacillus sp. PS3 | |
| N,N'-dicyclohexylcarbodiimide | binds to F0 | Bacteria | |
| N,N'-dicyclohexylcarbodiimide | - |
Enterococcus faecalis | |
| N,N'-dicyclohexylcarbodiimide | - |
Escherichia coli | |
| N3- | - |
Bacteria | |
| N3- | - |
Escherichia coli | |
| N3- | - |
Micrococcus luteus | |
| oligomycin | binds to F0 | Bacteria | |
| oligomycin | - |
Escherichia coli | |
| tributyltin | - |
Bacillus sp. PS3 | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Bacteria | 16020 | - |
| membrane | - |
Escherichia coli | 16020 | - |
| membrane | - |
Enterococcus faecalis | 16020 | - |
| membrane | - |
Micrococcus luteus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli | |
| Mg2+ | - |
Enterococcus faecalis | |
| Mg2+ | required | Bacteria | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + phosphate + H+ | Bacteria | couples the H+-translocation driven by an electrochemical potential of H+ to the synthesis of ATP from ADP and phosphate. ATPase in photosynthetic bacteria and strict aerobes seems to function strictly as the ATP-synthetase of photophosphorylation or oxidative phosphorylation | ATP + H2O | - |
r | |
| ATP + phosphate + H+/in | Bacteria | the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen | ADP + phosphate + H+/out | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Allochromatium vinosum | - |
- |
- |
| Bacillus sp. PS3 | - |
- |
- |
| Bacteria | - |
- |
- |
| Clostridium sp. | - |
- |
- |
| Enterococcus faecalis | - |
- |
- |
| Escherichia coli | - |
- |
- |
| Micrococcus luteus | - |
- |
- |
| Mycolicibacterium phlei | - |
- |
- |
| Rhodospirillum rubrum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
- |
Enterococcus faecalis |
- |
Mycolicibacterium phlei |
- |
Rhodospirillum rubrum |
- |
Bacillus sp. PS3 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + phosphate + H+ | couples the H+-translocation driven by an electrochemical potential of H+ to the synthesis of ATP from ADP and phosphate. ATPase in photosynthetic bacteria and strict aerobes seems to function strictly as the ATP-synthetase of photophosphorylation or oxidative phosphorylation | Bacteria | ATP + H2O | - |
r | |
| ATP + H2O + H+/in | - |
Escherichia coli | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Enterococcus faecalis | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Mycolicibacterium phlei | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Micrococcus luteus | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Rhodospirillum rubrum | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Clostridium sp. | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Allochromatium vinosum | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Bacillus sp. PS3 | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen | Bacteria | ADP + phosphate + H+/out | - |
r | |
| ATP + phosphate + H+/in | the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen | Bacteria | ADP + phosphate + H+/out | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | F1 is composed of five types of subunits, F0 is composed of three types of subunits, ratio of F1 subunits: alpha3beta3gamma1delta1epsilon1, ratio of F0 subunits: chi2psi2omega10 | Escherichia coli |
| More | the enzyme is composed of two structurally and functionally distinct sectors, F1 and F0. F1 shows ATPase activity, Fo mediates H+ translocation across the membrane | Bacteria |
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