Activating Compound | Comment | Organism | Structure |
---|---|---|---|
lauryl dimethylamine-N-oxide | - |
Thermosynechococcus vestitus | |
additional information | by reduction, both the alpha3beta3gammaredox complex and the purified CF1 show a 2.7fold activation | Thermosynechococcus vestitus |
Cloned (Comment) | Organism |
---|---|
expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex | Spinacia oleracea |
expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex | Thermosynechococcus vestitus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a chimeric F1 complex using cyanobacterial F1 from Thermosynechoccus elongatus, which mimics the regulatory properties of the chloroplast F1-ATPase introducing the regulatory element of spinach F1-ATPase gamma subunit, residues 187-210. The redox state of the gamma-subunit does not affect the ATP-binding rate to the catalytic site(s) and the torque for rotation. The long pauses caused by ADP inhibition are frequently observed in the oxidized state. The duration of continuous rotation is relatively shorter in the oxidized recombinant alpha3beta3gammaredox complex. The chimeric complex becomes biotinylated and shows higher stability for purification and assay experiments than the cyanobacterial wild-type, overview | Spinacia oleracea |
additional information | construction of a chimeric F1 complex using the cyanobacterial F1, which mimics the regulatory properties of the chloroplast F1-ATPase from Spinacia oleracea introducing the regulatory element of the higher plant F1-ATPase gamma subunit, residues187-210. The redox state of the gamma-subunit does not affect the ATP-binding rate to the catalytic site(s) and the torque for rotation. The long pauses caused by ADP inhibition are frequently observed in the oxidized state. The duration of continuous rotation is relatively shorter in the oxidized recombinant alpha3beta3gammaredox complex. The chimeric complex becomes biotinylated and shows higher stability for purification and assay experiments than the cyanobacterial wild-type, overview | Thermosynechococcus vestitus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Spinacia oleracea | |
ADP | inhibition of the enzyme causing pauses in the ATP synthesis or hydrolysis, reversible by lauryl dimethylamine-N-oxide | Thermosynechococcus vestitus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Spinacia oleracea | 9507 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Spinacia oleracea | |
Mg2+ | required | Thermosynechococcus vestitus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | Thermosynechococcus vestitus | - |
ADP + phosphate + H+/out | - |
r | |
ATP + H2O + H+/in | Spinacia oleracea | F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis | ADP + phosphate + H+/out | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Spinacia oleracea | - |
- |
- |
Thermosynechococcus vestitus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration | Spinacia oleracea |
recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration | Thermosynechococcus vestitus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | - |
Spinacia oleracea | ADP + phosphate + H+/out | - |
r | |
ATP + H2O + H+/in | - |
Thermosynechococcus vestitus | ADP + phosphate + H+/out | - |
r | |
ATP + H2O + H+/in | F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis | Spinacia oleracea | ADP + phosphate + H+/out | - |
r |
Synonyms | Comment | Organism |
---|---|---|
F1-ATP synthase | - |
Spinacia oleracea |
F1-ATP synthase | - |
Thermosynechococcus vestitus |
F1-ATPase | - |
Spinacia oleracea |
F1-ATPase | - |
Thermosynechococcus vestitus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
ATP hydrolysis assay at | Spinacia oleracea |
25 | - |
ATP hydrolysis assay at | Thermosynechococcus vestitus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
ATP hydrolysis assay at | Spinacia oleracea |
7.5 | - |
ATP hydrolysis assay at | Thermosynechococcus vestitus |
General Information | Comment | Organism |
---|---|---|
metabolism | F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis. Chloroplast F1-ATPase is subject to redox regulation, whereby ATP hydrolysis activity is regulated by formation and reduction of the disulfide bond located on the gamma-subunit, molecular mechanism, overview | Spinacia oleracea |