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Literature summary extracted from

  • Kim, Y.; Konno, H.; Sugano, Y.; Hisabori, T.
    Redox regulation of rotation of the cyanobacterial F1-ATPase containing thiol regulation switch (2011), J. Biol. Chem., 286, 9071-9078.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.1.2.2 lauryl dimethylamine-N-oxide
-
 Thermosynechococcus vestitus
7.1.2.2 additional information by reduction, both the alpha3beta3gammaredox complex and the purified CF1 show a 2.7fold activation Thermosynechococcus vestitus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.2.2 expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex Spinacia oleracea
7.1.2.2 expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex Thermosynechococcus vestitus

Protein Variants

EC Number Protein Variants Comment Organism
7.1.2.2 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
7.1.2.2 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

EC Number Inhibitors Comment Organism Structure
7.1.2.2 ADP
-
 Spinacia oleracea
7.1.2.2 ADP inhibition of the enzyme causing pauses in the ATP synthesis or hydrolysis, reversible by lauryl dimethylamine-N-oxide Thermosynechococcus vestitus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.2.2 chloroplast
-
 Spinacia oleracea 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.2.2 Mg2+ required Spinacia oleracea
7.1.2.2 Mg2+ required Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.2.2 ATP + H2O + H+/in Thermosynechococcus vestitus
-
 ADP + phosphate + H+/out
-
 r
7.1.2.2 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

EC Number Organism UniProt Comment Textmining
7.1.2.2 Spinacia oleracea
-
-
-
7.1.2.2 Thermosynechococcus vestitus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.2.2 recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration Spinacia oleracea
7.1.2.2 recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration Thermosynechococcus vestitus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.2.2 ATP + H2O + H+/in
-
 Spinacia oleracea ADP + phosphate + H+/out
-
 r
7.1.2.2 ATP + H2O + H+/in
-
 Thermosynechococcus vestitus ADP + phosphate + H+/out
-
 r
7.1.2.2 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

EC Number Synonyms Comment Organism
7.1.2.2 F1-ATP synthase
-
 Spinacia oleracea
7.1.2.2 F1-ATP synthase
-
 Thermosynechococcus vestitus
7.1.2.2 F1-ATPase
-
 Spinacia oleracea
7.1.2.2 F1-ATPase
-
 Thermosynechococcus vestitus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.1.2.2 25
-
 ATP hydrolysis assay at Spinacia oleracea
7.1.2.2 25
-
 ATP hydrolysis assay at Thermosynechococcus vestitus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.2.2 7.5
-
 ATP hydrolysis assay at Spinacia oleracea
7.1.2.2 7.5
-
 ATP hydrolysis assay at Thermosynechococcus vestitus

General Information

EC Number General Information Comment Organism
7.1.2.2 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