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Literature summary for 7.2.2.1 extracted from

  • Mayer, F.; Lim, J.K.; Langer, J.D.; Kang, S.G.; Müller, V.
    Na+ transport by the A1AO ATP synthase purified from Thermococcus onnurineus and reconstituted into liposomes (2015), J. Biol. Chem., 290, 6994-7002.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.1

Activating Compound

Activating Compound Comment Organism Structure
3,5-di-tert-butyl-4-hydroxybenzylidenemalononitrile i.e.SF 6847. Transport of Na+ is slightly stimulated, indicating that Na+ transport is electrogenic Thermococcus onnurineus
NaHSO3 stimulates Thermococcus onnurineus

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ almost no ATPase activity is observed in the presence of CuCl2 or NiCl2 Thermococcus onnurineus
diethylstilbestrol 0.75 mM, almost complete inhibition. ATP-driven Na+ transport in proteoliposomes is also inhibited completely Thermococcus onnurineus
N,N'-dicyclohexyl-carbodiimide half maximal inhibition at 0.1 mM. N,N'-dicyclohexyl-carbodiimide and Na+ compete for binding to subunit c Thermococcus onnurineus
N,N,N',N'-tetracyclohexyl-1,2-phenylenedioxydiacetamide i.e. ETH 2120, complete inhibition. Addition of ETH 2120 to the assay during active transport of Na+ immediately stops further Na+ translocation into the lumen of the proteoliposomes Thermococcus onnurineus
Ni2+ almost no ATPase activity is observed in the presence of CuCl2 or NiCl2 Thermococcus onnurineus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Thermococcus onnurineus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the enzyme requires divalent cations for activity, highest stimulation is with Mn2+ followed by Mg2+ and Co2+ (10 mM each) Thermococcus onnurineus
Mn2+ the enzyme requires divalent cations for activity, highest stimulation is with Mn2+ followed by Mg2+ and Co2+ (10 mM each) Thermococcus onnurineus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
670000
-
 gel filtration Thermococcus onnurineus

Organism

Organism UniProt Comment Textmining
Thermococcus onnurineus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermococcus onnurineus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Na+/in the enzyme reconstituted in proteoliposomes, generated from Escherichia coli lipids, catalyzes ATP-driven Na+ transport Thermococcus onnurineus ADP + phosphate + Na+/out
-
 ?

Subunits

Subunits Comment Organism
nonamer the c subunit determines the ion specificity of the ATP synthases/ATPases (Na+-transporting or H+-transporting). Calculated from sequence, the c subunit has a molecular mass of 16061 Da with four transmembrane helices Thermococcus onnurineus

Synonyms

Synonyms Comment Organism
A1AO ATP synthase
-
 Thermococcus onnurineus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
 Thermococcus onnurineus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Thermococcus onnurineus