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 | 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Thermococcus onnurineus | 16020 | - |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
670000 | - |
gel filtration | Thermococcus onnurineus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus onnurineus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Thermococcus onnurineus |
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 | 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 | Comment | Organism |
---|---|---|
A1AO ATP synthase | - |
Thermococcus onnurineus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
- |
Thermococcus onnurineus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Thermococcus onnurineus |