EC Number | Cloned (Comment) | Organism |
---|---|---|
7.1.2.2 | - |
Haloferax volcanii |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
7.1.2.2 | additional information | the ATP synthase activity is inhibited neither by the F-ATPase inhibitors 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (up to 1 mM) and phlorizin (up to 2 mM) nor by the V-ATPase inhibitor bafilomycin (0.1 mM) | Haloferax volcanii | |
7.1.2.2 | N,N'-dicyclohexylcarbodiimide | incubation of the membranes overnight at 4°C in the presence of 1 mM N,N'-dicyclohexylcarbodiimide results in a residual activity of 18% of the ATP synthesis rate measured with vesicles that are stored under the same conditions without N,N'-dicyclohexylcarbodiimide. Lower concentrations of N,N'-dicyclohexylcarbodiimide and short incubation times have only negligible effects | Haloferax volcanii | |
7.1.2.2 | N-ethylmaleimide | a potent V-ATPase inhibitor, causes only a 5–10% loss of activity if the vesicles are preincubated for 2 h and a concentration of 10 mM is employed | Haloferax volcanii | |
7.1.2.2 | nigericin | 50% inhibition at 4 mM | Haloferax volcanii | |
7.1.2.2 | p-Trifluoromethoxyphenylhydrazone | diminishes ATP synthesis very effectively at 200 mM | Haloferax volcanii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
7.1.2.2 | 0.57 | - |
ADP | pH 9.0, 40°C | Haloferax volcanii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
7.1.2.2 | KCl | like ATP hydrolysis, ATP synthesis can be performed in 1.75 mol/l KCl instead of NaCl | Haloferax volcanii | |
7.1.2.2 | Mg2+ | in contrast to the ATP hydrolysis reaction, where Mn2+ and Mg2+ can be used almost equally, the ATP synthesis reaction strictly depends on Mg2+. Mn2+ can replace Mg2+, but with a dramatic loss of activity | Haloferax volcanii | |
7.1.2.2 | Mn2+ | in contrast to the ATP hydrolysis reaction, where Mn2+ and Mg2+ can be used almost equally, the ATP synthesis reaction strictly depends on Mg2+. Mn2+ can replace Mg2+, but with a dramatic loss of activity | Haloferax volcanii | |
7.1.2.2 | NaCl | like ATP hydrolysis, ATP synthesis can be performed in 1.75 mol/l KCl instead of NaCl | Haloferax volcanii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
7.1.2.2 | 9700 | - |
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE | Haloferax volcanii |
7.1.2.2 | 12000 | - |
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE | Haloferax volcanii |
7.1.2.2 | 37000 | - |
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE | Haloferax volcanii |
7.1.2.2 | 55000 | - |
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE | Haloferax volcanii |
7.1.2.2 | 70000 | - |
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE | Haloferax volcanii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.1.2.2 | ADP + phosphate + H+/out | Haloferax volcanii | the enzyme synthesizes ATP at the expense of a proton gradient | ATP + H2O + H+/in | - |
r | |
7.1.2.2 | ADP + phosphate + H+/out | Haloferax volcanii WR 340 | the enzyme synthesizes ATP at the expense of a proton gradient | ATP + H2O + H+/in | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.1.2.2 | Haloferax volcanii | - |
- |
- |
7.1.2.2 | Haloferax volcanii WR 340 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
7.1.2.2 | - |
Haloferax volcanii |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
7.1.2.2 | 0.0071 | - |
pH 9.0, 40°C, ATP synthesis in presence of Mn2+ | Haloferax volcanii |
7.1.2.2 | 0.0182 | - |
pH 9.0, 40°C, ATP synthesis in presence of Mg2+ | Haloferax volcanii |
7.1.2.2 | 0.0314 | - |
pH 9.0, 40°C, ATP hydrolysis, purified enzyme | Haloferax volcanii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.1.2.2 | ADP + phosphate + H+/out | - |
Haloferax volcanii | ATP + H2O + H+/in | - |
r | |
7.1.2.2 | ADP + phosphate + H+/out | the enzyme synthesizes ATP at the expense of a proton gradient | Haloferax volcanii | ATP + H2O + H+/in | - |
r | |
7.1.2.2 | ADP + phosphate + H+/out | - |
Haloferax volcanii WR 340 | ATP + H2O + H+/in | - |
r | |
7.1.2.2 | ADP + phosphate + H+/out | the enzyme synthesizes ATP at the expense of a proton gradient | Haloferax volcanii WR 340 | ATP + H2O + H+/in | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
7.1.2.2 | ? | the calculated molecular masses of the deduced gene products are 22.0 kDa (subunit D), 38.7 kDa (subunit C), 11.6 kDa (subunit E), 52.0 kDa (subunit B), and 64.5 kDa (subunit A). The described operon contains genes in the order D, C, E, B, and A. It contains no gene for the hydrophobic, so-called proteolipid (subunit c, the proton-conducting subunit of the A0 part). This subunit is isolated and purified its molecular mass as deduced by SDS-polyacrylamide gel electrophoresis is 9.7 kDa | Haloferax volcanii |
7.1.2.2 | ? | x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE | Haloferax volcanii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
7.1.2.2 | 60 | - |
ATP synthesis in washed membranes of Haloferax volcanii | Haloferax volcanii |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
7.1.2.2 | 25 | 70 | ATP synthesis in washed membranes of Haloferax volcanii, 25°C: 10% of the optimal activity, 30°C: 30% of the optimal activity | Haloferax volcanii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
7.1.2.2 | 9 | - |
ATP synthesis in washed membranes of Haloferax volcanii | Haloferax volcanii |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
7.1.2.2 | 10 | - |
ATP synthesis in washed membranes of Haloferax volcanii, 75% of the optimal activity | Haloferax volcanii |