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Literature summary for 7.1.2.2 extracted from

  • Steinert, K.; Wagner, V.; Kroth-Pancic, P.G.; Bickel-Sandkötter, S.
    Characterization and subunit structure of the ATP synthase of the halophilic archaeon Haloferax volcanii and organization of the ATP synthase genes (1997), J. Biol. Chem., 272, 6261-6269.
    View publication on PubMed
Search for more literature for 7.1.2.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Haloferax volcanii

Inhibitors

Inhibitors Comment Organism Structure
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
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
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
nigericin 50% inhibition at 4 mM Haloferax volcanii
p-Trifluoromethoxyphenylhydrazone diminishes ATP synthesis very effectively at 200 mM Haloferax volcanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.57
-
 ADP pH 9.0, 40°C Haloferax volcanii

Metals/Ions

Metals/Ions Comment Organism Structure
KCl like ATP hydrolysis, ATP synthesis can be performed in 1.75 mol/l KCl instead of NaCl Haloferax volcanii
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
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
NaCl like ATP hydrolysis, ATP synthesis can be performed in 1.75 mol/l KCl instead of NaCl Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
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
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
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
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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + phosphate + H+/out Haloferax volcanii the enzyme synthesizes ATP at the expense of a proton gradient ATP + H2O + H+/in
-
 r
ADP + phosphate + H+/out Haloferax volcanii WR 340 the enzyme synthesizes ATP at the expense of a proton gradient ATP + H2O + H+/in
-
 r

Organism

Organism UniProt Comment Textmining
Haloferax volcanii
-
-
-
Haloferax volcanii WR 340
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0071
-
 pH 9.0, 40°C, ATP synthesis in presence of Mn2+ Haloferax volcanii
0.0182
-
 pH 9.0, 40°C, ATP synthesis in presence of Mg2+ Haloferax volcanii
0.0314
-
 pH 9.0, 40°C, ATP hydrolysis, purified enzyme Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphate + H+/out
-
 Haloferax volcanii ATP + H2O + H+/in
-
 r
ADP + phosphate + H+/out the enzyme synthesizes ATP at the expense of a proton gradient Haloferax volcanii ATP + H2O + H+/in
-
 r
ADP + phosphate + H+/out
-
 Haloferax volcanii WR 340 ATP + H2O + H+/in
-
 r
ADP + phosphate + H+/out the enzyme synthesizes ATP at the expense of a proton gradient Haloferax volcanii WR 340 ATP + H2O + H+/in
-
 r

Subunits

Subunits Comment Organism
? 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
? x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 ATP synthesis in washed membranes of Haloferax volcanii Haloferax volcanii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 ATP synthesis in washed membranes of Haloferax volcanii Haloferax volcanii

pH Range

pH Minimum pH Maximum Comment Organism
10
-
 ATP synthesis in washed membranes of Haloferax volcanii, 75% of the optimal activity Haloferax volcanii