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Literature summary extracted from
- A sodium ion-dependent A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus (2007), FEBS J., 274, 3928-3938.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 2.7.7.7 | hanging-drop vapor-diffusion method at 20°C, the N-terminal (1300) domain structure of the large subunit was determined by X-ray crystallography. The determined structure consists of nine alpha helices and three beta strands. The N-terminal (1100) region plays crucial roles in the folding of the large subunit dimer by connecting the about 50 N-terminal residues with their own catalytic region (7921163) | Pyrococcus horikoshii |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.1 | dienestrol | - |
Pyrococcus furiosus |  |
| 7.2.2.1 | diethylstilbestrol | - |
Pyrococcus furiosus | |
| 7.2.2.1 | Hexestrol | - |
Pyrococcus furiosus | |
| 7.2.2.1 | additional information | trans-stilbene does not inhibit ATP hydrolysis | Pyrococcus furiosus | |
| 7.2.2.1 | N',N'-dicyclohexylcarbodiimide | inhibition can be relieved by Na+ | Pyrococcus furiosus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.1 | 0.63 | - |
ATP | pH 6.0, 100°C | Pyrococcus furiosus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.2.2.1 | membrane | - |
Pyrococcus furiosus | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.2.2.1 | Ca2+ | divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%) | Pyrococcus furiosus | |
| 7.2.2.1 | Cu2+ | divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%) | Pyrococcus furiosus | |
| 7.2.2.1 | Mg2+ | divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%) | Pyrococcus furiosus | |
| 7.2.2.1 | Mn2+ | divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%) | Pyrococcus furiosus | |
| 7.2.2.1 | Ni2+ | divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%) | Pyrococcus furiosus | |
| 7.2.2.1 | Zn2+ | divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%) | Pyrococcus furiosus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.1 | ATP + H2O + Na+/in | Pyrococcus furiosus | - |
ADP + phosphate + Na+/out | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.7.7.7 | Pyrococcus horikoshii | O57861 | - |
- |
| 2.7.7.7 | Pyrococcus horikoshii OT-3 | O57861 | - |
- |
| 7.2.2.1 | Pyrococcus furiosus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.2.2.1 | - |
Pyrococcus furiosus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.1 | 5.8 | - |
pH 6.0, 100°C | Pyrococcus furiosus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.1 | ATP + H2O + Na+/in | - |
Pyrococcus furiosus | ADP + phosphate + Na+/out | - |
? | |
| 7.2.2.1 | ATP + H2O + Na+/in | ATP hydrolysis is strictly dependent on Na+, with a Km of 0.6 mM. Li+, but not K+, can substitute for Na+. The Na+ dependence is less pronounced at higher proton concentrations, indicating competition between Na+ and H+ for a common binding site | Pyrococcus furiosus | ADP + phosphate + Na+/out | - |
? | |
| 7.2.2.1 | CTP + H2O + Na+/in | CTP is hydrolyzed at 14% compared to hydrolysis of ATP | Pyrococcus furiosus | CDP + phosphate + Na+/out | - |
? | |
| 7.2.2.1 | GTP + H2O + Na+/in | GTP is hydrolyzed at 64% compared to hydrolysis of ATP | Pyrococcus furiosus | GDP + phosphate + Na+/out | - |
? | |
| 7.2.2.1 | ITP + H2O + Na+/in | ITP is hydrolyzed at 99% compared to hydrolysis of ATP | Pyrococcus furiosus | IDP + phosphate + Na+/out | - |
? | |
| 7.2.2.1 | additional information | neither ADP nor diphosphate are hydrolyzed | Pyrococcus furiosus | ? | - |
? | |
| 7.2.2.1 | UTP + H2O + Na+/in | UTP is hydrolyzed at 31% compared to hydrolysis of ATP | Pyrococcus furiosus | UDP + phosphate + Na+/out | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 2.7.7.7 | heterotetramer | consisting of two large polymerase subunits and two small exonuclease subunits | Pyrococcus horikoshii |
| 7.2.2.1 | More | hypothetical model of the subunit topology of A1AO ATP synthases: subunits a and c form the membrane-embedded motor, with a being the stator, and multiple copies of subunit c forming the rotor. The rotor subunit c forms an SDS-resistant oligomer | Pyrococcus furiosus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.2.2.1 | A1AO ATP synthase | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.1 | 100 | - |
- |
Pyrococcus furiosus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.1 | 6 | - |
- |
Pyrococcus furiosus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.1 | 5.5 | 9 | pH 5.0: about 20% of maximal activity, pH 5.5: about 85% of maximal activity, pH 9.0: abozt 55% of maximal activity | Pyrococcus furiosus |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 7.2.2.1 | 0.36 | - |
pH 6.0, 100°C | Pyrococcus furiosus | diethylstilbestrol | |
| 7.2.2.1 | 0.52 | - |
pH 6.0, 100°C | Pyrococcus furiosus | dienestrol | |
| 7.2.2.1 | 0.59 | - |
pH 6.0, 100°C | Pyrococcus furiosus | Hexestrol | |
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