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Literature summary for 7.2.2.1 extracted from

  • Pisa, K.Y.; Huber, H.; Thomm, M.; Mueller, V.
    A sodium ion-dependent A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus (2007), FEBS J., 274, 3928-3938.
    View publication on PubMed
Search for more literature for 7.2.2.1

Inhibitors

Inhibitors Comment Organism Structure
dienestrol
-
 Pyrococcus furiosus
diethylstilbestrol
-
 Pyrococcus furiosus
Hexestrol
-
 Pyrococcus furiosus
additional information trans-stilbene does not inhibit ATP hydrolysis Pyrococcus furiosus
N',N'-dicyclohexylcarbodiimide inhibition can be relieved by Na+ Pyrococcus furiosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.63
-
 ATP pH 6.0, 100°C Pyrococcus furiosus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Pyrococcus furiosus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
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
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
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Na+/in Pyrococcus furiosus
-
 ADP + phosphate + Na+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.8
-
 pH 6.0, 100°C Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Na+/in
-
 Pyrococcus furiosus ADP + phosphate + Na+/out
-
 ?
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
-
 ?
CTP + H2O + Na+/in CTP is hydrolyzed at 14% compared to hydrolysis of ATP Pyrococcus furiosus CDP + phosphate + Na+/out
-
 ?
GTP + H2O + Na+/in GTP is hydrolyzed at 64% compared to hydrolysis of ATP Pyrococcus furiosus GDP + phosphate + Na+/out
-
 ?
ITP + H2O + Na+/in ITP is hydrolyzed at 99% compared to hydrolysis of ATP Pyrococcus furiosus IDP + phosphate + Na+/out
-
 ?
additional information neither ADP nor diphosphate are hydrolyzed Pyrococcus furiosus ?
-
 ?
UTP + H2O + Na+/in UTP is hydrolyzed at 31% compared to hydrolysis of ATP Pyrococcus furiosus UDP + phosphate + Na+/out
-
 ?

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
A1AO ATP synthase
-
 Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
100
-
-
 Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Pyrococcus furiosus

pH Range

pH Minimum pH Maximum Comment Organism
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

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.36
-
 pH 6.0, 100°C Pyrococcus furiosus diethylstilbestrol
0.52
-
 pH 6.0, 100°C Pyrococcus furiosus dienestrol
0.59
-
 pH 6.0, 100°C Pyrococcus furiosus Hexestrol