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Literature summary for 7.1.2.2 extracted from

  • Andrianaivomananjaona, T.; Moune-Dimala, M.; Herga, S.; David, V.; Haraux, F.
    How the N-terminal extremity of Saccharomyces cerevisiae IF1 interacts with ATP synthase: a kinetic approach (2011), Biochim. Biophys. Acta, 1807, 197-204.
    View publication on PubMed
Search for more literature for 7.1.2.2

Inhibitors

Inhibitors Comment Organism Structure
intrinsic inhibitory peptide IF1 from Saccharomyces cerevisiae, the N-terminal part of the inhibitory peptide IF1 interacts with the central gamma subunit of mitochondrial isolated extrinsic part of ATP synthase in the inhibited complex. Kinetics of inhibition of the isolated and membrane-bound enzymes with IF1 modified in N-terminal extremity, i.e. IF1-Nter, overview. IF1-Nter plays no role in the recognition step but contributes to stabilize the inhibited complex. Its binding to the enzyme is not affected by truncations or fusion with PsaE, a 8 kDa globular-like protein Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic model of the F1-ATPase, dependence of kinetic behaviour on the ATP concentration, overview Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial membrane
-
 Saccharomyces cerevisiae 31966
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Saccharomyces cerevisiae
-
 ADP + phosphate + H+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Saccharomyces cerevisiae ADP + phosphate + H+/out
-
 ?

Synonyms

Synonyms Comment Organism
ATP synthase
-
 Saccharomyces cerevisiae
F0F1-ATPase
-
 Saccharomyces cerevisiae
F1-ATPase isolated extrinsic part of ATP synthase, extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information F1-ATPase is the isolated extrinsic part of ATP synthase, the extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria Saccharomyces cerevisiae