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Literature summary for 7.1.2.2 extracted from

  • Esparza-Molto, P.B.; Nuevo-Tapioles, C.; Cuezva, J.M.
    Regulation of the H+-ATP synthase by IF1 a role in mitohormesis (2017), Cell. Mol. Life Sci., 74, 2151-2166 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.2.2

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxyglutarate
-
 Saccharomyces cerevisiae
2-oxoglutarate
-
 Saccharomyces cerevisiae
ATPase inhibitory factor 1 physiological inhibitor Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + 4 H+[side 1] Saccharomyces cerevisiae
-
 ADP + phosphate + 4 H+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + 4 H+[side 1]
-
 Saccharomyces cerevisiae ADP + phosphate + 4 H+[side 2]
-
 ?

Synonyms

Synonyms Comment Organism
H+-ATP synthase the multisubunit complex is built by two major functional domains: the membrane-embedded Fo-ATPase (a and 8c subunits) and the membrane extrinsic catalytic F1-ATPase (3alpha, 3beta, gamma, delta and epsilon subunits) domains Saccharomyces cerevisiae

General Information

General Information Comment Organism
metabolism the enzyme modulates signaling pathways that activate the mitohormetic response, namely ATP, reactive oxygen species, and target of rapamycin Saccharomyces cerevisiae