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Literature summary for 7.1.2.2 extracted from

  • Wagner, K.; Perschil, I.; Fichter, C.D.; van der Laan, M.
    Stepwise assembly of dimeric F1Fo-ATP synthase in mitochondria involves the small Fo-subunits k and i (2010), Mol. Biol. Cell, 21, 1494-1504.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.2.2

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane oligomerization of ATP synthase is critical for the morphology of the inner mitochondrial membrane because it supports the generation of tubular cristae membrane domains, overview. Association of individual F1Fo-ATP synthase complexes is mediated by the membrane-embedded Fo-part Saccharomyces cerevisiae 5743
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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
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 ADP + phosphate + H+/out
-
 r

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
-
 r

Subunits

Subunits Comment Organism
oligomer oligomerization of ATP synthase is critical for the morphology of the inner mitochondrial membrane because it supports the generation of tubular cristae membrane domains, overview. Association of individual F1Fo-ATP synthase complexes is mediated by the membrane-embedded Fo-part. Subunits e, g, k, and i are involved in the stepwise assembly of F1Fo-ATP synthase dimers and oligomers. Subunit i facilitates the incorporation of newly synthesized subunits into ATP synthase complexes, while subunit k stabilizes the dimer. Formation of one dimeric form of ATP synthase is inhibited in the absence of subunit. Detailed overview i Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
F1FO-ATP synthase
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
 assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function F1Fo-ATP synthase is a key enzyme of oxidative phosphorylation that is localized in the inner membrane of mitochondria. It uses the energy stored in the proton gradient across the inner mitochondrial membrane to catalyze the synthesis of ATP from ADP and phosphate Saccharomyces cerevisiae