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Literature summary for 7.1.2.2 extracted from

  • Vahidi, S.; Bi, Y.; Dunn, S.D.; Konermann, L.
    Load-dependent destabilization of the gamma-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry (2016), Proc. Natl. Acad. Sci. USA, 113, 2412-2417 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + phosphate + 4 H+[side 2] Escherichia coli the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis ATP + H2O + 4 H+[side 1]
-
r
ATP + H2O + 4 H+[side 1] Escherichia coli the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis ADP + phosphate + 4 H+[side 2]
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphate + 4 H+[side 2] the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis Escherichia coli ATP + H2O + 4 H+[side 1]
-
r
ATP + H2O + 4 H+[side 1] the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis Escherichia coli ADP + phosphate + 4 H+[side 2]
-
r

Synonyms

Synonyms Comment Organism
FoF1
-
Escherichia coli
FoF1 ATP synthase
-
Escherichia coli