Literature summary for 7.1.2.2 extracted from

Sielaff, H.; Duncan, T.M.; Boersch, M.
The regulatory subunit epsilon in Escherichia coli F0F1-ATP synthase (2018), Biochim. Biophys. Acta, 1859, 775-788 .

Search for more literature for 7.1.2.2

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
plasma membrane	-	Escherichia coli	5886	-

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	-	ATP + H2O + 4 H+[side 1]	-	r
ATP + H2O + 4 H+[side 1]	Escherichia coli	-	ADP + phosphate + 4 H+[side 2]	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6E6	epsilon subunit	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + phosphate + 4 H+[side 2]	-	Escherichia coli	ATP + H2O + 4 H+[side 1]	-	r
ATP + H2O + 4 H+[side 1]	-	Escherichia coli	ADP + phosphate + 4 H+[side 2]	-	r

Synonyms

Synonyms	Comment	Organism
FoF1-ATP synthase	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	the enzyme uses the proton motive force across the bacterial plasma membrane to drive rotation of the central rotor subunits within a stator subunit complex. Through this mechanical rotation, the rotor coordinates three nucleotide binding sites that sequentially catalyze the synthesis of ATP. Moreover, the enzyme can hydrolyze ATP to turn the rotor in the opposite direction and generate proton motive force	Escherichia coli

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Release 2023.1 (January 2023)