Literature summary for 7.1.2.2 extracted from

Martin, J.; Hudson, J.; Hornung, T.; Frasch, W.D.
Fo-driven rotation in the ATP synthase direction against the force of F1 ATPase in the FoF1 ATP synthase (2015), J. Biol. Chem., 290, 10717-10728.

Search for more literature for 7.1.2.2

Protein Variants

Protein Variants	Comment	Organism
E196L	the mutation decreases ATP synthase activity 15fold	Escherichia coli
E196Q	the mutation decreases ATP synthase activity 4.7fold	Escherichia coli
R50L	the mutation decreases ATP synthase activity 11fold	Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
F1-ATPase	-	Escherichia coli
FoF1 ATP synthase	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)