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Literature summary for 7.1.2.2 extracted from

  • Shah, N.B.; Hutcheon, M.L.; Haarer, B.K.; Duncan, T.M.
    F1-ATPase of Escherichia coli: the epsilon-inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands (2013), J. Biol. Chem., 288, 9383-9395.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 strain T7 Express lysY Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
Escherichia coli
azide
-
Escherichia coli
additional information the enzyme is autoinhibited by the subunit epsilon C-terminal domain. Nucleotide hydrolysis is required to form the epsilon-inhibited state 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Talon resin column chromatography and Sephacryl S100 gel filtration 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