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Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.2.2 ADP
-
 Escherichia coli
7.1.2.2 azide
-
 Escherichia coli
7.1.2.2 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)

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

Organism

EC Number Organism UniProt Comment Textmining
7.1.2.2 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.2.2 Talon resin column chromatography and Sephacryl S100 gel filtration Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
7.1.2.2 F1-ATPase
-
 Escherichia coli