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Literature summary for 7.1.2.2 extracted from

  • Tang, C.; Capaldi, R.A.
    Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase (1996), J. Biol. Chem., 271, 3018-3024.
    View publication on PubMed
Search for more literature for 7.1.2.2

Protein Variants

Protein Variants Comment Organism
M138C modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit Escherichia coli
additional information modification of the Cys at position 10 with NEM or fluorescein maleimide further reduces the binding affinity of, and the maximal inhibition by, the epsilon subunit Escherichia coli
S10C modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit Escherichia coli
S65C modification of epsilon-subunit, increases inhibition of ECF1 by the epsilon subunit Escherichia coli

General Stability

General Stability Organism
F1 part of the enzyme EC 3.6.3.14 treated with trypsin at pH 7.0 still binds purified epsilon subunit, while enzyme treated with the protease at pH 8.0 does not Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NEM modification of the Cys at position 10 with NEM or fluorescein maleimide further reduces the binding affinity of, and the maximal inhibition by the epsilon subunit Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Escherichia coli ADP + phosphate + H+/out
-
 ?
additional information sites around residues 70 and/or between 202 and 212 of the gamma subunit are involved in epsilon subunit binding Escherichia coli ?
-
 ?