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Literature summary extracted from

  • Feniouk, B.A.; Suzuki, T.; Yoshida, M.
    The role of subunit epsilon in the catalysis and regulation of FoF1-ATP synthase (2006), Biochim. Biophys. Acta, 1757, 326-338.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.1.2.2 additional information subunit F might be involved in intramolecular regulation of ATPase activity Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
7.1.2.2 additional information deletion of 8-20 amino acid residues from the N-terminus of subunit gamma leads to decreased inhibitory effect of subunit epsilon, subunit gamma adopts a different conformation in a mutant lacking subunit epsilon and showing loss of activity, mutation of the acidic residues in the betaDELSEED motif to alanines leads to highly decreased inhibitory activity of subunit epsilon on ATPase activity, while exchange of DELSEED to DCLSEED increases ATPase activity, overview Escherichia coli
7.1.2.2 additional information subunit beta adopts a different conformation during ATP synthesis in a mutant lacking the C-terminal domain of subunit epsilon, mutation of subunit epsilon C-terminal alpha-helix residues DELSDED leads to highly decreased inhibitory activity of subunit epsilon on ATPase activity, overview Bacillus sp. (in: Bacteria)

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.2.2 ADP
-
 Bacillus sp. (in: Bacteria)
7.1.2.2 ADP
-
 Escherichia coli
7.1.2.2 additional information subunit F might be involved in intramolecular regulation of ATPase activity Thermus thermophilus
7.1.2.2 peptide IF1 the inhibitory effect might be mediated through interaction of IF1 with the betaDELSEED sequence of the F1 domain of the mitochondrial enzyme, the alpha-helical IF1 N-terminus can penetrate into the alpha3beta3-hexamer between alpha and beta subunits, overview Bos taurus
7.1.2.2 subunit epsilon subunit epsilon is required for inhibitory activity on F1 ATPase activity, mechanism, subunit epsilon can extend its C-terminus further inside the alpha3beta3-hexamer up to the N-terminus of subunit gamma, which has an anisotropic effect and enhances ATP hydrolysis inhibition to about 80% without affecting ATP synthesis, the C-terminal alpha-helix residues DELSDED are involved in inhibition, overview Bacillus sp. (in: Bacteria)
7.1.2.2 subunit epsilon subunit epsilon is required for inhibitory activity on F1 ATPase activity, the C-terminal alpha-helix residues DELSEED are involved in inhibition, mechanism, overview Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.2.2 membrane
-
 Escherichia coli 16020
-
7.1.2.2 membrane
-
 Bacillus sp. (in: Bacteria) 16020
-
7.1.2.2 mitochondrion
-
 Bos taurus 5739
-

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 Bos taurus
-
 ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in Escherichia coli FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in Bacillus sp. (in: Bacteria) FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in Thermus thermophilus subunit F might be involved in intramolecular regulation of ATPase activity ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in Bacillus sp. (in: Bacteria) PS3 FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview ADP + phosphate + H+/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.2.2 Bacillus sp. (in: Bacteria)
-
-
-
7.1.2.2 Bacillus sp. (in: Bacteria) PS3
-
-
-
7.1.2.2 Bos taurus
-
-
-
7.1.2.2 Escherichia coli
-
-
-
7.1.2.2 Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.2.2 ATP + H2O + H+/in
-
 Thermus thermophilus ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in
-
 Bos taurus ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview Escherichia coli ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in subunit F might be involved in intramolecular regulation of ATPase activity Thermus thermophilus ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in subunit epsilon plays a role in intra-enzymatic energy transfer and is required for coupling of ATP synthesis and hydrolysis to proton pumping, the isolated F1 domain shows reduced ATPase activity compared to the complete enzyme complex F1Fo-ATP synthase involving intramolecular inhibition by the C-terminal subunit epsilon, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview Escherichia coli ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in subunit epsilon plays a role in intra-enzymatic energy transfer and is required for coupling of ATP synthesis and hydrolysis to proton pumping, the isolated F1 domain shows reduced ATPase activity compared to the complete enzyme complex F1Fo-ATP synthase involving intramolecular inhibition by the C-terminal subunit epsilon, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 ?
7.1.2.2 ATP + H2O + H+/in subunit epsilon plays a role in intra-enzymatic energy transfer and is required for coupling of ATP synthesis and hydrolysis to proton pumping, the isolated F1 domain shows reduced ATPase activity compared to the complete enzyme complex F1Fo-ATP synthase involving intramolecular inhibition by the C-terminal subunit epsilon, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.2.2 More structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the N-terminal beta-sandwich of the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview Escherichia coli
7.1.2.2 More structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview Bacillus sp. (in: Bacteria)

Synonyms

EC Number Synonyms Comment Organism
7.1.2.2 ATPase
-
 Escherichia coli
7.1.2.2 ATPase
-
 Bos taurus
7.1.2.2 ATPase
-
 Bacillus sp. (in: Bacteria)
7.1.2.2 FoF1-ATP synthase
-
 Escherichia coli
7.1.2.2 FoF1-ATP synthase
-
 Bos taurus
7.1.2.2 FoF1-ATP synthase
-
 Bacillus sp. (in: Bacteria)
7.1.2.2 V-type ATPase/synthase
-
 Thermus thermophilus
7.1.2.2 V-type H+-ATPase
-
 Thermus thermophilus