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Literature summary for 7.1.2.2 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
Search for more literature for 7.1.2.2

Activating Compound

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

Protein Variants

Protein Variants Comment Organism
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
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

Inhibitors Comment Organism Structure
ADP
-
 Bacillus sp. (in: Bacteria)
ADP
-
 Escherichia coli
additional information subunit F might be involved in intramolecular regulation of ATPase activity Thermus thermophilus
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
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)
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Bos taurus
-
 ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in Escherichia coli FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview ADP + phosphate + H+/out
-
 ?
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
-
 ?
ATP + H2O + H+/in Thermus thermophilus subunit F might be involved in intramolecular regulation of ATPase activity ADP + phosphate + H+/out
-
 ?
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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Thermus thermophilus ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in
-
 Bos taurus ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview Escherichia coli ADP + phosphate + H+/out
-
 ?
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
-
 ?
ATP + H2O + H+/in subunit F might be involved in intramolecular regulation of ATPase activity Thermus thermophilus ADP + phosphate + H+/out
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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

Subunits Comment Organism
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
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

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