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Literature summary for 7.1.2.2 extracted from

  • Futai, M.; Kanazawa, H.
    Structure and function of proton-translocating adenosine triphosphatase (F0F1): Biochemical and molecular biological approaches (1983), Microbiol. Rev., 47, 285-312.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information mutation of the subunits alpha, beta, gamma and delta and epsilon, mutations of the F0 subunit Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
N,N'-dicyclohexylcarbodiimide
-
Bacillus sp. PS3
N,N'-dicyclohexylcarbodiimide
-
Bos taurus
N,N'-dicyclohexylcarbodiimide
-
Escherichia coli
N,N'-dicyclohexylcarbodiimide
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Bacillus sp. PS3
-
-
-
Bos taurus
-
-
-
Escherichia coli
-
-
-
Mus musculus
-
-
-
Saccharomyces cerevisiae
-
-
-
Spinacia oleracea
-
-
-
Zea mays
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] mechanism of proton conduction through F0, and the catalytic mechanism of F1 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
Mus musculus ADP + phosphate + H+/out
-
?
ATP + H2O + H+/in
-
Escherichia coli ADP + phosphate + H+/out
-
?
ATP + H2O + H+/in
-
Saccharomyces cerevisiae ADP + phosphate + H+/out
-
?
ATP + H2O + H+/in
-
Bos taurus ADP + phosphate + H+/out
-
?
ATP + H2O + H+/in
-
Spinacia oleracea ADP + phosphate + H+/out
-
?
ATP + H2O + H+/in
-
Zea mays ADP + phosphate + H+/out
-
?
ATP + H2O + H+/in
-
Bacillus sp. PS3 ADP + phosphate + H+/out
-
?

Subunits

Subunits Comment Organism
?
-
Escherichia coli
?
-
Bos taurus
?
-
Spinacia oleracea
More
-
Saccharomyces cerevisiae
More
-
Bos taurus
More x * F1alpha, 55259 + x * F1beta, 50117, + x * F1gamma, 19303, + x * F1epsilon, 14914, + x * F0a, 30275, + x * F0b, 17244, + x * F0c, 8246 Escherichia coli