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Literature summary for 7.1.2.2 extracted from

  • Grover, G.J.; Marone, P.A.; Koetzner, L.; Seto-Young, D.
    Energetic signalling in the control of mitochondrial F1F0 ATP synthase activity in health and disease (2008), Int. J. Biochem. Cell Biol., 40, 2698-2701.
    View publication on PubMed
Search for more literature for 7.1.2.2

Inhibitors

Inhibitors Comment Organism Structure
aurovertin B non-selective ATPase inhibitor Rattus norvegicus
BMS-199264 a benzopyran analogue, selectively inhibits F1F0 ATP hydrolase activity with no effect on ATP synthase activity, BMS-199264 has no effect on ATP before ischemia, but reduces the decline in ATP during ischemia Rattus norvegicus
IF1 protein the hydrolytic activity of the mitochondrial F1F0 ATP hydrolase, but not the synthase, is naturally inhibited by an 84 residue, heat-stable protein IF-1, which binds to F1F0 ATP hyrolase at the F1 domain with a 1:1 stoichiometry. In the absence of a proton motive force, IF-1 is a reversible, non-competitive inhibitor of ATPase hydrolase activity and is optimally functional at a pH below 7.0. The mechanism of IF-1 inhibition is via trapping of adenine nucleotides within the catalytic sites of F1 Rattus norvegicus
oligomycin non-selective ATPase inhibitor Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
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 Rattus norvegicus 16020
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mitochondrion
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 Rattus norvegicus 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Rattus norvegicus the mitochondrial F1F0 ATP synthase mitochondrial F1F0 ATP synthase is also an ATP hydrolase under ischemic conditions, and is a critical enzyme that works by coupling the proton motive force generated by the electron transport chain via proton transfer through the F0 or proton-pore forming domain of this enzyme to release ATP from the catalyticF1 domain. The enzyme is regulated by calcium, ADP, and inorganic phosphate as well as increased transcription through several pathways. Role of the F1F0 ATPase during myocardial ischemia and reperfusion, overview ADP + phosphate + H+/out
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
heart healthy and ischemic Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in the mitochondrial F1F0 ATP synthase mitochondrial F1F0 ATP synthase is also an ATP hydrolase under ischemic conditions, and is a critical enzyme that works by coupling the proton motive force generated by the electron transport chain via proton transfer through the F0 or proton-pore forming domain of this enzyme to release ATP from the catalyticF1 domain. The enzyme is regulated by calcium, ADP, and inorganic phosphate as well as increased transcription through several pathways. Role of the F1F0 ATPase during myocardial ischemia and reperfusion, overview Rattus norvegicus ADP + phosphate + H+/out
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 ?
ATP + H2O + H+/in the mitochondrial F1F0 ATP synthase is also an ATP hydrolase under ischemic conditions. A a conformational change in the F1F0 ATPase enzyme occurs when switching from synthase to hydrolase activity Rattus norvegicus ADP + phosphate + H+/out
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 ?

Synonyms

Synonyms Comment Organism
mitochondrial F1F0 ATP hydrolase
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 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
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 Rattus norvegicus