Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.1.2.2 extracted from

  • Feldkamp, T.; Kribben, A.; Weinberg, J.M.
    F1FO-ATPase activity and ATP dependence of mitochondrial energization in proximal tubules after hypoxia/reoxygenation (2005), J. Am. Soc. Nephrol., 16, 1742-1751.
    View publication on PubMed

Application

Application Comment Organism
medicine ATP hydrolysis by F1FO-ATPase is well preserved after hypoxia/reoxygenation as long as Mg2+ is available, indicating that function of the enzyme is largely intact, but ATP hydrolysis by F1FO-ATPase does not restore mitochondrial membrane potential as much as expected from the rate of ATP utilization, it is likely that uncoupling plays a major role in the mitochondrial dysfunction in proximal tubules during hypoxia/reoxygenation Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
oligomycin inhibits ATP hydrolysis Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Oryctolagus cuniculus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ restores most oligomycin-sensitive ATPase activity after hypoxia/reoxygenation Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Oryctolagus cuniculus
-
proximal tubule
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
Oryctolagus cuniculus ADP + phosphate + H+/out
-
?

Synonyms

Synonyms Comment Organism
F1FO-ATPase
-
Oryctolagus cuniculus