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

BRENDA support

Literature summary for 7.1.2.2 extracted from

  • Langemeyer, L.; Engelbrecht, S.
    Essential arginine in subunit a and aspartate in subunit c of FoF1 ATP synthase. Effect of repositioning within helix 4 of subunit a and helix 2 of subunit c (2007), Biochim. Biophys. Acta, 1767, 998-1005.
    View publication on PubMed
Search for more literature for 7.1.2.2

Activating Compound

Activating Compound Comment Organism Structure
Lauryldimethylamine oxide LDAO, stimulates F1-ATPase Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes complex in strain DK8 Escherichia coli

Protein Variants

Protein Variants Comment Organism
aR210A/aN214R site-directed mutagenesis, the subunit a mutant supports proton conduction onyl through EF1-depleted EFo, but not in EfoEF1, nor ATP-driven proton pumping Escherichia coli
cD61N/cM65D site-directed mutagenesis, the subunit c mutant grows on succinate, retains the ability to synthesize ATP, and supports passive proton conduction, but not ATP hydrolysis-driven proton pumping, overview Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Dicyclohexylcarbodiimide DCCD Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Escherichia coli the enzyme complex can pump protons in the reverse direction driven by ATP hydrolysis generating a ion-motive force, the F1 domain, comprising subunits alpha3beta3gammadeltaepsilon and possessing the nucleotide binding site, is responsible for the ATP hydrolysis upon detachment from the Fo domain ADP + phosphate + H+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Escherichia coli ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in the enzyme complex can pump protons in the reverse direction driven by ATP hydrolysis generating a ion-motive force, the F1 domain, comprising subunits alpha3beta3gammadeltaepsilon and possessing the nucleotide binding site, is responsible for the ATP hydrolysis upon detachment from the Fo domain Escherichia coli ADP + phosphate + H+/out
-
 ?

Synonyms

Synonyms Comment Organism
F1-ATPase
-
 Escherichia coli
FoF1 ATP synthase
-
 Escherichia coli