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Literature summary for 7.2.2.1 extracted from

  • Kluge, C.; Dimroth, P.
    Studies on Na+ and H+ translocation through the F0 part of the Na+-translocating F1F0 ATPase from Propionibacterium modestum: discovery of a membrane potential dependent step (1992), Biochemistry, 31, 12665-12672.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N,N'-dicyclohexylcarbodiimide
-
Propionigenium modestum

Metals/Ions

Metals/Ions Comment Organism Structure
Na+ the enzyme has Na+-translocating activity Propionigenium modestum

Organism

Organism UniProt Comment Textmining
Propionigenium modestum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Propionigenium modestum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Propionigenium modestum ADP + phosphate
-
?
additional information Na+-translocation involves a minimum of four steps: 1. binding of Na+ from a defined surface of the membrane, translocation of the binary complex to the outer surface, 3. release of Na+, 4. return of the unloaded carrier to the original surface Propionigenium modestum ?
-
?

Synonyms

Synonyms Comment Organism
F1FO-ATPase
-
Propionigenium modestum