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Literature summary for 7.1.2.2 extracted from

  • Shu, Y.G.; Lai, P.Y.
    Systematic kinetics study of FoF1-ATPase: analytic results and comparison with experiments (2008), J. Phys. Chem. B, 112, 13453-13459.
    View publication on PubMed
Search for more literature for 7.1.2.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state Michaelis-Menten kinetics, investigation of the systematic kinetics of the holoenzyme FoF1-ATPase by a tri-site filled, random binding order, and stochastic mechanochemical tight coupling model, reaction dynamics, detailed overview Spinacia oleracea
additional information
-
 additional information steady-state Michaelis-Menten kinetics, investigation of the systematic kinetics of the holoenzyme FoF1-ATPase by a tri-site filled, random binding order, and stochastic mechanochemical tight coupling model, reaction dynamics, detailed overview Rhodobacter capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Spinacia oleracea 9507
-
chromatophore
-
 Rhodobacter capsulatus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the motor requires a free magnesium ion as an indispensable cofactor to bring into service Spinacia oleracea
Mg2+ the motor requires a free magnesium ion as an indispensable cofactor to bring into service Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Spinacia oleracea
-
 ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in Rhodobacter capsulatus
-
 ADP + phosphate + H+/out
-
 r

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-
Spinacia oleracea
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Spinacia oleracea
-
leaf
-
 Rhodobacter capsulatus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Spinacia oleracea ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in
-
 Rhodobacter capsulatus ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in the binding of ATP and ADP/phosphate on an open site is competitive while that of ADP and phosphate is random. The chemical reaction of ATP hydrolysis takes place in the tight to loose, and vice versa, conformational changing, and is tightly coupled with transmembrane proton transport in Fo by the rotation of rotor. ATP can be reversibly synthesized and hydrolyzed in FoF1-ATPase, reversible reaction pathways of the enzyme F1, overview Spinacia oleracea ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in the binding of ATP and ADP/phosphate on an open site is competitive while that of ADP and phosphate is random. The chemical reaction of ATP hydrolysis takes place in the tight to loose, and vice versa, conformational changing, and is tightly coupled with transmembrane proton transport in Fo by the rotation of rotor. ATP can be reversibly synthesized and hydrolyzed in FoF1-ATPase, reversible reaction pathways of the enzyme F1, overview Rhodobacter capsulatus ADP + phosphate + H+/out
-
 r

Synonyms

Synonyms Comment Organism
FoF1-ATPase
-
 Spinacia oleracea
FoF1-ATPase
-
 Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Spinacia oleracea
ATP
-
 Rhodobacter capsulatus