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Literature summary for 7.1.2.2 extracted from

  • Watanabe, R.; Iino, R.; Noji, H.
    Phosphate release in F1-ATPase catalytic cycle follows ADP release (2010), Nat. Chem. Biol., 6, 814-820.
    View publication on PubMed
Search for more literature for 7.1.2.2

Protein Variants

Protein Variants Comment Organism
E190D reversibility of ATPgammaS hydrolysis and synthesis on F1(betaE190D) , overview Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics relevant to ATP and ATPgammaS hydrolysis and synthesis and phosphate or thiophosphate release and binding, overview Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Bacillus sp. (in: Bacteria)
-
 ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in Bacillus sp. (in: Bacteria) PS3
-
 ADP + phosphate + H+/out
-
 r

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) PS3
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in ATP hydrolysis is essentially reversible, implying that phosphate is released after the gamma rotation and ADP release, although extremely slow, phosphate release is found at the ATP hydrolysis angle as an uncoupling side reaction, affinity for phosphate is strongly angle dependent, selective ADP binding, overview. Models of phosphate release in chemomechanical coupling of F1 Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in ATP hydrolysis is essentially reversible, implying that phosphate is released after the gamma rotation and ADP release, although extremely slow, phosphate release is found at the ATP hydrolysis angle as an uncoupling side reaction, affinity for phosphate is strongly angle dependent, selective ADP binding, overview. Models of phosphate release in chemomechanical coupling of F1 Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 r
ATPgammaS + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) ADP + thiophosphate + H+/out
-
 r
ATPgammaS + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) PS3 ADP + thiophosphate + H+/out
-
 r

Synonyms

Synonyms Comment Organism
F1-ATPase
-
 Bacillus sp. (in: Bacteria)

General Information

General Information Comment Organism
physiological function F1-ATPase is an ATP-driven rotary motor protein in which the gamma-subunit rotates against the catalytic stator ring Bacillus sp. (in: Bacteria)