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

BRENDA support

Literature summary for 7.1.2.2 extracted from

  • Watanabe, R.; Okuno, D.; Sakakihara, S.; Shimabukuro, K.; Iino, R.; Yoshida, M.; Noji, H.
    Mechanical modulation of catalytic power on F1-ATPase (2012), Nat. Chem. Biol., 8, 86-92.
    View publication on PubMed
Search for more literature for 7.1.2.2

Inhibitors

Inhibitors Comment Organism Structure
ADP F1 strongly binds ADP lapsing into ADP inhibition, which pauses the rotation Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information molecular basis of positive cooperativity among three catalytic sites, acceleration of the ATP docking process occurs via thermally agitated conformational fluctuations, overview. Rate constants of ATP binding and hydrolysis are determined as functions of the rotary angle 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
-
 ?
ATP + H2O + H+/in Bacillus sp. (in: Bacteria) PS3
-
 ADP + phosphate + H+/out
-
 ?

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
-
 ?
ATP + H2O + H+/in the rate enhancement induced by ATP binding upon rotation is greater than that brought about by hydrolysis, suggesting that the ATP binding step contributes more to torque generation than does the hydrolysis step Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in the rate enhancement induced by ATP binding upon rotation is greater than that brought about by hydrolysis, suggesting that the ATP binding step contributes more to torque generation than does the hydrolysis step Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 ?
GTP + H2O + H+/in 3.3fold slower reaction compared to ATP hydrolysis Bacillus sp. (in: Bacteria) GDP + phosphate + H+/out
-
 ?
GTP + H2O + H+/in 3.3fold slower reaction compared to ATP hydrolysis Bacillus sp. (in: Bacteria) PS3 GDP + phosphate + H+/out
-
 ?
additional information angle dependence of ATP or GTP binding and of hydrolysis, overview. Modulation of the high reversibility of mechanochemical cou­pling, the kinetics and chemical equilibrium of the individual reaction steps comprising ATP hydrolysis on F1 inevitably in response to the gamma rotation Bacillus sp. (in: Bacteria) ?
-
 ?
additional information angle dependence of ATP or GTP binding and of hydrolysis, overview. Modulation of the high reversibility of mechanochemical cou­pling, the kinetics and chemical equilibrium of the individual reaction steps comprising ATP hydrolysis on F1 inevitably in response to the gamma rotation Bacillus sp. (in: Bacteria) PS3 ?
-
 ?

Synonyms

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