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Literature summary for 7.1.2.2 extracted from

  • Bulygin, V.V.; Milgrom, Y.M.
    Probes of inhibition of Escherichia coli F1-ATPase by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole in the presence of MgADP and MgATP support a bi-site mechanism of ATP hydrolysis by the enzyme (2010), Biochemistry (Moscow), 75, 327-335.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
betaY331W the F1 beta subunit mutant shows higher sensitivity to Mg2+ increasing the inhibitory potency of 7-chloro-4-nitrobenz-2-oxa-1,3-diazole Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
7-chloro-4-nitrobenz-2-oxa-1,3-diazole i.e. NBD-Cl, MgADP at low concentrations promotes the inhibition, whereas at higher concentrations EcF1 is protected from inhibition, that need to be higher for the mutant betaY331W, than for the wild-type enzyme. In absence of added MgATP, selenite slows down inhibition of EcF1 by 0.2 mM NBD-Cl Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.053
-
 ATP pH 8.0, 37°C, MgATPase activity of EcF1, in absence of selenite Escherichia coli
0.073
-
 ATP pH 8.0, 37°C, MgATPase activity of EcF1, in presence of selenite Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Selenite one of the activating anions, that stimulates MgATPase activity of EcF1, likely due to a decrease in a relative content of MgADP-inhibited EcF1 because activating anions accelerate reactivation of MgADP-inhibited enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + phosphate + H+/out Escherichia coli
-
 ATP + H2O + H+/in
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] substrate modulation of multi-site activity of F1 is due to the substrate binding to the second catalytic site, bi-site catalytic mechanism, effects of Mg2+, overview Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphate + H+/out
-
 Escherichia coli ATP + H2O + H+/in
-
 ?

Synonyms

Synonyms Comment Organism
ECF1
-
 Escherichia coli
F1-ATPase
-
 Escherichia coli