EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
7.1.2.2 | 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 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
7.1.2.2 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
7.1.2.2 | 0.053 | - |
ATP | pH 8.0, 37°C, MgATPase activity of EcF1, in absence of selenite | Escherichia coli | |
7.1.2.2 | 0.073 | - |
ATP | pH 8.0, 37°C, MgATPase activity of EcF1, in presence of selenite | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
7.1.2.2 | membrane | - |
Escherichia coli | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
7.1.2.2 | Mg2+ | required | Escherichia coli | |
7.1.2.2 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.1.2.2 | ADP + phosphate + H+/out | Escherichia coli | - |
ATP + H2O + H+/in | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.1.2.2 | Escherichia coli | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
7.1.2.2 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.1.2.2 | ADP + phosphate + H+/out | - |
Escherichia coli | ATP + H2O + H+/in | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
7.1.2.2 | ECF1 | - |
Escherichia coli |
7.1.2.2 | F1-ATPase | - |
Escherichia coli |