Protein Variants | Comment | Organism |
---|---|---|
E190D | reversibility of ATPgammaS hydrolysis and synthesis on F1(betaE190D) , overview | Bacillus sp. (in: Bacteria) |
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Bacillus sp. (in: Bacteria) |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus sp. (in: Bacteria) | - |
- |
- |
Bacillus sp. (in: Bacteria) PS3 | - |
- |
- |
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 | Comment | Organism |
---|---|---|
F1-ATPase | - |
Bacillus sp. (in: Bacteria) |
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) |