Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | competitive inhibitor versus CoA when acetyl phosphate is at subsaturating levels but it does not inhibit versus CoA when acetyl phosphate is at saturating levels. Acetyl-CoA is a competitive inhibitor versus acetyl phosphate when CoA is at subsaturating levels but it does not inhibit versus acetyl phosphate when CoA is at saturating levels | Methanosarcina thermophila | |
desulfo-CoA | competitive inhibitor with respect to CoA, noncompetitive inhibitor with respect to acetyl phosphate | Methanosarcina thermophila | |
phosphate | competitive inhibitor versus acetyl phosphate when CoA is at saturating or subsaturating levels. Phosphate is a noncompetitive inhibitor versus CoA when acetyl phosphate is at a subsaturating level (0.15 mM), but it does not inhibit versus CoA when acetyl phosphate is at a saturating level (4 mM) | Methanosarcina thermophila |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.065 | - |
CoA | 25°C, pH 7.2 | Methanosarcina thermophila | |
0.096 | - |
acetyl phosphate | 25°C, pH 7.2 | Methanosarcina thermophila | |
0.186 | - |
acetyl phosphate | 25°C, pH 7.2 | Methanosarcina thermophila | |
0.742 | - |
phosphate | 25°C, pH 7.2 | Methanosarcina thermophila |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
71000 | - |
dynamic light scattering | Methanosarcina thermophila |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanosarcina thermophila | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl-CoA + phosphate = CoA + acetyl phosphate | ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order | Methanosarcina thermophila |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-phosphate + CoA | ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order | Methanosarcina thermophila | acetyl-CoA + phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | dynamic light scattering | Methanosarcina thermophila |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1500 | - |
phosphate | 25°C, pH 7.2 | Methanosarcina thermophila | |
1500 | - |
acetyl phosphate | 25°C, pH 7.2 | Methanosarcina thermophila | |
5190 | - |
CoA | 25°C, pH 7.2 | Methanosarcina thermophila | |
5190 | - |
acetyl phosphate | 25°C, pH 7.2 | Methanosarcina thermophila |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0013 | - |
desulfo-CoA | 25°C, pH 7.2, with respect to CoA | Methanosarcina thermophila | |
0.0028 | - |
desulfo-CoA | 25°C, pH 7.2, with respect to acetyl phosphate | Methanosarcina thermophila |