Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CTP | IC50 for the native enzyme: 0.12 in presence of 0.5 mM ATP, 0.22 mM in presence of 1 mM ATP. IC50 for the phosphorylated enzyme: 0.21 mM in presence of 0.5 mM ATP, 0.31 mM in presence of 1 mM ATP | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.04 | - |
UTP | pH 8.0, 30°C, phosphorylated enzyme, in presence of 2 mM ATP | Saccharomyces cerevisiae | |
0.05 | - |
UTP | pH 8.0, 30°C, native enzyme, in presence of 2 mM ATP | Saccharomyces cerevisiae | |
0.08 | - |
UTP | pH 8.0, 30°C, native enzyme or phosphorylated enzyme, in presence of 0.5 mM ATP | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylation of CTP synthetase by protein kinase A results in the stimulation of CTP synthetase activity. The mechanism of stimulation involves an increase in Vmax of the reaction and an increase of the enzyme affinity for ATP | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + UTP + glutamine | - |
Saccharomyces cerevisiae | ADP + phosphate + CTP + Glu | - |
? | |
ATP + UTP + NH4+ | - |
Saccharomyces cerevisiae | ADP + phosphate + CTP | - |
? |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.21 | - |
IC50 for the native enzyme: 0.12 in presence of 0.5 mM ATP, 0.22 mM in presence of 1 mM ATP. IC50 for the phosphorylated enzyme: 0.21 mM in presence of 0.5 mM ATP, 0.31 mM in presence of 1 mM ATP | Saccharomyces cerevisiae | CTP |