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Literature summary for 6.3.4.2 extracted from

  • Yang, W.L.; Carman, G.M.
    Phosphorylation and regulation of CTP synthetase from Saccharomyces cerevisiae by protein kinase A (1996), J. Biol. Chem., 271, 28777-28783.
    View publication on PubMed

Inhibitors

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 [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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

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 and Products (Substrate)

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 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