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Literature summary for 6.3.4.2 extracted from

  • Park, T.S.; O'Brien, D.J.; Carman, G.M.
    Phosphorylation of CTP synthetase on Ser36, Ser330, Ser354, and Ser454 regulates the levels of CTP and phosphatidylcholine synthesis in Saccharomyces cerevisiae (2003), J. Biol. Chem., 278, 20785-20794.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in a ura7ura8 double mutant that lacks CTP synthetase activity Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
S330A CTP synthetase activity in cells bearing the mutant enzyme is elevated, mutation causes an elevation in the Vmax of the reaction. Mutation does not have a major effect on the oligomerization of CTP synthetase Saccharomyces cerevisiae
S354A CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme, decrease in Vmax of the reaction. The amount of inactive dimeric enzyme form is 98% greater compared to wild-type enzyme Saccharomyces cerevisiae
S36A CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme, decrease in Vmax of the reaction. The amount of inactive dimeric enzyme form is 54% greater compared to wild-type enzyme Saccharomyces cerevisiae
S454A CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme. Mutation does not have a major effect on the oligomerization of CTP synthetase Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
CTP IC50: 0.3 mM Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
UTP pH 8.0, mutant enzyme S354A, kinetic constant determined with 0.5 mM ATP Saccharomyces cerevisiae
0.1
-
UTP pH 8.0, mutant enzyme S330A, kinetic constant determined with 0.5 mM ATP Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the enzyme is phosphorylated and stimulated by protein kinase C. Phosphorylation of CTP synthetase on Ser36, Ser330, Ser354, and Ser454 regulates the levels of CTP and phosphatidylcholine synthesis Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes S63A, S330A, S254A and S454A Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.2
-
mutant enzyme S354A Saccharomyces cerevisiae
0.3
-
mutant enzyme S36A Saccharomyces cerevisiae
0.6
-
mutant enzyme S454A Saccharomyces cerevisiae
0.66
-
wild-type enzyme Saccharomyces cerevisiae
0.83
-
mutant enzyme S330A Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
-80°C, stable for at least 6 months Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + NH4+
-
Saccharomyces cerevisiae ADP + phosphate + CTP
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
wild-type and mutant enzymes S36A, S330A, S354A and S454A Saccharomyces cerevisiae

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.3
-
IC50: 0.3 mM Saccharomyces cerevisiae CTP