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Literature summary extracted from

  • Pappas, A.; Park, T.S.; Carman, G.M.
    Characterization of a novel dUTP-dependent activity of CTP synthetase from Saccharomyces cerevisiae (1999), Biochemistry, 38, 16671-16677.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.4.2 CTP IC50: 0.32 mM Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.2 Mg2+ dUTP-dependent activity is dependent on Mg2+, maximal activity at 4 mM Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.2 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.2
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.4.2 1.3
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
6.3.4.2 tetramer UTP and ATP are responsible for the tetramerization and activation of the inactive dimeric form of the enzyme. UTP is absolutely required for the tatramerization of the enzyme when ATP is present at a saturating concentration Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.2 8
-
dUTP-dependent activity Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
6.3.4.2 7.5 9 pH 7.5: about 70% of maximal activity, pH 9.0: about 55% of maximal activity, dUTP-dependent activity Saccharomyces cerevisiae

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
6.3.4.2 0.32
-
IC50: 0.32 mM Saccharomyces cerevisiae CTP