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Literature summary for 6.3.4.2 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
Search for more literature for 6.3.4.2

Inhibitors

Inhibitors Comment Organism Structure
CTP IC50: 0.32 mM Saccharomyces cerevisiae

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

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

pH Range

pH Minimum pH Maximum Comment Organism
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

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