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Literature summary extracted from

  • Belendiuk, G.; Mangnall, D.; Tung, B.; Westley, J.; Getz, G.S.
    CTP-phosphatidic acid cytidyltransferase from Saccharomyces cerevisiae. Partial purification, characterization, and kinetic behavior (1978), J. Biol. Chem., 253, 4555-4565.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.7.7.41 the solubilized protein is quite labile. Its stability is markedly enhanced by exchange dialysis against 10% glycerol, 20% propylene glycol, 25 mM cacodylate buffer, pH 6.5, 10 mM MgCl2 Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.41 dCTP 2.5 mM, 54% inhibition of purified enzyme; competitive with respect to CTP Saccharomyces cerevisiae
2.7.7.41 diphosphate 2.5 mM, 80% inhibition of purified enzyme, noncompetitive with respect to CTP and phosphatidic acid Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.41 mitochondrial membrane
-
 Saccharomyces cerevisiae 31966
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.41 400000
-
 approximately, gel filtration Saccharomyces cerevisiae

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.41 partial Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.41 0.45
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.41 CTP + phosphatidate
-
 Saccharomyces cerevisiae diphosphate + CDPdiacylglycerol
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.41 More two distinct protein bands of 45000 Da and 19000 Da are detected by SDS-PAGE, it is yet unclear whether this represents simple aggregation of two unrelated proteins in a monomer dimer relationship, or whether the enzyme has two distinct subunits present in a 1:4 molar ratio Saccharomyces cerevisiae