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Literature summary for 2.7.7.41 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

General Stability Organism
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

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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