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Literature summary for 2.3.1.26 extracted from

  • Doolittle, G.M.; Chang, T.Y.
    Solubilization, partial purification, and reconstitution in phosphatidylcholine-cholesterol liposomes of acyl-CoA:cholesterol acyltransferase (1982), Biochemistry, 21, 674-679.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylethanolamine weak stimulatory effect on activity Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
phosphatidylinositol
-
Sus scrofa
phosphatidylserine
-
Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Sus scrofa
-
-

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial, using ammonium acetate fractionation and Sepharose 4B column chromatography Sus scrofa

Renatured (Commentary)

Renatured (Comment) Organism
solubilization of enzyme activity by deoxycholate, reconstitution of the solubilized activity into liposome of known cholesterol and phospholipid content by employing a cholate dialysis procedure Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00008
-
solubilized enzyme Sus scrofa
0.015
-
partially purified enzyme Sus scrofa

Storage Stability

Storage Stability Organism
4°C, Tris buffer, 1 mM EDTA, pH 7.7, 6.0 mg/ml protein, 5.0 mg/ml cholate, 5.5 mg/ml deoxycholate, 0.5 M potassium chloride, solubilized enzyme, stable for at least 18 h Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + cholesterol
-
Sus scrofa CoA + cholesterol ester
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Sus scrofa