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Literature summary extracted from

  • Van Veldhoven, P.P.; Asselberghs, S.; Eyssen, H.J.; Mannaerts, G.P.
    Stabilisation and partial purification of Triton X-100 solubilised trihydroxycoprostanoyl-CoA synthetase from rat liver (1996), Biochem. Mol. Biol. Int., 40, 447-457.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.2.1.7 Phospholipid addition of phospholipids is necessary to restore the activity of the delipidated enzyme stabilized by high concentrations of glucose and sucrose Rattus norvegicus

General Stability

EC Number General Stability Organism
6.2.1.7 PMSF, 0.1 M, can counteract the inactivation of the enzyme at 4°C Rattus norvegicus
6.2.1.7 the lability of the delipidated enzyme can be suppressed by high concentrations of polyols such as sucrose and glucose Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.2.1.7 212000
-
 gel filtration Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.7 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.2.1.7 liver
-
 Rattus norvegicus
-

Storage Stability

EC Number Storage Stability Organism
6.2.1.7 unstable at 4°C. PMSF, 0.1 M, can counteract the inactivation of the enzyme Rattus norvegicus
6.2.1.7 when glucose and Triton H-666 are added together to lipid-poor Triton X-100 solubilized preparations, enzyme activity remains stable for at least 3 months at -20°C or for 2 days at 4°C Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.7 ATP + cholate + CoA
-
 Rattus norvegicus AMP + diphosphate + choloyl-CoA
-
 ?