Literature summary for 6.2.1.7 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.

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Activating Compound

Activating Compound	Comment	Organism	Structure
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

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

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-

Storage Stability

Storage Stability	Organism
unstable at 4°C. PMSF, 0.1 M, can counteract the inactivation of the enzyme	Rattus norvegicus
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)

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

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Release 2023.1 (January 2023)