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Literature summary extracted from

  • Kelley, M.; Vessey, D.A.
    Dual role of divalent cations in the bile acid:CoA ligase catalyzed reaction (1994), Biochim. Biophys. Acta, 1209, 51-55.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.2.1.7 EDTA
-
 Cavia porcellus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.2.1.7 microsome
-
 Cavia porcellus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.7 Mg2+ complex of Mg2+ with ATP is the form of ATP that is substrate for the enzyme, in addition a secondary site of the enzyme binds Mg2+ with relatively low affinity, which results in a rate enhancement, Mn2+ is more effective than Mg2+ Cavia porcellus
6.2.1.7 Mn2+ a complex of Mn2+ with ATP is the form of ATP that is substrate for the enzyme, in addition a secondary site of the enzyme binds Mn2+ with relatively low affinity, which results in a rate enhancement, Mn2+ is more effective than Mg2+ Cavia porcellus

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.7 Cavia porcellus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.2.1.7 liver
-
 Cavia porcellus
-

Substrates and Products (Substrate)

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