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Literature summary extracted from

  • Smeland, T.E.; Li, J.; Chu, C.h.; Cuebas, D.; Schulz, H.
    The 3-hydroxyacyl-CoA epimerase activity of rat liver peroxisomes is due to the combined actions of two enoyl-CoA hydratases: a revision of the epimerase-dependent pathway of unsaturated fatty acid oxidation (1989), Biochem. Biophys. Res. Commun., 160, 988-992.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.1.2.3 peroxisome
-
 Rattus norvegicus 5777
-

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
5.1.2.3 (S)-3-Hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA epimerization of D-3-hydroxyacyl-CoA does not occur directly but proceeds instead via 2-trans-enoyl-CoA as an intermediate by combined actions of a novel D-specific enoyl-CoA hydratase, D-hydratase, and an L-specific enoyl-CoA hydratase Rattus norvegicus
a

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.2.3 D-3-hydroxyoctanoly-CoA
-
 Rattus norvegicus L-3-hydroxyoctanoyl-CoA
-
 ?