Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.1.2.3 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
Search for more literature for 5.1.2.3

Localization

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(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

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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