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.
Chromatography of a rat liver extract on DEAE-cellulose resulted in the near total loss of 3-hydroxyacyl-CoA epimerase activity. The activity was regained either when fractions were recombined or when purified crotonase was added to the early column fractions. A new enoyl-CoA hydratase present in these early fractions catalyzes the conversion of D-3-hydroxyacyl-CoA to 2-trans-enoyl-CoA which can be hydrated by crotonase or the peroxisomal bifunctional enzyme to L-3-hydroxyacyl-CoA. Thus, the 3-hydroxyacyl-CoA epimerase activity is due to the combined actions of two enoyl-CoA hydratases with opposite stereospecificities.
Smeland
T E
TE
Department of Chemistry, City College of the City University of New York, New York 10031.
Li
J X
JX
Chu
C H
CH
Cuebas
D
D
Schulz
H
H
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D004746:Enoyl-CoA Hydratase / Q000378:metabolism*; D005231:Fatty Acids, Unsaturated / Q000378:metabolism*; D006836:Hydro-Lyases / Q000378:metabolism*; D007535:Isomerases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008830:Microbodies / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology; D010084:Oxidation-Reduction; D019998:Racemases and Epimerases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D005231:Fatty Acids, Unsaturated; D006836:Hydro-Lyases; D004746:Enoyl-CoA Hydratase; D007535:Isomerases; D019998:Racemases and Epimerases; C029601:3-hydroxybutyryl-CoA epimerase