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

• Published in: Biochemical and biophysical research communications Vol. 160; no. 3; pp. 988 - 992
• Main Authors: Smeland, Tor E., Jianxun, Li, Chu, Chin-hung, Cuebas, Dean, Schulz, Horst
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 15.05.1989; Elsevier
• Subjects: 3-hydroxyacyl-CoA epimerase; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chromatography, DEAE-Cellulose; Chromatography, High Pressure Liquid; enoyl-CoA hydratase; Enoyl-CoA Hydratase - metabolism; Enzymes and enzyme inhibitors; Fatty Acids, Unsaturated - metabolism; Fundamental and applied biological sciences. Psychology; Hydro-Lyases - metabolism; Isomerases - metabolism; Liver - enzymology; Lyases; Microbodies - enzymology; Mitochondria, Liver - enzymology; Oxidation-Reduction; peroxisomes; Racemases and Epimerases - isolation & purification; Racemases and Epimerases - metabolism; Rats; Purification; Rat; Enzyme; Liver; Rodentia; HPLC chromatography; Metabolism; Ion exchange chromatography; Enoyl-CoA hydratase; Intermolecular interaction; Vertebrata; Mitochondria; Mammalia; Enzymatic activity; 3-Hydroxybutyryl-CoA epimerase; Peroxisome; Unsaturated fatty acid; Oxidation
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(89)80098-1

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.