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Different chain length specificities of peroxisomal and mitochondrial enoyl coenzyme a hydratases


Archives of Biochemistry & Biophysics 206(2): 342-345
Different chain length specificities of peroxisomal and mitochondrial enoyl coenzyme a hydratases
Peroxisomes and mitochondria were purified from rat liver by differential and equilibrium density centrifugation. Enoyl-CoA hydratase activity was assayed with 2 substrates: crotonyl-CoA (C4) and dodecenoyl-CoA (C12). The chain length specificity of the hydratase(s) in the 2 organelles differed strikingly: the ratio of activity on the C4 substrate/C12 substrate was 8-10 for the peak mitochondrial fraction and about 2 for the peak peroxisomal fraction. The subcellular distribution of the hydratase activity also depended on chain length. Peroxisomes contain 30-50% of the dodecenoyl-CoA hydratase activity but only 9-15% of the crotonase activity of rat liver.


Accession: 005151973



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