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Studies on the substrate specificity of the inducible and non-inducible acyl-CoA oxidases from rat kidney peroxisomes

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  • Biology
  • Chemistry


J. Biochem. 113, 577-582 (1993) Studies on the Substrate Specificity of the Inducible and Non-Inducible Acyl-CoA Oxidases from Rat Kidney Peroxisomes 1 Ronaid J.A. Wanders, *.2 Simone W. Denis,* and Georges Dacremont** •Department of Clinical Biochemistry, University Hospital Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands; and ••Department of Pediatrics, State University Ghent, B-~OOO Ghent, Belgium Received for publication, October 19, 1992 We have studied the substrate specificity of the inducible (acyl-CoA oxidase I) and non-inducible (acyl-CoAoxidase II) oxidases in peroxisome-enriched fractions from rat kidney. The two oxidases were separated by means of ion-exchange chromatography and shown 10 accept a variety of acyl-CoA esters as substrates, including lignoceroyl-CoA, palmi1oyl-CoA, lauroyl-CoA, caproyl-CoA, and trimethyltridecanoyl-CoA. Glutaryl-CoA was found 10 react exclusively with the inducible enzyme, and pristanoyl-CoA exclusively with the non-inducible enzyme. We conclude that under normal non-induced conditions both acyl-CoA oxidase I and II contribute to the oxidation of the various acyl-CoA esters with the exception of pristanoyl-CoA and glutaryl-CoA, although the extent 10 which each enzyme contributes to the oxidation was found 10 differ between the various acyl-CoA esters. Mitochondria were long believed to be the sole site of fatty acid j3 -oxidation. Following the finding of Lazarow and de Duve (1) that rat liver peroxisomes are also capable of fatty acid j3-oxidation, it has been established that non-mito- chondrial fatty acid j3 -oxidation is much more widely distributed in nature than j3-oxidation in mitochondria, which is mainly restricted to the animal kingdom. Although the significance of a second j3 -oxidation system in peroxisomes was initially obscure, it is now clear that peroxisomes catalyze the j3-oxidative chain-shortening of a distinct set of fatty acids and fatty acid derivatives (2). Indeed, peroxisomes are obligatory for the ox

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