We have studied the substrate specificity of the inducible (acyl-CoA oxidase I) and non-inducible (acyl-CoA oxidase II) oxidases in peroxisome-enriched fractions from rat kidney. The two oxidases were separated by means of ion-exchange chromatography and shown to accept a variety of acyl-CoA esters as substrates, including lignoceroyl-CoA, palmitoyl-CoA, lauroyl-CoA, caproyl-CoA, and trimethyltridecanoyl-CoA. Glutaryl-CoA was found to 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 to which each enzyme contributes to the oxidation was found to differ between the various acyl-CoA esters. [on SciFinder (R)]
|Journal||Journal of Biochemistry|
|Publication status||Published - 1993|
Wanders, R. J. A., Denis, S. W., & Dacremont, G. (1993). Studies on the substrate specificity of the inducible and non-inducible acyl-CoA oxidases from rat kidney peroxisomes. Journal of Biochemistry, 113(5), 577-582.