Studies on the substrate specificity of the inducible and non-inducible acyl-CoA oxidases from rat kidney peroxisomes.
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.
Wanders
B J
BJ
Department of Clinical Biochemistry, University Hospital Amsterdam, The Netherlands.
Denis
S W
SW
Dacremont
G
G
D000214:Acyl Coenzyme A / Q000378:metabolism*; D042962:Acyl-CoA Oxidase; D000818:Animals; D002458:Cell Fractionation; D002852:Chromatography, Ion Exchange; D004790:Enzyme Induction; D004952:Esters; D007668:Kidney / Q000201:enzymology*; D008830:Microbodies / Q000201:enzymology*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D000214:Acyl Coenzyme A; D004952:Esters; D010088:Oxidoreductases; D042962:Acyl-CoA Oxidase