Identification of pristanoyl-CoA oxidase as a distinct, clofibrate non-inducible enzyme in rat liver peroxisomes.
In this paper we describe the identification of pristanoyl-CoA oxidase activity in rat liver peroxisomes. This activity was not stimulated by clofibrate feeding. Furthermore, the activity was found in multiple tissues. These results show that pristanoyl-CoA oxidase is different from any of the known oxidases which include a clofibrate-inducible acyl-CoA oxidase and the recently identified cholestanoyl-CoA oxidase. Gelfiltration and chromatofocusing experiments provide conclusive evidence that we are dealing with a novel acyl-CoA oxidase with a unique function in peroxisomal beta-oxidation.
Department of Clinical Biochemistry, University Hospital Amsterdam, The Netherlands.
R J
RJ
Wanders
S
S
Denis
C
C
Jakobs
H J
HJ
ten Brink
D000818:Animals; D002994:Clofibrate / Q000494:pharmacology; D003605:D-Amino-Acid Oxidase / Q000032:analysis; D004790:Enzyme Induction / Q000187:drug effects; D005969:Glutamate Dehydrogenase / Q000032:analysis; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008830:Microbodies / Q000187:drug effects / Q000201:enzymology*; D010084:Oxidation-Reduction / Q000187:drug effects; D010088:Oxidoreductases / Q000096:biosynthesis*; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
D010088:Oxidoreductases; C066272:pristanoyl-CoA oxidase; D005969:Glutamate Dehydrogenase; D003605:D-Amino-Acid Oxidase; D002994:Clofibrate