Alterations in the activities of enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, and 2,4-dienoyl-CoA reductase in rat liver mitochondria and peroxisomes caused by clofibrate were compared in order to clarify the metabolic pathways for unsaturated fatty acids. Our results suggest that there are two pathways for fatty acids having (a) double bond(s) at the even-numbered carbon atom(s) both in mitochondria and in peroxisomes. One is the hydratase-epimerase participating pathways, and the other is the reductase participating pathway. It is considered that the former in mitochondria occurs mainly under normal conditions, and the latter becomes significant when the degradation of fatty acids is stimulated.
2,4-Dienoyl-CoA reductase has been detected in crude extracts of E. coli. The reductase was shown to be induced many fold when the cells were grown in the presence of linoleic or oleic acid. The activity profile of the reductase on gel filtration was different from those of other enoyl reductases. These results suggest that there are two pathways even in E. coli for the degradation of cis-4-decenoyl-CoA, which is an intermediate in the beta-oxidation of linoleic acid, as recently proposed in rat liver.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.