Author:

Keywords:

rat-liver peroxisomes, acyl-coa oxidase, fatty-acid oxidation, human skin fibroblasts, lipid-transfer protein, trihydroxycoprostanoyl-coa, sterol-carrier, alpha-oxidation, palmitoyl-coa, long-chain, Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Cell Biology, Medicine, Research & Experimental, Multidisciplinary Sciences, Research & Experimental Medicine, Science & Technology - Other Topics, RAT-LIVER PEROXISOMES, ACYL-COA OXIDASE, FATTY-ACID OXIDATION, HUMAN SKIN FIBROBLASTS, LIPID-TRANSFER PROTEIN, TRIHYDROXYCOPROSTANOYL-COA, STEROL-CARRIER, ALPHA-OXIDATION, PALMITOYL-COA, LONG-CHAIN, 3-Hydroxyacyl CoA Dehydrogenases, Acetyl-CoA C-Acetyltransferase, Acyl Coenzyme A, Animals, Coenzyme A Ligases, Enoyl-CoA Hydratase, Fatty Acids, Humans, Intracellular Membranes, Isomerases, Microbodies, Mitochondria, Multienzyme Complexes, Oxidation-Reduction, Peroxisomal Bifunctional Enzyme, Rats, Repressor Proteins, Saccharomyces cerevisiae Proteins, Substrate Specificity, General Science & Technology

Abstract:

In eukaryotic microorganisms such as yeasts and fungi, peroxisomes are the sole site of beta-oxidation. Also in plants, peroxisomes are capable of beta-oxidizing fatty acids. Whether plant mitochondria are involved in fatty acid catabolism remains controversial. A few reports indicate, however, that plant mitochondria contain a functional beta-oxidation system, but its capacity seems to be 50- to 200-fold lower than that of peroxisomes.(1) In mammals, both peroxisomes and mitochondria are actively engaged in the beta-oxidation of fatty acids and other lipophilic carboxylates. This paper deals with peroxisomal beta-oxidation in mammals. Since peroxisomal beta-oxidation has been best characterized in rat and man, our description will be limited mainly to these two species.