Interactions between the omega- and beta-oxidations of fatty acids.
Long-chain monocarboxylic, omega-hydroxymonocarboxylic and dicarboxylic acids were activated approximately at the same rate by rat liver homogenates into their CoA esters (2-3 U/g liver). These acyl-CoA were substrates for rat liver peroxisomal beta-oxidation. The distribution of the peroxisomal oxidation of these substrates was also studied in various tissues. Rat liver mitochondria were capable of oxidizing long-chain monocarboxyl- and omega-hydroxymonocarboxylyl-CoAs but not dicarboxylyl-CoAs. When the mitochondrial preparations were incubated in coupling conditions, the addition of either free decanoic acid or free 10-hydroxydecanoic acid resulted in an increase of the oxygen uptake conversely to the addition of decanedioic acid. The comparative study of the chain-length substrate specificity of peroxisomal fatty acyl-CoA oxidase and mitochondrial fatty acyl-CoA dehydrogenase activities revealed that, actually, both types of organelles, peroxisomes and mitochondria, contain "oxido-reductases" active on long-chain monocarboxylyl-CoAs, omega-hydroxymonocarboxylyl-CoAs and dicarboxylyl-CoAs.
Vamecq
J
J
Laboratoire de Chimie Physiologique, International Institute of Cellular and Molecular Pathology, Brussels, Belgium.
Draye
J P
JP
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D002264:Carboxylic Acids / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D008830:Microbodies / Q000378:metabolism; D008930:Mitochondria, Liver / Q000378:metabolism; D009928:Organ Specificity; D010084:Oxidation-Reduction; D051381:Rats; D011919:Rats, Inbred Strains; D013329:Structure-Activity Relationship
D000214:Acyl Coenzyme A; D002264:Carboxylic Acids