Acyl-Coenzyme A synthetase and fatty acid oxidation in rat liver peroxisomes.
Rat liver peroxisomes oxidized palmitate in the presence of ATP, CoA and NAD+, and the rate of palmitate oxidation exceeded that of palmitoyl-CoA oxidation. Acyl-CoA synthetase [acid: CoA ligase (AMP-forming); EC 6.2.1.3] was found in peroxisomes. The substrate specificity of the peroxisomal synthetase towards fatty acids with various carbon chain lengths was similar to that of the microsomal enzyme. The peroxisomal synthetase activity toward palmitate (40--100 nmol/min per mg protein) was higher than the rate of palmitate oxidation by the peroxisomal system (0.7--1.7 nmol/min per mg protein). The data show that peroxisomes activate long chain fatty acids and oxidize their acyl-CoA derivatives.
D000227:Adenine Nucleotides / Q000494:pharmacology; D000818:Animals; D003065:Coenzyme A / Q000494:pharmacology; D003066:Coenzyme A Ligases / Q000378:metabolism*; D004051:Diethylhexyl Phthalate / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D008297:Male; D008830:Microbodies / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D009243:NAD / Q000494:pharmacology; D009940:Organoids / Q000201:enzymology*; D010168:Palmitates / Q000378:metabolism*; D010169:Palmitic Acids / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D000227:Adenine Nucleotides; D010168:Palmitates; D010169:Palmitic Acids; D009243:NAD; D004051:Diethylhexyl Phthalate; D003066:Coenzyme A Ligases; D003065:Coenzyme A