Pyrene dodecanoic acid coenzyme A ester: peroxisomal oxidation and chain shortening.
Pyrenedodecanoyl-CoA was beta-oxidized by isolated rat liver peroxisomes at a rate which was about 50% of that observed with palmitoyl-CoA. Measurement of the quantity of NADH formed from a limiting amount of pyrenedodecanoyl-CoA suggested that it was subjected to two to three cycles of beta-oxidation. Pyrenedodecanoyl-CoA was a very poor substrate for carnitine palmitoyltransferase, exhibiting less than 1% of the rate obtained with palmitoyl-CoA; it also was a strong inhibitor of this enzyme. With rat liver microsomal alpha-glycerophosphate acyltransferase the rate of reaction with pyrenedodecanoyl-CoA was only 3-4% of that observed with palmitoyl-CoA.
Gatt
S
S
Department of Membrane Biochemistry and Neurochemistry, Hebrew University-Hadassah School of Medicine, Jerusalem, Israel.
Bremer
J
J
Osmundsen
H
H
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000378:metabolism; D002458:Cell Fractionation; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D008830:Microbodies / Q000378:metabolism*; D010084:Oxidation-Reduction; D010171:Palmitoyl Coenzyme A / Q000378:metabolism; D051381:Rats
D000214:Acyl Coenzyme A; D010171:Palmitoyl Coenzyme A; C044859:pyrenedodecanoyl-coenzyme A; D002334:Carnitine O-Palmitoyltransferase