Pyrene dodecanoic acid coenzyme A ester: peroxisomal oxidation and chain shortening

Shimon Gatt, Jon Bremer, Harald Osmundsen

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)130-133
Number of pages4
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume958
Issue number1
DOIs
StatePublished - 19 Jan 1988
Externally publishedYes

Keywords

  • Beta oxidation
  • Peroxisomal beta oxidation
  • Pyrene dodeconoic acid
  • Pyrene fatty acid

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