Oleate β-oxidation in yeast involves thioesterase but not Yor180c protein that is not a dienoyl-CoA isomerase

André G. Ntamack, Igor V. Karpichev, Stephen J. Gould, Gillian M. Small, Horst Schulz

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


The β-oxidation of oleic acid in Saccharomyces cerevisiae (S. cerevisiae) was studied by comparing the growth of wild-type cells on oleic acid or palmitic acid with the growth of mutants that either had a deletion in the YOR180c (DCI1) gene reported to encode Δ3,52,4-dienoyl-CoA isomerase (dienoyl-CoA isomerase) or in the PTE1 gene encoding peroxisomal thioesterase 1. Growth of wild-type cells was indistinguishable from that of YOR180c mutant cells on either palmitic acid or oleic acid, whereas the PTE1 mutant grew slower and to a lower density on oleic acid but not on palmitic acid. The identification of 3,5-tetradecadienoic acid in the medium of wild-type cells but not in the medium of the PTE1 mutant proves the operation of the thioesterase-dependent pathway of oleate β-oxidation in S. cerevisiae. Dienoyl-CoA isomerase activity was very low in wild-type cells, fourfold higher in the YOR180c mutant, and not associated with purified Yor180c protein. These observations support the conclusion that the YOR180c gene does not encode dienoyl-CoA isomerase.

Original languageEnglish (US)
Pages (from-to)371-378
Number of pages8
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Issue number5
StatePublished - May 2009


  • Oleic acid
  • Peroxisomal β-oxidation
  • Saccharomyces cerevisiae
  • Thioesterase-dependent pathway
  • Yor180c protein
  • Δ,Δ-dienoyl-CoA isomerase

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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