Literature DB >> 19830908

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

André G Ntamack1, Igor V Karpichev, Stephen J Gould, Gillian M Small, Horst Schulz.   

Abstract

The beta-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 delta3,5,delta2,4-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 beta-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.

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Year:  2009        PMID: 19830908      PMCID: PMC3005976          DOI: 10.1016/j.bbalip.2009.01.026

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  20 in total

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Journal:  Methods Enzymol       Date:  1981       Impact factor: 1.600

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Authors:  H Schulz; H Staack
Journal:  Methods Enzymol       Date:  1981       Impact factor: 1.600

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Journal:  Biochem Biophys Res Commun       Date:  1999-06-24       Impact factor: 3.575

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Journal:  Anal Biochem       Date:  1986-06       Impact factor: 3.365

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