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Analysis of the beta-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway.
Biochim Biophys Acta. 2005 May 15; 1734(2):169-77.BB

Abstract

The degradation of fatty acids having cis- or trans-unsaturated bond at an even carbon was analyzed in Saccharomyces cerevisiae by monitoring polyhydroxyalkanoate production in the peroxisome. Polyhydroxyalkanaote is synthesized by the polymerization of the beta-oxidation intermediates 3-hydroxy-acyl-CoAs via a bacterial polyhydroxyalkanoate synthase targeted to the peroxisome. The synthesis of polyhydroxyalkanoate in cells grown in media containing 10-cis-heptadecenoic acid was dependent on the presence of 2,4-dienoyl-CoA reductase activity as well as on Delta3,Delta2-enoyl-CoA isomerase activity. The synthesis of polyhydroxyalkanoate from 10-trans-heptadecenoic acid in mutants devoid of 2,4-dienoyl-CoA reductase revealed degradation of the trans fatty acid directly via the enoyl-CoA hydratase II activity of the multifunctional enzyme (MFE), although the level of polyhydroxyalkanoate was 10-25% to that of wild type cells. Polyhydroxyalkanoate produced from 10-trans-heptadecenoic acid in wild type cells showed substantial carbon flux through both a reductase-dependent and a direct MFE-dependent pathway. Flux through beta-oxidation was more severely reduced in mutants devoid of Delta3,Delta2-enoyl-CoA isomerase compared to mutants devoid of 2,4-dienoyl-CoA reductase. It is concluded that the intermediate 2-trans,4-trans-dienoyl-CoA is metabolized in vivo in yeast by both the enoyl-CoA hydratase II activity of the multifunctional protein and the 2,4-dienoyl-CoA reductase, and that the synthesis of the intermediate 3-trans-enoyl-CoA in the absence of the Delta3,Delta2-enoyl-CoA isomerase leads to the blockage of the direct MFE-dependent pathway in vivo.

Authors+Show Affiliations

Département de Biologie Moléculaire Végétale, Bâtiment de Biologie, Université de Lausanne, CH-1015 Lausanne, Switzerland.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15904873

Citation

Robert, Julien, et al. "Analysis of the Beta-oxidation of Trans-unsaturated Fatty Acid in Recombinant Saccharomyces Cerevisiae Expressing a Peroxisomal PHA Synthase Reveals the Involvement of a Reductase-dependent Pathway." Biochimica Et Biophysica Acta, vol. 1734, no. 2, 2005, pp. 169-77.
Robert J, Marchesini S, Delessert S, et al. Analysis of the beta-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway. Biochim Biophys Acta. 2005;1734(2):169-77.
Robert, J., Marchesini, S., Delessert, S., & Poirier, Y. (2005). Analysis of the beta-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway. Biochimica Et Biophysica Acta, 1734(2), 169-77.
Robert J, et al. Analysis of the Beta-oxidation of Trans-unsaturated Fatty Acid in Recombinant Saccharomyces Cerevisiae Expressing a Peroxisomal PHA Synthase Reveals the Involvement of a Reductase-dependent Pathway. Biochim Biophys Acta. 2005 May 15;1734(2):169-77. PubMed PMID: 15904873.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Analysis of the beta-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway. AU - Robert,Julien, AU - Marchesini,Silvia, AU - Delessert,Syndie, AU - Poirier,Yves, Y1 - 2005/03/23/ PY - 2005/01/07/received PY - 2005/02/24/revised PY - 2005/02/24/accepted PY - 2005/5/21/pubmed PY - 2005/7/7/medline PY - 2005/5/21/entrez SP - 169 EP - 77 JF - Biochimica et biophysica acta JO - Biochim Biophys Acta VL - 1734 IS - 2 N2 - The degradation of fatty acids having cis- or trans-unsaturated bond at an even carbon was analyzed in Saccharomyces cerevisiae by monitoring polyhydroxyalkanoate production in the peroxisome. Polyhydroxyalkanaote is synthesized by the polymerization of the beta-oxidation intermediates 3-hydroxy-acyl-CoAs via a bacterial polyhydroxyalkanoate synthase targeted to the peroxisome. The synthesis of polyhydroxyalkanoate in cells grown in media containing 10-cis-heptadecenoic acid was dependent on the presence of 2,4-dienoyl-CoA reductase activity as well as on Delta3,Delta2-enoyl-CoA isomerase activity. The synthesis of polyhydroxyalkanoate from 10-trans-heptadecenoic acid in mutants devoid of 2,4-dienoyl-CoA reductase revealed degradation of the trans fatty acid directly via the enoyl-CoA hydratase II activity of the multifunctional enzyme (MFE), although the level of polyhydroxyalkanoate was 10-25% to that of wild type cells. Polyhydroxyalkanoate produced from 10-trans-heptadecenoic acid in wild type cells showed substantial carbon flux through both a reductase-dependent and a direct MFE-dependent pathway. Flux through beta-oxidation was more severely reduced in mutants devoid of Delta3,Delta2-enoyl-CoA isomerase compared to mutants devoid of 2,4-dienoyl-CoA reductase. It is concluded that the intermediate 2-trans,4-trans-dienoyl-CoA is metabolized in vivo in yeast by both the enoyl-CoA hydratase II activity of the multifunctional protein and the 2,4-dienoyl-CoA reductase, and that the synthesis of the intermediate 3-trans-enoyl-CoA in the absence of the Delta3,Delta2-enoyl-CoA isomerase leads to the blockage of the direct MFE-dependent pathway in vivo. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/15904873/Analysis_of_the_beta_oxidation_of_trans_unsaturated_fatty_acid_in_recombinant_Saccharomyces_cerevisiae_expressing_a_peroxisomal_PHA_synthase_reveals_the_involvement_of_a_reductase_dependent_pathway_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1388-1981(05)00042-9 DB - PRIME DP - Unbound Medicine ER -