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J. Biol. Chem., Vol. 281, Issue 17, 11729-11735, April 28, 2006

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The Peroxisomal Acyl-CoA Thioesterase Pte1p from Saccharomyces cerevisiae Is Required for Efficient Degradation of Short Straight Chain and Branched Chain Fatty Acids^*

Isamu Maeda¹, Syndie Delessert, Seiko Hasegawa, Yoshiaki Seto, Sophie Zuber, and Yves Poirier, Funded, in part, from FNRS Grant 3100A0-105874 as well from the Herbette Foundation and the Etat de Vaud²

From the Department of Bioproductive Science, Faculty of Agriculture, Utsunomiya University, 350 Minemachi, Utsunomiya 321-8505, Japan and Department of Plant Molecular Biology, Biophore, University of Lausanne, CH-1015 Lausanne, Switzerland

The role of the Saccharomyces cerevisae peroxisomal acyl-coenzyme A (acyl-CoA) thioesterase (Pte1p) in fatty acid -oxidation was studied by analyzing the in vitro kinetic activity of the purified protein as well as by measuring the carbon flux through the -oxidation cycle in vivo using the synthesis of peroxisomal polyhydroxyalkanoate (PHA) from the polymerization of the 3-hydroxyacyl-CoAs as a marker. The amount of PHA synthesized from the degradation of 10-cis-heptadecenoic, tridecanoic, undecanoic, or nonanoic acids was equivalent or slightly reduced in the pte1 strain compared with wild type. In contrast, a strong reduction in PHA synthesized from heptanoic acid and 8-methyl-nonanoic acid was observed for the pte1 strain compared with wild type. The poor catabolism of 8-methyl-nonanoic acid via -oxidation in pte1 negatively impacted the degradation of 10-cis-heptadecenoic acid and reduced the ability of the cells to efficiently grow in medium containing such fatty acids. An increase in the proportion of the short chain 3-hydroxyacid monomers was observed in PHA synthesized in pte1 cells grown on a variety of fatty acids, indicating a reduction in the metabolism of short chain acyl-CoAs in these cells. A purified histidine-tagged Pte1p showed high activity toward short and medium chain length acyl-CoAs, including butyryl-CoA, decanoyl-CoA and 8-methyl-nonanoyl-CoA. The kinetic parameters measured for the purified Pte1p fit well with the implication of this enzyme in the efficient metabolism of short straight and branched chain fatty acyl-CoAs by the -oxidation cycle.

Received for publication, October 31, 2005 , and in revised form, February 17, 2006.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipient of a fellowship of the exchange program between the Fonds National Suisse de la Recherche Scientifique (FNRS) and the Japan Society for the Promotion of Science (83JS-067392).

² To whom correspondence should be addressed: Dept. of Plant Molecular Biology, Biophore, University of Lausanne, CH-1015 Lausanne, Switzerland. Tel.: 41-21-692-4222; Fax: 41-21-692-4195; E-mail: yves.poirier{at}unil.ch.

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