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A more recent version of this article appeared on June 1, 2004

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J. Lipid Res., doi:10.1194/jlr.M300512-JLR200
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Submitted on December 16, 2003
Revised on March 19, 2004
Accepted on March 19, 2004

Identification of the peroxisomal beta -oxidation enzymes involved in the degradation of long-chain dicarboxylic acids

Sacha Ferdinandusse, Simone Denis, Carlo W. T. van Roermund, Ronald J. A. Wanders, and Georges Dacremont

Lab. Genetic Metabolic Diseases, Academic Medical Center, Amsterdam 1100 DE

Corresponding Author: s.ferdinandusse{at}amc.uva.nl

Dicarboxylic acids (DCAs) are omega -oxidation products of monocarboxylic acids. After activation by a dicarboxylyl-CoA synthetase, the dicarboxylyl-CoA esters are shortened via beta -oxidation. Although it has been extensively studied where this beta -oxidation process takes place, the intracellular site of DCA oxidation has remained controversial. Making use of fibroblasts from patients with defined mitochondrial and peroxisomal fatty acid oxidation defects, we show in this paper that peroxisomes, and not mitochondria, are involved in the beta -oxidation of C16DCA. Additional studies in fibroblasts from patients with X-linked adrenoleukodystrophy (X-ALD), straight-chain acyl-CoA oxidase (SCOX) deficiency, D-bifunctional protein (DBP) deficiency and rhizomelic chondrodysplasia punctata (RCDP) type 1, together with direct enzyme measurements with human recombinant L-bifunctional protein (LBP) and DBP expressed in a fox2 deletion mutant of Saccharomyces cerevisiae, show that the main enzymes involved in beta -oxidation of C16DCA are SCOX, both LBP and DBP, and sterol carrier protein X (SCPx) possibly together with the classical 3-ketoacyl-CoA thiolase. This is the first indication of a specific function for LBP, which has remained elusive until now.


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