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A more recent version of this article appeared on December 1, 2003

Papers In Press, published online ahead of print August 16, 2003
J. Lipid Res., doi:10.1194/jlr.M300230-JLR200
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Submitted on May 28, 2003
Revised on August 12, 2003
Accepted on August 12, 2003

Further studies on the substrate spectrum of phytanoyl-CoA hydroxylase: implications for Refsum disease?

Veerle Foulon, Stanny Asselberghs, Wendy Geens, Guy P. Mannaerts, Minne Casteels, and Paul P. Van Veldhoven

Moleculaire Celbiologie, Katholieke Universiteit Leuven, Leuven B3000

Corresponding Author: paul.vanveldhoven{at}med.kuleuven.ac.be

Refsum disease is a peroxisomal disorder characterized by adult-onset retinitis pigmentosa, anosmia, sensory neuropathy, ataxia and an accumulation of phytanic acid in plasma and tissues. About 45% of cases are caused by mutations in phytanoyl-CoA hydroxylase (PAHX), the enzyme catalyzing the second step in the peroxisomal alpha-oxidation of 3-methylbranched fatty acids. To study the substrate specificity of human PAHX, different 3-alkyl-branched substrates were synthesized and incubated with a recombinant polyhistidine-tagged protein. The enzyme showed activity not only towards racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also towards a variety of other mono-branched 3-methylacyl-CoA esters with a chain length down to 7 carbon atoms. Furthermore, PAHX hydroxylated a 3-ethylacyl-CoA quite well, whereas a 3-propylacyl-CoA was a poor substrate. Hydroxylation of neither 2- or 4-methyl-branched acyl-CoA esters, nor long or very long straight chain acyl-CoA esters could be detected. Conclusion: The results presented in this paper show that the substrate specificity of PAHX, with regard to the length of both the acyl-chain and the branch at position 3, is broader than expected. Hence, Refsum disease might be characterized not only by an accumulation of phytanic acid, but also of other 3-alkyl-branched fatty acids.


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