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A more recent version of this article appeared on March 1, 2007

Papers In Press, published online ahead of print November 28, 2006
J. Lipid Res., doi:10.1194/jlr.C600019-JLR200
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Submitted on November 7, 2006
Revised on November 27, 2006
Accepted on November 28, 2006

Identification and characterization of a human ethanolaminephosphotransferase1 (hEPT1)

Yasuhiro Horibata and Yoshio Hirabayashi

Brain Science Institute, RIKEN, Saitama 351-0198

Corresponding Author: horibata{at}brain.riken.jp

CDP-ethanolamine:diacylglycerol ethanolaminephosphotransferase (EPT) catalyses the transfer of phosphoethanolamine from CDP-ethanolamine to diacylglycerol to produce phosphatidylethanolamine (PE). Up to date, the dual specificity of choline/ethanolaminephosphotransferase (CEPT) has been recognized as the total activity responsible for the synthesis of PE via CDP-ethanolamine pathway in human. We report here the identification and characterization of another human cDNA that encodes CDP-ethanolamine specific EPT (hEPT1). Though homology search, we found that human selenoprotein I contained the CDP-alcohol phosphatidyltransferase signature, a common motif conserved in phospholipids synthases. Bacterial expression of the cDNA in Escherichia coli demonstrated that the product specifically utilized CDP-ethanolamine as the phosphobase donor to produce PE with the activation by both Mn2+ and Mg2+. RT-PCR and northern blot analysis revealed that hEPT1 was ubiquitously expressed in multiple tissues, but in brain, highly in cerebellum. Here we propose that in addition to previously identified CEPT, hEPT1 is involved in the biosynthesis of PE via Kennedy pathway.


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