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Originally published In Press as doi:10.1074/jbc.M008794200 on October 23, 2000

J. Biol. Chem., Vol. 276, Issue 3, 2174-2179, January 19, 2001
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Overexpression of a Mammalian Ethanolamine-specific Kinase Accelerates the CDP-ethanolamine Pathway*

Athanasios LykidisDagger , Jina WangDagger , Mohammad A. KarimDagger , and Suzanne JackowskiDagger §

From the Dagger  Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 38105 and the § Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163

Ethanolamine kinase (EKI) is the first committed step in phosphatidylethanolamine (PtdEtn) biosynthesis via the CDP-ethanolamine pathway. We identify a human cDNA encoding an ethanolamine-specific kinase EKI1 and the structure of the EKI1 gene located on chromosome 12. EKI1 overexpression in COS-7 cells results in a 170-fold increase in ethanolamine kinase-specific activity and accelerates the rate of [3H]ethanolamine incorporation into PtdEtn as a function of the ethanolamine concentration in the culture medium. Acceleration of the CDP-ethanolamine pathway does not result in elevated cellular PtdEtn levels, but rather the excess PtdEtn is degraded to glycerophosphoethanolamine. EKI1 has negligible choline kinase activity in vitro and does not influence phosphatidylcholine biosynthesis. Acceleration of the CDP-ethanolamine pathway also does not change the rate of PtdEtn formation via the decarboxylation of phosphatidylserine. The data demonstrate the existence of separate ethanolamine and choline kinases in mammals and show that ethanolamine kinase can be a rate-controlling step in PtdEtn biosynthesis.

* This work was supported by National Institutes of Health Grant GM 45737 (S. J.), Cancer Center (CORE) Support Grant CA 21765, and the American Lebanese Associated Charities.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF207600.

To whom correspondence should be addressed: Dept. of Biochemistry, St. Jude Children's Research Hosp., 332 N. Lauderdale, Memphis, TN 38105-2794. Tel.: 901-495-3433; Fax: 901-525-8025; E-mail: suzanne.jackowski@stjude.org.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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