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Papers In Press, published online ahead of print October 23, 2000
Biochemistry, St. Jude Children's Research Hospital, Memphis, TN 38105-2794
Corresponding Author: suzanne.jackowski{at}stjude.org
Ethanolamine kinase 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 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.
J. Biol. Chem, 10.1074/jbc.M008794200
Submitted on September 26, 2000
Revised on October 19, 2000
Accepted on October 23, 2000
Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway
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