Identification of inhibitors of <Emphasis Type="Italic">Plasmodium falciparum</Emphasis> phosphoethanolamine methyltransferase using an enzyme-coupled transmethylation assay |
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| Authors: | April M Bobenchik Jae-Yeon Choi Arunima Mishra Iulian N Rujan Bing Hao Dennis R Voelker Jeffrey C Hoch Choukri Ben Mamoun |
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| Institution: | (1) Department of Internal Medicine, Section of Infectious Diseases, Yale School of Medicine, 333 Cedar St., New Haven, 06052, USA;(2) Department of Genetics and Developmental Biology, University of Connecticut Health Center, 263 Farmington Ave., Farmington, 06030, USA;(3) The Program in Cell Biology, Department of Medicine, National Jewish Medical and Research Center, 1400 Jackson St, Denver, 80206, USA;(4) Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, 263 Farmington Ave., Farmington, 06030, USA |
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| Abstract: | Background The phosphoethanolamine methyltransferase, PfPMT, of the human malaria parasite Plasmodium falciparum, a member of a newly identified family of phosphoethanolamine methyltransferases (PMT) found solely in some protozoa, nematodes,
frogs, and plants, is involved in the synthesis of the major membrane phospholipid, phosphatidylcholine. PMT enzymes catalyze
a three-step S-adenosylmethionine-dependent methylation of the nitrogen atom of phosphoethanolamine to form phosphocholine.
In P. falciparum, this activity is a limiting step in the pathway of synthesis of phosphatidylcholine from serine and plays an important role
in the development, replication and survival of the parasite within human red blood cells. |
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