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Logo of jbcThe Journal of Biological Chemistry
 
J Biol Chem. 2014 December 5; 289(49): 33826.
PMCID: PMC4256318

Finding How an Essential Enzyme in the Malarial Parasite Plasmodium falciparum Functions♦

An Alternative Mechanism for the Methylation of Phosphoethanolamine Catalyzed by Plasmodium falciparum Phosphoethanolamine Methyltransferase

♦ See referenced article, J. Biol. Chem. 2014, 289, 33815–33825

Plasmodium falciparum is the parasite that causes malaria. One of the parasitic enzymes, phosphoethanolamine methyltransferase (PfPMT), is critical for the organism's growth and development. This makes PfPMT an attractive drug target. In this Paper of the Week, a team led by Joseph Jez at Washington University in St. Louis and Victor Guallar at the Barcelona Supercomputing Center carried out computational, biochemical, and structural analyses to show that Asp-128 in PfPMT is needed for the methylation of phosphoethanolamine. Asp-128 takes on a proton via a bridging molecule of water and then transfers a methyl group from S-adenosylmethionine to phosphoethanolamine. The residue is not needed for the methylation of other phosphorylated bases. The authors note that their work “provides new insight on the evolution of multiple substrate activity” in a family of methyltransferases from different organisms.

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The phosphobase methylation pathway and the active site of the P. falciparum phosphoethanolamine methyltransferase.


Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology