CELE_F54D11.1, F54D11.1

pmt-2 encodes an experimentally validated N-methyltransferase required for phosphocholine biosynthesis and viability; PMT-2 lacks known mammalian orthologs, but has orthologs in parasitic nematodes, fish, amphibians, echinoderms, plants, alveolata, and bacteria; PMT-2 is distantly paralogous to PMT-1; PMT-2 has a single C-terminal methyltransferase domain, unlike plant enzymes that have two tandem domains, and catalyses only two of three steps in phosphocholine biosynthesis (methylation of phosphomonomethylethanolamine [P-MME] to phosphodimethylethanolamine [P-DME] and of P-DME to phosphocholine, but not methylation of phosphoethanolamine to P-MME); pmt-2(RNAi) animals are unable to progress past the L1 larval stage, but can be rescued by choline in their food media; PMT-2 binds its substrates in random order, and is competitively inhibited by phosphocholine; given its phylogenetic and enzymatic specificity, coupled with its inviable RNAi phenotype, PMT-1 is a plausible target for nematicides.

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