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.
Enables phosphatidyl-N-dimethylethanolamine N-methyltransferase activity and phosphatidyl-N-methylethanolamine N-methyltransferase activity. Involved in phosphatidylcholine biosynthetic process. Is an ortholog of human TMT1A (thiol methyltransferase 1A) and TMT1B (thiol methyltransferase 1B).
Map position created from combination of previous interpolated map position (based on known location of sequence) and allele information. Therefore this is not a genetic map position based on recombination frequencies or genetic experiments. This was done on advice of the CGC.