ArticleStructure (London, England : 1993)2013
Evolution of structure and mechanistic divergence in di-domain methyltransferases from nematode phosphocholine biosynthesis.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Toward understanding the catalytic mechanism for two classes of bacterial phospholipid N-methyltransferases.The FEBS journal · 2026Article
- Fungal Sphingolipids: Biosynthesis Pathways, Structural Features and Biological Functions.Journal of fungi (Basel, Switzerland) · 2026Review
- Structural basis for phosphatidylcholine synthesis by bacterial phospholipid N-methyltransferases.The Journal of biological chemistry · 2025Article
- Broad-Spectrum Inhibitors for Conserved Unique Phosphoethanolamine Methyltransferases in Parasitic Nematodes Possess Anthelmintic Efficacy.Antimicrobial agents and chemotherapy · 2023Article
- Cloning and Functional Identification of Phosphoethanolamine Methyltransferase in Soybean (Frontiers in plant science · 2021Article
- The Structure of the Bifunctional Everninomicin Biosynthetic Enzyme EvdMO1 Suggests Independent Activity of the Fused Methyltransferase-Oxidase Domains.Biochemistry · 2018Article
- Covering their bases: The phosphobase methylation pathway in plants.The Journal of biological chemistry · 2017Article
- Conformational changes in the di-domain structure ofThe Journal of biological chemistry · 2017Article
- Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity.The Journal of biological chemistry · 2016Article
- In vitro anthelmintic efficacy of inhibitors of phosphoethanolamine Methyltransferases in Haemonchus contortus.International journal for parasitology. Drugs and drug resistance · 2016Article
- An alternative mechanism for the methylation of phosphoethanolamine catalyzed by Plasmodium falciparum phosphoethanolamine methyltransferase.The Journal of biological chemistry · 2014Article
- Nematode phospholipid metabolism: an example of closing the genome-structure-function circle.Trends in parasitology · 2014Review
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2 authors at 1 institution in 1 country.
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Abstract
The phosphobase methylation pathway is the major route for supplying phosphocholine to phospholipid biosynthesis in plants, nematodes, and Plasmodium. In this pathway, phosphoethanolamine N-methyltransferase (PMT) catalyzes the sequential methylation of phosphoethanolamine to phosphocholine. In the PMT, one domain (MT1) catalyzes methylation of phosphoethanolamine to phosphomonomethylethanolamine and a second domain (MT2) completes the synthesis of phosphocholine. The X-ray crystal structures of the di-domain PMT from the parasitic nematode Haemonchus contortus (HcPMT1 and HcPMT2) reveal that the catalytic domains of these proteins are structurally distinct and allow for selective methylation of phosphobase substrates using different active site architectures. These structures also reveal changes leading to loss of function in the vestigial domains of the nematode PMT. Divergence of function in the two nematode PMTs provides two distinct antiparasitic inhibitor targets within the same essential metabolic pathway. The PMTs from nematodes, plants, and Plasmodium also highlight adaptable metabolic modularity in evolutionarily diverse organisms.
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