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Literature summary extracted from

  • Reynolds, J.M.; Takebe, S.; Choi, J.Y.; El Bissati, K.; Witola, W.H.; Bobenchik, A.M.; Hoch, J.C.; Voelker, D.R.; Mamoun, C.B.
    Biochemical and genetic analysis of the phosphoethanolamine methyltransferase of the human malaria parasite Plasmodium falciparum (2008), J. Biol. Chem., 283, 7894-7900.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.103 expression of wild-type and mutant enzymes in Escherichia coli, and complementation study using the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.103 D128A site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 D128E site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 D128N site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 D61A site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 D61E site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 D61N site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 G153A site-directed mutagenesis, the PfPMT mutant complements the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 G63A site-directed mutagenesis, the PfPMT mutant complements the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 G83A site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview Plasmodium falciparum
2.1.1.103 additional information construction of 24 mutants of PMT Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.103 additional information
-
 additional information kinetics Plasmodium falciparum
2.1.1.103 0.0352
-
 S-adenosyl-L-methionine
-
 Plasmodium falciparum
2.1.1.103 0.0661
-
 Phosphoethanolamine
-
 Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.103 S-adenosyl-L-methionine + phosphoethanolamine Plasmodium falciparum Plasmodium falciparum PMT plays a critical role in the synthesis of phosphatidylcholine via a plant-like pathway involving serine decarboxylation and phosphoethanolamine methylation S-adenosyl-L-homocysteine + methylethanolamine phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.103 Plasmodium falciparum Q6T755 gene PfPMT
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.103 recombinant wild-type and mutant enzymes from Escherichia coli by affinity chromatography Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.103 S-adenosyl-L-methionine + phosphoethanolamine Plasmodium falciparum PMT plays a critical role in the synthesis of phosphatidylcholine via a plant-like pathway involving serine decarboxylation and phosphoethanolamine methylation Plasmodium falciparum S-adenosyl-L-homocysteine + methylethanolamine phosphate
-
 ?
2.1.1.103 S-adenosyl-L-methionine + phosphoethanolamine amino acids Asp61, Gly83, and Asp128 play a critical role in enzyme activity. Asp-61 is located within the VLDIGSGLG motif I of PfPMT conserved in all PMTs, mutational analysis of PfPMT substrate binding, overview Plasmodium falciparum S-adenosyl-L-homocysteine + methylethanolamine phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.103 More secondary structure of wild-type and mutant enzymes, analysis of folding properties by circular dichroism spectrophotometry, overview Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
2.1.1.103 More PfPMT is a member of an unusual class of SAM-dependent methyltransferases Plasmodium falciparum
2.1.1.103 phosphoethanolamine methyltransferase
-
 Plasmodium falciparum
2.1.1.103 PMT
-
 Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.103 S-adenosyl-L-methionine
-
 Plasmodium falciparum