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Literature summary for 2.1.1.103 extracted from

  • Witola, W.H.; El Bissati, K.; Pessi, G.; Xie, C.; Roepe, P.D.; Ben Mamoun, C.
    Disruption of the Plasmodium falciparum PfPMT gene results in a complete loss of phosphatidylcholine biosynthesis via the SDPM pathway and severe growth and survival defects (2008), J. Biol. Chem., 283, 27636-27643.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.103

Protein Variants

Protein Variants Comment Organism
additional information construction of knockout mutants, disruption of the PfPMT gene results in a complete loss of phosphatidylcholine biosynthesis via the serine-decarboxylase phosphoethanolamine-methyltransferase, SDPM, pathway and severe growth and survival defects, phenotype, overview Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Plasmodium falciparum the transmethylation of phosphatidylethanolamine plays a role in the biosynthesis of phosphatidylcholine via the serine-decarboxylase phosphoethanolamine-methyltransferase pathway, which is important in the parasite's growth and survival, overview ?
-
 ?
S-adenosyl-L-methionine + phosphoethanolamine Plasmodium falciparum the enzyme catalyzes one step of the the three-step methylation of phosphoethanolamine to phosphocholine S-adenosyl-L-homocysteine + methylethanolamine phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-
Plasmodium falciparum
-
 gene PfPMT
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the transmethylation of phosphatidylethanolamine plays a role in the biosynthesis of phosphatidylcholine via the serine-decarboxylase phosphoethanolamine-methyltransferase pathway, which is important in the parasite's growth and survival, overview Plasmodium falciparum ?
-
 ?
S-adenosyl-L-methionine + ethanolamine phosphate
-
 Plasmodium falciparum S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
 ?
S-adenosyl-L-methionine + phosphoethanolamine
-
 Plasmodium falciparum S-adenosyl-L-homocysteine + methylethanolamine phosphate
-
 ?
S-adenosyl-L-methionine + phosphoethanolamine the enzyme catalyzes one step of the the three-step methylation of phosphoethanolamine to phosphocholine Plasmodium falciparum S-adenosyl-L-homocysteine + methylethanolamine phosphate
-
 ?

Synonyms

Synonyms Comment Organism
phosphoethanolamine methyltransferase
-
 Plasmodium falciparum
PMT
-
 Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
 assay at Plasmodium falciparum

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Plasmodium falciparum

General Information

General Information Comment Organism
malfunction knock-out of the PMT gene encoding the phosphoethanolamine methyltransferase enzyme completely abrogates the biosynthesis of phosphatidylcholine via the serine-decarboxylase-phosphoethanolamine-methyltransferase pathway, loss of PMT results in significant defects in parasite growth, multiplication, and viability, suggesting that this gene plays an important role in the pathogenesis of intraerythrocytic Plasmodium parasites Plasmodium falciparum