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Literature summary for 2.1.1.103 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)

Cloned (Comment) Organism
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

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Plasmodium falciparum Q6T755 gene PfPMT
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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

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

Synonyms

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

Cofactor

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