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 | 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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | Q6T755 | gene PfPMT | - |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli by affinity chromatography | Plasmodium falciparum |
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 | Comment | Organism |
---|---|---|
More | secondary structure of wild-type and mutant enzymes, analysis of folding properties by circular dichroism spectrophotometry, overview | Plasmodium falciparum |
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 | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Plasmodium falciparum |