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Literature summary for 6.3.2.17 extracted from

  • Salcedo, E.; Cortese, J.F.; Plowe, C.V.; Sims, P.F.G.; Hyde, J.E.
    A bifunctional dihydrofolate synthetase--folylpolyglutamate synthetase in Plasmodium falciparum identified by functional complementation in yeast and bacteria (2001), Mol. Biochem. Parasitol., 112, 239-252.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli and Saccharomyces cerevisiae Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
additional information removal of the first 16 or 40 residues of the protein abolishes the enzyme activity in the yeast cell host, Saccharomyces cerevisiae but not in Escherichia coli Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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3D7, K1, Tak9, M24, K39, HB3, W282, V1/S, Dd2 and FCB lines
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the expression of the enzyme in Escherichia coli and Saccharomyces cerevisiae defective strains restores Escherichia coli cells to methionine and glycine prototrophy on minimal medium, but cannot entirely compensate for the loss of the native homologue in Saccharomyces cerevisiae. The malarial gene encodes a protein carrying dihydrofolate synthetase and folylpolyglutamate synthetase activities, both needed for the de novo folate synthesis Plasmodium falciparum ?
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