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Literature summary for 2.7.6.3 extracted from

  • Joensson, M.; Swedberg, G.
    Hydroxymethyldihydropterin pyrophosphokinase from Plasmodium falciparum complements a folK-knockout mutant in E. coli when expressed as a separate polypeptide detached from dihydropteroate synthase (2005), Mol. Biochem. Parasitol., 140, 123-125.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
hydroxymethyldihydropterin diphosphokinase from Plasmodium falciparum complements a folK-knockout mutant in Escherichia coli when expressed as a separate polypeptide detached from dihydropteroate synthase. Hydroxymethyldihydropterin diphosphokinase part of the bifunctional protein can function by itself but that a larger part of the polypeptide is needed to ensure full functionality Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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Synonyms

Synonyms Comment Organism
HPPK/dihydropteroate synthase HPPK part of the bifunctional protein can function by itself but a larger part of the polypeptide is needed to ensure full functionality Plasmodium falciparum
hydroxymethyldihydropterin diphosphokinase/dihydropteroate synthase HPPK part of the bifunctional protein can function by itself but a larger part of the polypeptide is needed to ensure full functionality Plasmodium falciparum