Hydroxymethyldihydropterin pyrophosphokinase from Plasmodium falciparum complements a folK-knockout mutant in E. coli when expressed as a separate polypeptide detached from dihydropteroate synthase-Reference-Cited by-同舟云学术

Hydroxymethyldihydropterin pyrophosphokinase from Plasmodium falciparum complements a folK-knockout mutant in E. coli when expressed as a separate polypeptide detached from dihydropteroate synthase

Published:2005-03 Issue:1 Volume:140 Page:123-125
ISSN:0166-6851
Container-title:Molecular and Biochemical Parasitology
language:en
Short-container-title:Molecular and Biochemical Parasitology

Author:

Jönsson Maria,Swedberg Göte

Publisher

Elsevier BV

Subject

Molecular Biology,Parasitology

Reference13 articles.

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3. The hydroxymethyldihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis Fas protein of Pneumocystis carinii expressed as an independent enzyme in Escherichia coli: refolding and characterization of the recombinant enzyme;Ballantine;Protein Expr Purif,1994

4. The multifunctional folic acid synthesis fas gene of Pneumocystis carinii encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase;Volpe;Eur J Biochem,1993

5. Molecular characterization of bifunctional hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium falciparum;Kasekarn;Mol Biochem Parasitol,2004

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