Plasmodium falciparum: isolation and characterisation of a gene encoding protozoan GMP synthase

Exp Parasitol. 2000 Jan;94(1):23-32. doi: 10.1006/expr.1999.4467.


The final step in guanylate nucleotide biosynthesis is catalysed by GMP synthase. This paper presents the first isolation of a gene encoding a protozoan GMP synthase. The deduced amino acid sequence from Plasmodium falciparum shares 40% identity with yeast GMP synthase and contains motifs conserved in catalysis. Expression of the gene is regulated through the parasite's development in human red blood cells with maximal expression during the point of DNA replication. Psicofuranine, which inhibits GMP synthase, interrupts parasite growth, supporting the role of this enzyme. These findings will aid development of inhibitors of purine salvage in malaria parasites.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbon-Nitrogen Ligases / chemistry
  • Carbon-Nitrogen Ligases / genetics*
  • Conserved Sequence
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Molecular Sequence Data
  • Plasmodium falciparum / enzymology
  • Plasmodium falciparum / genetics*
  • Sequence Alignment


  • Carbon-Nitrogen Ligases
  • GMP synthase (glutamine-hydrolyzing)

Associated data

  • GENBANK/AF152349