Plasmodium falciparum: isolation and characterisation of a gene encoding protozoan GMP synthase.
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.
McConkey
G A
GA
Department of Biology, University of Leeds, Miall Building, Clarendon Way, United Kingdom, Leeds LS2 9JT.
D000595:Amino Acid Sequence; D000818:Animals; D019731:Carbon-Nitrogen Ligases / Q000737:chemistry / Q000235:genetics*; D017124:Conserved Sequence; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000201:enzymology / Q000235:genetics*; D016415:Sequence Alignment
D019731:Carbon-Nitrogen Ligases; C020828:GMP synthase (glutamine-hydrolyzing)