Characterization of N-myristoyltransferase from Plasmodium falciparum

Ruwani S. Gunaratne, Mohammed Sajid, Irene T. Ling, Renu Tripathi, Justin A. Pachebat, Anthony A Holder

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54 Citations (SciVal)


The gene coding for myristoyl-CoA:protein N-myristoyltransferase (NMT) has been cloned from the malaria parasite Plasmodium falciparum. The gene appears to be single copy and mRNA is expressed in asexual blood-stage forms. Comparison of cDNA and genomic sequences identified three small introns. The open reading frame codes for a 410-amino-acid protein and no evidence of forms with an extended N-terminal coding sequence was obtained. Residues important in substrate binding and in the catalytic mechanism in other species are conserved. The protein was expressed from a plasmid in Escherichia coli, partially purified and shown to have enzymic activity using a synthetic peptide substrate. Comparison of the malaria parasite protein with that derived from the human gene showed a different pattern of inhibition by chemical modification. Human NMT activity was inhibited by diethylpyrocarbonate and partially inhibited by iodacetamide, whereas P. falciparum NMT activity was not inhibited by either pre-treatment. Since the enzyme in infectious fungi is a target for potential chemotherapeutic drugs, it should also be investigated in the context of parasitic infections such as that responsible for malaria.

Original languageEnglish
Pages (from-to)459-463
Number of pages5
JournalBiochemical Journal
Issue number2
Publication statusPublished - 01 Jun 2000


  • Acyltransferases
  • Amino Acid Sequence
  • Animals
  • Candida albicans
  • Cloning, Molecular
  • Diethyl Pyrocarbonate
  • Ethylmaleimide
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Open Reading Frames
  • Plasmodium falciparum
  • Polymerase Chain Reaction
  • Protein Biosynthesis
  • Recombinant Proteins
  • Saccharomyces cerevisiae
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Recombinant enzyme
  • Protein acylation
  • Malaria parasite


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