Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast

Takuya Maeda, Tomoya Saito, Omar S. Harb, David S. Roos, Satoru Takeo, Hiroko Suzuki, Takafumi Tsuboi, Tsutomu Takeuchi, Takashi Asai

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


Bioinformatics research on Plasmodium falciparum revealed two isoforms of pyruvate kinase: type-I and type-II enzymes. The type-I enzyme shows typical glycolytic properties, while type-II enzyme is involved in fatty acid type-II biosynthesis and has been predicted to localize to the apicoplast with the targeting signal in its N-terminus. The type-I and type-II isoforms have the same evolutionary origin as Toxoplasma gondii isozymes, TgPyKI and TgPyKII, respectively; however, TgPyKII localizes to both the mitochondrion and the apicoplast. Accordingly, we made a recombinant full length of P. falciparum pyruvate kinase type-II protein using a wheat germ cell-free expression system and obtained a specific antibody against the type-II protein. Fluorescent microscopic analysis revealed that P. falciparum type-II enzyme was localized only to the apicoplast, not to the mitochondrion. The data suggest differences in localization and metabolic pathways between P. falciparum and T. gondii pyruvate kinase isoforms.

Original languageEnglish
Pages (from-to)101-105
Number of pages5
JournalParasitology International
Issue number1
Publication statusPublished - 2009 Mar
Externally publishedYes


  • Apicoplast
  • Cell-free expression
  • Mitochondria
  • Plasmodium falciparum
  • Pyruvate kinase II

ASJC Scopus subject areas

  • Parasitology
  • Infectious Diseases


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