Characterization of a leucine aminopeptidase from Toxoplasma gondii

Honglin Jia, Yoshifumi Nishikawa, Yuzi Luo, Junya Yamagishi, Chihiro Sugimoto, Xuenan Xuan

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)


The M17 family leucine aminopeptidase (LAP) hydrolyzes amino acids from the N-terminus of peptides. Many LAPs from parasitic protozoa, including Plasmodium, Trypanosoma, and Leishmania, have been intensely investigated because of their crucial roles in parasite biology. In this study, the functional recombinant Toxoplasma gondii LAP (rTgLAP) was expressed in Escherichia coli, and its enzymatic activity against synthetic substrates for aminopeptidase, as well as cellular localization, was determined. The activity was strongly dependent on metal divalent cations, and was inhibited by bestatin, which is an inhibitor for metalloprotease. Our results indicated that TgLAP is a functional aminopeptidase in the cytoplasm of T. gondii.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalMolecular and Biochemical Parasitology
Issue number1
Publication statusPublished - 2010 Mar
Externally publishedYes


  • Enzymatic activity
  • Leucine aminopeptidase
  • Toxoplasma gondii

ASJC Scopus subject areas

  • Parasitology
  • Molecular Biology


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