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

    30 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


    • Enzymatic activity
    • Leucine aminopeptidase
    • Toxoplasma gondii

    ASJC Scopus subject areas

    • Parasitology
    • Molecular Biology


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