Characterization of a leucine aminopeptidase of Babesia gibsoni

H. Jia, M. A. Terkawi, G. O. Aboge, Y. K. Goo, Y. Luo, Y. Li, J. Yamagishi, Y. Nishikawa, I. Igarashi, C. Sugimoto, K. Fujisaki, X. Xuan

    Research output: Contribution to journalArticlepeer-review

    12 Citations (Scopus)


    Peptidases of parasitic protozoa are currently under intense investigation in order to identify novel virulence factors, drug targets, and vaccine candidates, except in Babesia. Leucine aminopeptidases in protozoa, such as Plasmodium and Leishmania, have been identified to be involved in free amino acid regulation. We report here the molecular and enzymatic characterization, as well as the localization of a leucine aminopeptidase, a member of the M17 cytosolic aminopeptidase family, from B. gibsoni (BgLAP). A functional recombinant BgLAP (rBgLAP) expressed in Escherichia coli efficiently hydrolysed synthetic substrates for aminopeptidase, a leucine substrate. Enzyme activity of the rBgLAP was found to be optimum at pH 80 and at 37C. The substrate profile was slightly different from its homologue in P. falciprum. The activity was also strongly dependent on metal divalent cations, and was inhibited by bestatin, which is a specific inhibitor for metalloprotease. These results indicated that BgLAP played an important role in free amino acid regulation.

    Original languageEnglish
    Pages (from-to)945-952
    Number of pages8
    Issue number9
    Publication statusPublished - 2009 Aug 1


    • Babesia gibsoni
    • Enzymatic activity
    • Leucine aminopeptidase

    ASJC Scopus subject areas

    • Parasitology
    • Animal Science and Zoology
    • Infectious Diseases


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