| Literature DB >> 19931316 |
Honglin Jia1, Yoshifumi Nishikawa, Yuzi Luo, Junya Yamagishi, Chihiro Sugimoto, Xuenan Xuan.
Abstract
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.Entities:
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Year: 2009 PMID： 19931316 DOI： 10.1016/j.molbiopara.2009.11.005
Source DB: PubMed Journal: Mol Biochem Parasitol ISSN： 0166-6851 Impact factor: 1.759