Mol Biochem Parasitol. 2009 Nov 17. [Epub ahead of print]
Characterizaion of a leucine aminopeptidase from Toxoplasma gondii
Jia H, Nishikawa Y, Luo Y, Yamagishi J, Sugimoto C, Xuan X.
National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido 080-8555, Japan; Department of Collaboration and Education, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Hokkaido 001-0020, Japan.
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 (E. coli), and its enzymatic activity against synthetic substrates for aminopeptidase, as well as cellular localization, were 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.
PMID: 19931316 [PubMed - as supplied by publisher]