Jia Honglin, Nishikawa Yoshifumi, Luo Yuzi, Yamagishi Junya, Sugimoto Chihiro, Xuan Xuenan
National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Inada-cho, Obihiro, Hokkaido 080-8555, Japan.
Mol Biochem Parasitol. 2010 Mar;170(1):1-6. doi: 10.1016/j.molbiopara.2009.11.005. Epub 2009 Nov 18.
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.
M17家族亮氨酸氨肽酶（LAP）从肽的N端水解氨基酸。包括疟原虫、锥虫和利什曼原虫在内的许多寄生原生动物的LAP，因其在寄生虫生物学中的关键作用而受到深入研究。在本研究中，功能性重组弓形虫LAP（rTgLAP）在大肠杆菌中表达，并测定了其对氨肽酶合成底物的酶活性以及细胞定位。该活性强烈依赖于金属二价阳离子，并被金属蛋白酶抑制剂贝抑素所抑制。我们的结果表明，TgLAP是弓形虫细胞质中的一种功能性氨肽酶。
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