Characterization of a leucine aminopeptidase from Toxoplasma gondii
Characterization of a leucine aminopeptidase from Toxoplasma gondii
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DOI：
10.1016/j.molbiopara.2009.11.005
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发表时间：
2010-03-01
影响因子：
1.5
通讯作者：
Xuan, Xuenan
中科院分区：
文献类型：
--
作者：
Jia, Honglin;Nishikawa, Yoshifumi;Xuan, Xuenan
M17家族亮氨酸氨肽酶（Leucine aminopeptidase，简写为亮氨酸氨肽酶）从肽的N-末端水解氨基酸。许多来自寄生原生动物的LAPS，包括疟原虫、锥虫和利什曼原虫，由于其在寄生虫生物学中的关键作用而被深入研究。在这项研究中，功能性重组弓形虫弓形虫（rTgdR）在大肠杆菌中表达，并确定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bestatin抑制。我们的研究结果表明，Tgl是一种功能性氨肽酶，存在于T.刚地。(C)2009爱思唯尔有限公司版权所有。
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. (C) 2009 Elsevier B.V. All rights reserved.