Baig M S, Gangwar S, Goyal N
Central Drug Research Institute, Division of Biochemistry, Lucknow, India.
Cell Mol Biol (Noisy-le-grand). 2011 Feb 12;57(1):56-61.
The incidence of parasitic infection, leishmaniasis, has been steadily increasing worldwide. Since, the existing chemotherapy of these diseases suffers from lack of safe and effective drugs and/or the presence of widespread drug resistance, there is an urgent need for development of potent, mechanism-based anti-parasitic agents. The peptidases of protozoan parasites are becoming increasingly important for their role in parasite survival and pathogenecity. Leishmania donovani dipeptidylcarboxypeptidsae (LdDCP), an angiotensin converting enzyme (ACE) related metallopeptidase has been identified and characterized as a putative drug target for antileishmanial chemotherapy. The kinetic parameters for LdDCP with substrate, Hip-His-Leu were determined as, Km, 4 mM and Vmax, 1.173 μmole/ml/min. The enzyme was more sensitive to 1,10 phenanthroline than EDTA and was 80% inhibited in presence of NaCl. Among various protease inhibitors, pepstatin was found as potent inhibitor of LdDCP.
寄生虫感染疾病利什曼病在全球范围内的发病率一直在稳步上升。由于这些疾病现有的化疗方法存在缺乏安全有效的药物和/或广泛存在耐药性的问题，因此迫切需要开发强效的、基于作用机制的抗寄生虫药物。原生动物寄生虫的肽酶因其在寄生虫存活和致病性中的作用而变得越来越重要。杜氏利什曼原虫二肽基羧肽酶（LdDCP），一种与血管紧张素转换酶（ACE）相关的金属肽酶，已被鉴定并表征为抗利什曼原虫化疗的潜在药物靶点。LdDCP与底物Hip-His-Leu的动力学参数测定为：Km为4 mM，Vmax为1.173微摩尔/毫升/分钟。该酶对1,10-菲咯啉比对EDTA更敏感，在有NaCl存在的情况下被抑制80%。在各种蛋白酶抑制剂中，胃蛋白酶抑制剂被发现是LdDCP的强效抑制剂。
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