Trypanosoma are blood-borne parasites and are the causative agents of neglected tropical diseases (NTDs) affecting both humans and animals. These parasites mainly rely on glycolysis for their energy production within the mammalian host, which is why trypanosomal glycolytic enzymes have been pursued as interesting targets for the development of trypanocidal drugs. The structure–function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania) have been well-studied within this context. In this paper, we describe the structural and enzymatic characterization of PYK from T. congolense (TcoPYK), the main causative agent of Animal African Trypanosomosis (AAT), by employing a combination of enzymatic assays, thermal unfolding studies and X-ray crystallography.

锥虫是血液传播的寄生虫，是影响人类和动物的被忽视热带病 (NTD) 的病原体。这些寄生虫主要依靠糖酵解在哺乳动物宿主内产生能量，这就是为什么将锥虫糖酵解酶作为开发杀锥虫药物的有趣目标的原因。来自锥虫（锥虫和利什曼原虫）的丙酮酸激酶 (PYK) 的结构-功能关系已在此背景下得到充分研究。在本文中，我们描述了来自刚果锥虫( Tco ) 的PYK的结构和酶学特征。PYK)，非洲动物锥虫病 (AAT) 的主要病原体，通过结合酶分析、热展开研究和 X 射线晶体学。