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Cloning and characterization of the Plasmodium falciparum adenylosuccinate synthetase gene

机译:恶性疟原虫腺苷琥珀酸合成酶基因的克隆与鉴定

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Parasitic protozoa lack the de novo purine biosynthetic pathway and rely exclusively on the salvage pathway for their purine nucleotide requirements(1) Purine salvage enzymes are therefore potential chemotherapeutic targets, This paper reports the cloning and deduced amino acid sequence of Plasmodium falciparum adenylosuccinate synthetase (PfADSS), an enzyme involved in purine salvage. PfADSS exhibits 67% homology with that of the human enzyme. On expression in E. coli, enzymatically active ADSS was produced as deduced by functional complementation analysis. The PfADSS activity was shown to be inhibited by hadacidin, a known competitive inhibitor of this enzyme. [References: 38]
机译:寄生虫原生动物缺乏从头嘌呤的生物合成途径,并且仅依赖于挽救途径来满足其嘌呤核苷酸需求(1),因此,嘌呤挽救酶是潜在的化学治疗靶标。 ),一种参与嘌呤挽救的酶。 PfADSS与人类酶的同源性为67%。在大肠杆菌中表达后,通过功能互补分析推导产生了具有酶活性的ADSS。 PfADSS活性显示已被该酶的竞争性抑制剂哈达酸抑制。 [参考:38]

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