Chorismate synthase (Cs) is the last enzyme of the main trunk of shikimate pathway and catalyzes formation of chorismate, a major aromatic metabolite precursor. We have previously reported that Cs is highly conserved across different Plasmodium sp. Here we report that Cs from malaria parasites are bifunctional enzymes through expression and functional studies of two recombinant proteins rPfCs (Cs from P. falciparum) and rPvCs (Cs from P. vivax). We confirm bifunctional activity of both rPfCs and rPvCs based on their ability to catalyze formation of chorismate under aerobic conditions as well as their ability to catalyze generation of reduced flavin mononucleotide (FMN) as assessed through diaphorase assay.

分支酸合酶（Cs）是sh草酸途径的主要干线中的最后一种酶，可催化分支糖酸（一种主要的芳香代谢产物前体）的形成。我们以前曾报道过，Cs在不同的疟原虫种之间高度保守。在这里，我们报告通过两个重组蛋白rPfCs（恶性疟原虫的Cs ）和rPvCs（间日疟原虫的Cs）的表达和功能研究，来自疟原虫的Cs是双功能酶。我们通过rPfCs和rPvCs在有氧条件下催化形成分支酸盐的能力以及通过黄递酶分析评估的催化黄素单核苷酸（FMN）还原的能力来确认rPfCs和rPvCs的双功能活性。