Gierse Robin Matthias, Redeem Eswar, Diamanti Eleonora, Wrenger Carsten, Groves Matthew R, Hirsch Anna Kh
Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil.
Future Med Chem. 2017 Jul;9(11):1277-1294. doi: 10.4155/fmc-2016-0239. Epub 2017 Jun 21.
In this review, we analyze the enzyme DXS, the first and rate-limiting protein in the methylerythritol 4-phosphate pathway. This pathway was discovered in 1996 and is one of two known metabolic pathways for the biosynthesis of the universal building blocks for isoprenoids. It promises to offer new targets for the development of anti-infectives against the human pathogens, malaria or tuberculosis. We mapped the sequence conservation of 1-deoxy-xylulose-5-phosphate synthase on the protein structure and analyzed it in comparison with previously identified druggable pockets. We provide a recent overview of known inhibitors of the enzyme. Taken together, this sets the stage for future structure-based drug design.
在本综述中,我们分析了1-脱氧-D-木酮糖-5-磷酸合酶(DXS),它是甲基赤藓糖醇4-磷酸途径中的首个且限速的蛋白质。该途径于1996年被发现,是类异戊二烯通用构建模块生物合成的两种已知代谢途径之一。它有望为开发针对人类病原体(疟疾或结核病)的抗感染药物提供新靶点。我们绘制了1-脱氧-D-木酮糖-5-磷酸合酶在蛋白质结构上的序列保守性,并与先前确定的可成药口袋进行比较分析。我们提供了该酶已知抑制剂的最新综述。综上所述,这为未来基于结构的药物设计奠定了基础。