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DXS as a target for structure-based drug design.
Gierse, Robin Matthias; Redeem, Eswar; Diamanti, Eleonora; Wrenger, Carsten; Groves, Matthew R; Hirsch, Anna Kh.
Affiliation
  • Gierse RM; Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
  • Redeem E; Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
  • Diamanti E; Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
  • Wrenger C; Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil.
  • Groves MR; Structural Biology Unit, Drug Design, Department of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
  • Hirsch AK; Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
Future Med Chem ; 9(11): 1277-1294, 2017 07.
Article in En | MEDLINE | ID: mdl-28636418
ABSTRACT
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Transferases / Anti-Bacterial Agents / Antiprotozoal Agents Limits: Humans Language: En Journal: Future Med Chem Year: 2017 Document type: Article Affiliation country: Netherlands

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Transferases / Anti-Bacterial Agents / Antiprotozoal Agents Limits: Humans Language: En Journal: Future Med Chem Year: 2017 Document type: Article Affiliation country: Netherlands