| Literature DB >> 25906160 |
Miroslav Brecik1, Ivana Centárová1, Raju Mukherjee2, Gaëlle S Kolly2, Stanislav Huszár1, Adela Bobovská1, Emöke Kilacsková1, Veronika Mokošová1, Zuzana Svetlíková1, Michal Šarkan1, João Neres2, Jana Korduláková1, Stewart T Cole2, Katarína Mikušová1.
Abstract
The flavo-enzyme DprE1 catalyzes a key epimerization step in the decaprenyl-phosphoryl d-arabinose (DPA) pathway, which is essential for mycobacterial cell wall biogenesis and targeted by several new tuberculosis drug candidates. Here, using differential radiolabeling with DPA precursors and high-resolution fluorescence microscopy, we disclose the unexpected extracytoplasmic localization of DprE1 and periplasmic synthesis of DPA. Collectively, this explains the vulnerability of DprE1 and the remarkable potency of the best inhibitors.Entities:
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Year: 2015 PMID： 25906160 DOI： 10.1021/acschembio.5b00237
Source DB: PubMed Journal: ACS Chem Biol ISSN： 1554-8929 Impact factor: 5.100