Expression and Characterization of Soluble 4-Diphosphocytidyl-2-C-methyl-D-erythritol Kinase from Bacterial Pathogens

Hyungjin Eoh, Prabagaran Narayanasamy, Amanda C. Brown, Tanya Parish, Patrick J. Brennan, Dean C. Crick

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Many bacterial pathogens utilize the 2-C-methyl-D-erythritol 4-phosphate pathway for biosynthesizing isoprenoid precursors, a pathway that is vital for bacterial survival and absent from human cells, providing a potential source of drug targets. However, the characterization of 4-diphosphocytidyl-2-C-methyl-D-erythritol (CDP-ME) kinase (IspE) has been hindered due to a lack of enantiopure CDP-ME and difficulty in obtaining pure IspE. Here, enantiopure CDP-ME was chemically synthesized and recombinant IspE from bacterial pathogens were purified and characterized. Although gene disruption was not possible in Mycobacterium tuberculosis, IspE is essential in Mycobacterium smegmatis. The biochemical and kinetic characteristics of IspE provide the basis for development of a high throughput screen and structural characterization.

Original languageEnglish (US)
Pages (from-to)1230-1239
Number of pages10
JournalChemistry and Biology
Volume16
Issue number12
DOIs
StatePublished - Dec 24 2009

Keywords

  • CHEMBIO
  • MICROBIO

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry

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