Selective inhibition of E. coli 1-deoxy-d-xylulose-5-phosphate synthase by acetylphosphonates

Jessica M. Smith, Ryan J. Vierling, Caren L Meyers

Research output: Contribution to journalArticle

Abstract

DXP synthase catalyzes the formation of 1-deoxy-d-xylulose 5-phosphate, an essential precursor in pathogen isoprenoid biosynthesis. The selective inhibition of this ThDP-dependent transformation is a challenging goal in the development of isoprenoid biosynthesis inhibitors. Potent, selective inhibitors could lead to new anti-infective agents. Here, we demonstrate selective inhibition of E. coli DXP synthase by butylacetylphosphonate.

Original languageEnglish (US)
Pages (from-to)65-67
Number of pages3
JournalMedChemComm
Volume3
Issue number1
DOIs
StatePublished - 2012

Fingerprint

Biosynthesis
Terpenes
Escherichia coli
Pathogens
Anti-Infective Agents
xylulose-5-phosphate
deoxyxylulose-5-phosphate synthase
phosphonoacetaldehyde
butylacetylphosphonate

ASJC Scopus subject areas

  • Biochemistry
  • Pharmaceutical Science

Cite this

Selective inhibition of E. coli 1-deoxy-d-xylulose-5-phosphate synthase by acetylphosphonates. / Smith, Jessica M.; Vierling, Ryan J.; Meyers, Caren L.

In: MedChemComm, Vol. 3, No. 1, 2012, p. 65-67.

Research output: Contribution to journalArticle

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