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

Jessica M. Smith; Ryan J. Vierling; Caren Freel Meyers

doi:10.1039/c1md00233c

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

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

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 language	English (US)
Pages (from-to)	65-67
Number of pages	3
Journal	MedChemComm
Volume	3
Issue number	1
DOIs	https://doi.org/10.1039/c1md00233c
State	Published - Jan 2012

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Pharmacology
Pharmaceutical Science
Drug Discovery
Organic Chemistry

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10.1039/c1md00233c

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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.",

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N2 - 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.

AB - 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.

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UR - https://www.scopus.com/pages/publications/84862958712#tab=citedBy

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M3 - Article

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

Abstract

ASJC Scopus subject areas

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