Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin Article

Kim, DH, Lees, WJ, Kempsell, KE et al. (1996). Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin . BIOCHEMISTRY, 35(15), 4923-4928. 10.1021/bi952937w

Industry Collaboration International Collaboration

cited authors

  • Kim, DH; Lees, WJ; Kempsell, KE; Lane, WS; Duncan, K; Walsh, CT

sustainable development goals

authors

publication date

  • April 16, 1996

published in

keywords

  • ACTIVE-SITE
  • Biochemistry & Molecular Biology
  • Life Sciences & Biomedicine
  • MECHANISM
  • PATHWAY
  • PH
  • PHOSPHONOMYCIN
  • PROLINE RACEMASE
  • RESIDUES
  • STRUCTURAL ELUCIDATION
  • Science & Technology
  • TETRAHEDRAL INTERMEDIATE

Digital Object Identifier (DOI)

publisher

  • AMER CHEMICAL SOC

start page

  • 4923

end page

  • 4928

volume

  • 35

issue

  • 15