Identification of a UDP-Gal: GlcNAc-R galactosyltransferase activity in Escherichia coli VW187

Pedro J Montoya-Peleaz, John G Riley, Walter A Szarek, Miguel A Valvano, John S Schutzbach, Inka Brockhausen

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)


A novel acceptor substrate for galactosyltransferase was synthesized containing GlcNAcalpha-pyrophosphate, covalently bound to a hydrophobic phenoxyundecyl moiety (GlcNAc alpha-O-PO(3)-PO(3)-(CH(2))(11)-O-Phenyl). The new substrate was used to develop an assay for a galactosyltransferase activity from Escherichia coli strain VW187 that is involved in lipopolysaccharide synthesis and has not been studied by others. We showed that Gal was transferred from UDP-Gal to the novel acceptor substrate. This was a significant improvement over our previous preliminary assays of the enzyme using endogenous substrate, and showed that these synthetic substrates are useful for assaying enzymes that utilize lipid-bound substrates in O-chain synthesis in Gram-negative bacteria.
Original languageEnglish
Pages (from-to)1205-11
Number of pages7
JournalBioorganic & Medicinal Chemistry Letters
Issue number4
Publication statusPublished - 15 Feb 2005

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science


Dive into the research topics of 'Identification of a UDP-Gal: GlcNAc-R galactosyltransferase activity in Escherichia coli VW187'. Together they form a unique fingerprint.

Cite this