Combining carbochips and mass spectrometry to study the donor specificity for the Neisseria meningitidis β1,3-N-acetylglucosaminyltransferase LgtA

Wanyi Guan, Lan Ban, Li Cai, Lei Li, Wenlan Chen, Xianwei Liu, Milan Mrksich, Peng George Wang*

*Corresponding author for this work

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

A library of 11 UDP-N-acetylglucosamine analogs were rapidly screened for their activities as donors for the Neisseria meningitidis β1,3-N- acetylglucosaminyltransferase (LgtA) by direct on-chip reaction and detection with SAMDI-TOF mass spectrometry. Six of the analogs were active in this assay and were analyzed by SAMDI to characterize the kinetics toward LgtA. The analysis revealed that substitutions on C-2, C-4, and C-6 affect the activity of the donors, with bulky groups at these positions decreasing affinity of the donors for the enzyme, and also revealed that activity is strongly affected by the stereochemistry at C-3, but not C-4, of the donor. The study is also significant because it demonstrates that SAMDI can be used to both profile glycosyltransferase activities and to provide a quantitative assessment of enzyme activity.

Original languageEnglish (US)
Pages (from-to)5025-5028
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume21
Issue number17
DOIs
StatePublished - Sep 1 2011

Keywords

  • Carbohydrate array
  • Glycosyltransferase
  • MALDI TOF MS
  • Unnatural sugar nucleotides

ASJC Scopus subject areas

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

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