The catalytic mechanism of indole-3-glycerol phosphate synthase (IGPS) investigated by electrospray ionization (tandem) mass spectrometry

Clarissa M. Czekster, Alexandre A. M. Lapis, Gustavo H. M. F. Souza, Marcos N. Eberlin, Luiz A. Basso, Diogenes S. Santos, Jairton Dupont, Brenno A. D. Neto

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

An enzymatic reaction has been monitored by on-line direct infusion electrospray ionization (tandem) mass spectrometry. Using this fast and sensitive technique, a key and transient intermediate of Mycobacterium tuberculosis indole-3-glycerol phosphate synthase (IGPS)-catalyzed reaction has been trapped. The reaction catalyzed by indole-3 -glycerol phosphate synthase is part of the tryptophan biosynthetic pathway, and is not present in mammals, including humans. This peculiarity renders this enzyme a potential target for the development of biospecific agents with potential anti-TB activity. The present results indicate the presence of two intermediates in the mechanism of this enzymatic reaction. (C) 2008 Elsevier Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)5914-5917
Number of pages4
JournalTetrahedron Letters
Volume49
Issue number41
DOIs
Publication statusPublished - 6 Oct 2008

Keywords

  • IONIC LIQUIDS
  • MYCOBACTERIUM-TUBERCULOSIS
  • SUBSTRATE
  • COMPLEX
  • ENZYME

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