| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5274169 | Tetrahedron Letters | 2008 | 4 Pages |
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.
Graphical abstractThe catalytic mechanism indole ring closure promoted by IGPS enzyme was studied by ESI mass spectrometry.Download full-size image
