The catalytic mechanism of indole-3-glycerol phosphate synthase (IGPS) investigated by electrospray ionization (tandem) mass spectrometry
| Autor: | Brenno A. D. Neto, Luiz Augusto Basso, Diógenes Santiago Santos, Jairton Dupont, Marcos N. Eberlin, Clarissa M. Czekster, Gustavo H.M.F. Souza, Alexandre A. M. Lapis |
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| Rok vydání: | 2008 |
| Předmět: |
chemistry.chemical_classification
Chromatography ATP synthase biology Electrospray ionization Organic Chemistry Tryptophan Indole-3-Glycerol-Phosphate Synthase Tandem mass spectrometry Phosphate Mass spectrometry Biochemistry chemistry.chemical_compound Enzyme chemistry Drug Discovery biology.protein |
| Zdroj: | Tetrahedron Letters. 49:5914-5917 |
| ISSN: | 0040-4039 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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