Author/Authors :
Czekster، نويسنده , , Clarissa M. and Lapis، نويسنده , , Alexandre A.M. and Souza، نويسنده , , Gustavo H.M.F. and Eberlin، نويسنده , , Marcos N. and Basso، نويسنده , , Luiz A. P. Santos، نويسنده , , Di?genes S. and Dupont، نويسنده , , Ja?¨rton and Neto، نويسنده , , Brenno A.D.، نويسنده ,
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.
