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

doi:10.1016/j.tetlet.2008.07.149

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 journal › Article › peer-review

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 language	English
Pages (from-to)	5914-5917
Number of pages	4
Journal	Tetrahedron Letters
Volume	49
Issue number	41
DOIs	https://doi.org/10.1016/j.tetlet.2008.07.149
Publication status	Published - 6 Oct 2008

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This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

IONIC LIQUIDS
MYCOBACTERIUM-TUBERCULOSIS
SUBSTRATE
COMPLEX
ENZYME

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

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.",

keywords = "IONIC LIQUIDS, MYCOBACTERIUM-TUBERCULOSIS, SUBSTRATE, COMPLEX, ENZYME",

author = "Czekster, \{Clarissa M.\} and Lapis, \{Alexandre A. M.\} and Souza, \{Gustavo H. M. F.\} and Eberlin, \{Marcos N.\} and Basso, \{Luiz A.\} and Santos, \{Diogenes S.\} and Jairton Dupont and Neto, \{Brenno A. D.\}",

year = "2008",

month = oct,

day = "6",

doi = "10.1016/j.tetlet.2008.07.149",

language = "English",

volume = "49",

pages = "5914--5917",

journal = "Tetrahedron Letters",

issn = "0040-4039",

publisher = "Elsevier",

number = "41",

}

TY - JOUR

T1 - The catalytic mechanism of indole-3-glycerol phosphate synthase (IGPS) investigated by electrospray ionization (tandem) mass spectrometry

AU - Czekster, Clarissa M.

AU - Lapis, Alexandre A. M.

AU - Souza, Gustavo H. M. F.

AU - Eberlin, Marcos N.

AU - Basso, Luiz A.

AU - Santos, Diogenes S.

AU - Dupont, Jairton

AU - Neto, Brenno A. D.

PY - 2008/10/6

Y1 - 2008/10/6

N2 - 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.

AB - 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.

KW - IONIC LIQUIDS

KW - MYCOBACTERIUM-TUBERCULOSIS

KW - SUBSTRATE

KW - COMPLEX

KW - ENZYME

U2 - 10.1016/j.tetlet.2008.07.149

DO - 10.1016/j.tetlet.2008.07.149

M3 - Article

SN - 0040-4039

VL - 49

SP - 5914

EP - 5917

JO - Tetrahedron Letters

JF - Tetrahedron Letters

IS - 41

ER -

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

Abstract

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Keywords

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