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

Keywords

IONIC LIQUIDS
MYCOBACTERIUM-TUBERCULOSIS
SUBSTRATE
COMPLEX
ENZYME

UN SDGs

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

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10.1016/j.tetlet.2008.07.149

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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 = "PERGAMON-ELSEVIER SCIENCE LTD",

number = "41",

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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

Keywords

UN SDGs

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