Understanding the different activities of highly promiscuous MbtI by computational methods
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Otros documentos de la autoría: Ferrer, Silvia; Martí Forés, Sergio; Moliner, Vicent; Tuñón, Iñaki; Bertrán, Juan
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http://dx.doi.org/10.1039/c2cp23149b |
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Título
Understanding the different activities of highly promiscuous MbtI by computational methodsFecha de publicación
2012Editor
Royal Society of ChemistryISSN
1463-9076; 1463-9084Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://pubs.rsc.org/en/content/articlepdf/2012/cp/c2cp23149bVersión
info:eu-repo/semantics/publishedVersionResumen
Salicylate synthase from Mycobacterium tuberculosis, MbtI, is a highly promiscuous Mg2+
dependent enzyme with up to four distinct activities detected in vitro: isochorismate synthase (IS),
isochorismate pyruvate ... [+]
Salicylate synthase from Mycobacterium tuberculosis, MbtI, is a highly promiscuous Mg2+
dependent enzyme with up to four distinct activities detected in vitro: isochorismate synthase (IS),
isochorismate pyruvate lyase (IPL), salicylate synthase (SS) and chorismate mutase (CM). In this
paper, Molecular Dynamic (MD) simulations employing hybrid quantum mechanics/molecular
mechanics (QM/MM) potentials have been carried out to get a detailed knowledge of the IS and
the IPL activities at the molecular level. According to our simulations, the architecture of the MbtI
active site allows catalyzing the two reactions: the isochorismate formation, by means of a stepwise
mechanism, and the salicylate production from isochorismate, that appears to be pericyclic in
nature. Findings also explain the role of the magnesium cation and the pH dependence activity
experimentally observed in MbtI. Mg2+ would be polarizing and pre-organizing the substrate and
active site, as well as shifting the pKa values of key active site residues. [-]
Publicado en
Phys. Chem. Chem. Phys., 2012,14Derechos de acceso
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