Understanding the different activities of highly promiscuous MbtI by computational methods
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Altres documents de l'autoria: Ferrer, Silvia; Martí Forés, Sergio; Moliner, Vicent; Tuñón, Iñaki; Bertrán, Juan
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Understanding the different activities of highly promiscuous MbtI by computational methodsData de publicació
2012Editor
Royal Society of ChemistryISSN
1463-9076; 1463-9084Tipus de document
info:eu-repo/semantics/articleVersió de l'editorial
http://pubs.rsc.org/en/content/articlepdf/2012/cp/c2cp23149bVersió
info:eu-repo/semantics/publishedVersionResum
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. [-]
Publicat a
Phys. Chem. Chem. Phys., 2012,14Drets d'accés
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