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metadata.artigo.dc.title: Molecular modeling of Mycobacterium tuberculosis dUTpase: docking and catalytic mechanism studies
metadata.artigo.dc.creator: Ramalho, Teodorico C.
Caetano, Melissa S.
Josa, Daniela
Luz, Gustavo P.
Freitas, Elisangela A.
Cunha, Elaine F. F. da
metadata.artigo.dc.subject: Mycobacterium tuberculosis
DUTpase enzyme
Theoretical calculations
Enzima dUTPase
Cálculos teóricos
metadata.artigo.dc.publisher: Taylor & Francis 12-Oct-2010
metadata.artigo.dc.identifier.citation: RAMALHO, T. C. et al. Molecular modeling of Mycobacterium tuberculosis dUTpase: docking and catalytic mechanism studies. Journal of Biomolecular Structure and Dynamics, New York, v. 28, n. 6, p. 907-917, 12 Oct. 2010.
metadata.artigo.dc.description.abstract: Mycobacterium tuberculosis is a leading cause of infectious disease in the world today. This outlook is aggravated by a growing number of M. tuberculosis infections in individuals who are immunocompromised as a result of HIV infections. Thus, new and more potent anti-TB agents are necessary. Therefore, dUTpase was selected as a target enzyme to combat M. tuberculosis. In this work, molecular modeling methods involving docking and QM/MM calculations were carried out to investigate the binding orientation and predict binding affinities of some potential dUTpase inhibitors. Our results suggest that the best potential inhibitor investigated, among the compounds studied in this work, is the compound dUPNPP. Regarding the reaction mechanism, we concluded that the decisive stage for the reaction is the stage 1. Furthermore, it was also observed that the compounds with a −1 electrostatic charge presented lower activation energy in relation to the compounds with a −2 charge.
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

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