Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23)

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dc.contributor.authorNunes, Jose E. S.
dc.contributor.authorDucati, Rodrigo G.
dc.contributor.authorBreda, Ardala
dc.contributor.authorRosado, Leonardo A.
dc.contributor.authorde Souza, Bibiana M. [UNESP]
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorSantos, Diogenes S.
dc.contributor.authorBasso, Luiz A.
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:54:59Z
dc.date.available2014-05-20T13:54:59Z
dc.date.issued2011-08-15
dc.description.abstractThe emergence of drug-resistant strains of Mycobacterium tuberculosis, the major causative agent of tuberculosis (TB), and the deadly HIV-TB co-infection have led to an urgent need for the development of new anti-TB drugs. The histidine biosynthetic pathway is present in bacteria, archaebacteria, lower eukaryotes and plants, but is absent in mammals. Disruption of the hisD gene has been shown to be essential for M. tuberculosis survival. Here we present cloning, expression and purification of recombinant hisD-encoded histidinol dehydrogenase (MtHisD). N-terminal amino acid sequencing and electrospray ionization mass spectrometry analyses confirmed the identity of homogeneous MtHisD. Analytical gel filtration, metal requirement analysis, steady-state kinetics and isothermal titration calorimetry data showed that homodimeric MtHisD is a metalloprotein that follows a Bi Uni Uni Bi Ping-Pong mechanism. pH-rate profiles and a three-dimensional model of MtHisD allowed proposal of amino acid residues involved in either catalysis or substrate(s) binding. (C) 2011 Elsevier B.V. All rights reserved.en
dc.description.affiliationPontificia Univ Catolica Grande Sul PUCRS, CPBMF, INCT TB, BR-90619900 Porto Alegre, RS, Brazil
dc.description.affiliationPontificia Univ Catolica Rio Grande do Sul, Programa Posgrad Biol Celular & Mol, Porto Alegre, RS, Brazil
dc.description.affiliationUniv Estadual Paulista UNESP, Inst Biociencias Rio Clara, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista UNESP, Inst Biociencias Rio Clara, BR-13506900 Rio Claro, SP, Brazil
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipBanco Nacional de Desenvolvimento Econômico e Social (BNDES)
dc.description.sponsorshipIdCNPq: 304051/1975-06
dc.description.sponsorshipIdCNPq: 520182/99-5
dc.format.extent143-153
dc.identifierhttp://dx.doi.org/10.1016/j.abb.2011.05.020
dc.identifier.citationArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 512, n. 2, p. 143-153, 2011.
dc.identifier.doi10.1016/j.abb.2011.05.020
dc.identifier.fileWOS000293258700004.pdf
dc.identifier.issn0003-9861
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19671
dc.identifier.wosWOS:000293258700004
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.relation.ispartofjcr3.118
dc.relation.ispartofsjr1,350
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectHistidinol dehydrogenaseen
dc.subjectMycobacterium tuberculosisen
dc.subjectMetalloenzymeen
dc.subjectThermodynamic binding parametersen
dc.subjectEnzyme mechanismen
dc.subjectMolecular modelen
dc.titleMolecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23)en
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0002-7363-8211[6]
unesp.author.orcid0000-0003-0903-2407[8]
unesp.author.orcid0000-0002-4349-0244[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Rio Claropt

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Artigos - Biologia - IBRC