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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/68140
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dc.contributor.authorRizzi, Caroline-
dc.contributor.authorPalma, Mario Sergio-
dc.contributor.authorSantos, Diógenes S.-
dc.contributor.authorBasso, Luiz A.-
dc.contributor.authorFrazzon, Jeverson-
dc.contributor.authorEly, Fernanda-
dc.contributor.authorWeber, Patrícia G.-
dc.contributor.authorFonseca, Isabel O. da-
dc.contributor.authorGallas, Michelle-
dc.contributor.authorOliveira, Jaim S.-
dc.contributor.authorMendes, Maria A.-
dc.contributor.authorSouza, Bibiana M. de-
dc.date.accessioned2014-05-27T11:21:17Z-
dc.date.accessioned2016-10-25T18:20:30Z-
dc.date.available2014-05-27T11:21:17Z-
dc.date.available2016-10-25T18:20:30Z-
dc.date.issued2005-03-01-
dc.identifierhttp://dx.doi.org/10.1016/j.pep.2004.06.040-
dc.identifier.citationProtein Expression and Purification, v. 40, n. 1, p. 23-30, 2005.-
dc.identifier.issn1046-5928-
dc.identifier.urihttp://hdl.handle.net/11449/68140-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/68140-
dc.description.abstractTuberculosis (TB), caused by Mycobacterium tuberculosis, remains the leading cause of mortality due to a bacterial pathogen. According to the 2004 Global TB Control Report of the World Health Organization, there are 300,000 new cases per year of multi-drug resistant strains (MDR-TB), defined as resistant to isoniazid and rifampicin, and 79% of MDR-TB cases are now super strains, resistant to at least three of the four main drugs used to treat TB. Thus there is a need for the development of effective new agents to treat TB. The shikimate pathway is an attractive target for the development of antimycobacterial agents because it has been shown to be essential for the viability of M. tuberculosis, but absent from mammals. The M. tuberculosis aroG-encoded 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (mtDAHPS) catalyzes the first committed step in this pathway. Here we describe the PCR amplification, cloning, and sequencing of aroG structural gene from M. tuberculosis H37Rv. The expression of recombinant mtDAHPS protein in the soluble form was obtained in Escherichia coli Rosetta-gami (DE3) host cells without IPTG induction. An approximately threefold purification protocol yielded homogeneous enzyme with a specific activity value of 0.47 U mg-1 under the experimental conditions used. Gel filtration chromatography results demonstrate that recombinant mtDAHPS is a pentamer in solution. The availability of homogeneous mtDAHPS will allow structural and kinetics studies to be performed aiming at antitubercular agents development. © 2004 Elsevier Inc. All rights reserved.en
dc.format.extent23-30-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectDAHP synthase-
dc.subjectMycobacterium tuberculosis-
dc.subjectProtein expression-
dc.subjectShikimate pathway-
dc.subject2 dehydro 3 deoxyphosphoheptonate aldolase-
dc.subjectrecombinant protein-
dc.subjectenzymology-
dc.subjectgenetics-
dc.subjectisolation and purification-
dc.subjectmass spectrometry-
dc.subjectmetabolism-
dc.subjectmolecular cloning-
dc.subjectmolecular genetics-
dc.subjectnucleotide sequence-
dc.subject3-Deoxy-7-Phosphoheptulonate Synthase-
dc.subjectBase Sequence-
dc.subjectCloning, Molecular-
dc.subjectMass Spectrometry-
dc.subjectMolecular Sequence Data-
dc.subjectRecombinant Proteins-
dc.subjectBacteria (microorganisms)-
dc.subjectEscherichia coli-
dc.subjectMammalia-
dc.subjectMycobacterium-
dc.subjectTrixis-
dc.titleDAHP synthase from Mycobacterium tuberculosis H37Rv: Cloning, expression, and purification of functional enzymeen
dc.typeoutro-
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)-
dc.description.affiliationDepto. Biol. Molec. e Biotecnologia Univ. Federal Do Rio Grande Do Sul, Porto Alegre, RS 91501-970-
dc.description.affiliationDepto. de Ciê. Dos Alimentos Univ. Federal Do Rio Grande Do Sul, Porto Alegre, RS 91501-970-
dc.description.affiliationDepartamento de Biologia/CEIS Univ. Do Estado de São Paulo, Rio Claro, SP 13506-900-
dc.description.affiliationCtro. Pesquisa Desenvolvimento B. Pont. Univ. Catol. Rio Grande Do Sul, Porto Alegre, RS 90619-900-
dc.identifier.doi10.1016/j.pep.2004.06.040-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofProtein Expression and Purification-
dc.identifier.scopus2-s2.0-13844272205-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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