{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T12:44:41Z","timestamp":1792500281687,"version":"4.5.0"},"reference-count":39,"publisher":"American Society for Microbiology","issue":"17","license":[{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2007,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The recent recrudescence of\n            <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n            infection and the emergence of multidrug-resistant strains have created an urgent need for new therapeutics against tuberculosis. The enzymes of the shikimate pathway are attractive drug targets because this route is absent in mammals and, in\n            <jats:italic>M. tuberculosis<\/jats:italic>\n            , it is essential for pathogen viability. This pathway leads to the biosynthesis of aromatic compounds, including aromatic amino acids, and it is found in plants, fungi, bacteria, and apicomplexan parasites. The\n            <jats:italic>aroB<\/jats:italic>\n            -encoded enzyme dehydroquinate synthase is the second enzyme of this pathway, and it catalyzes the cyclization of 3-deoxy-\n            <jats:sc>d<\/jats:sc>\n            -\n            <jats:italic>arabino<\/jats:italic>\n            -heptulosonate-7-phosphate in 3-dehydroquinate. Here we describe the PCR amplification and cloning of the\n            <jats:italic>aroB<\/jats:italic>\n            gene and the overexpression and purification of its product, dehydroquinate synthase, to homogeneity. In order to probe where the recombinant dehydroquinate synthase was active, genetic complementation studies were performed. The\n            <jats:italic>Escherichia coli<\/jats:italic>\n            AB2847 mutant was used to demonstrate that the plasmid construction was able to repair the mutants, allowing them to grow in minimal medium devoid of aromatic compound supplementation. In addition, homogeneous recombinant\n            <jats:italic>M. tuberculosis<\/jats:italic>\n            dehydroquinate synthase was active in the absence of other enzymes, showing that it is homomeric. These results will support the structural studies with\n            <jats:italic>M. tuberculosis<\/jats:italic>\n            dehydroquinate synthase that are essential for the rational design of antimycobacterial agents.\n          <\/jats:p>","DOI":"10.1128\/jb.00425-07","type":"journal-article","created":{"date-parts":[[2007,6,23]],"date-time":"2007-06-23T01:12:59Z","timestamp":1182561179000},"page":"6246-6252","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["Functional Characterization by Genetic Complementation of\n            <i>aroB<\/i>\n            -Encoded Dehydroquinate Synthase from\n            <i>Mycobacterium tuberculosis<\/i>\n            H37Rv and Its Heterologous Expression and Purification"],"prefix":"10.1128","volume":"189","author":[{"given":"Jordana Dutra","family":"de Mendonc\u0327a","sequence":"first","affiliation":[{"name":"Centro de Pesquisas em Biologia Molecular e Funcional, Pontifi\u0301cia Universidade Cato\u0301lica do Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fernanda","family":"Ely","sequence":"additional","affiliation":[{"name":"Centro de Pesquisas em Biologia Molecular e Funcional, Pontifi\u0301cia Universidade Cato\u0301lica do Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mario Sergio","family":"Palma","sequence":"additional","affiliation":[{"name":"Laborato\u0301rio de Biologia Estrutural e Zooqui\u0301mica, Centro de Estudos de Insetos Sociais, Departamento de Biologia, Instituto de Biocie\u0302ncias, Universidade Estadual Paulista, Rio Claro, Sa\u0303o Paulo 13506-900"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeverson","family":"Frazzon","sequence":"additional","affiliation":[{"name":"Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 91501-970, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiz Augusto","family":"Basso","sequence":"additional","affiliation":[{"name":"Centro de Pesquisas em Biologia Molecular e Funcional, Pontifi\u0301cia Universidade Cato\u0301lica do Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dio\u0301genes Santiago","family":"Santos","sequence":"additional","affiliation":[{"name":"Centro de Pesquisas em Biologia Molecular e Funcional, Pontifi\u0301cia Universidade Cato\u0301lica do Rio Grande do Sul, Porto Alegre, Rio Grande do Sul 90619-900"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","first-page":"393","volume":"2","year":"2005","unstructured":"Basso, L. 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