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http://purl.uniprot.org/citations/11483005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11483005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11483005http://www.w3.org/2000/01/rdf-schema#comment"Tuberculosis (TB) resurged in the late 1980s and an estimated 1.87 million people died of TB in 1997. The reemergence of tuberculosis as a public health threat, the high susceptibility of HIV-infected persons, and the proliferation of multidrug-resistant strains have created a need to develop new antimycobacterial agents. The existence of a shikimate pathway has been predicted by the determination of the genome sequence of Mycobacterium tuberculosis. The M. tuberculosis aroK-encoded shikimate kinase and aroA-encoded 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase were cloned and the enzymes overexpressed in soluble form. Overexpression was achieved without isopropyl beta-d-thiogalactoside induction, and cells grown to stationary phase yielded approximately 30% of target proteins to total soluble cell proteins. Enzyme activity measurements using coupled assays demonstrated that there was a 328-fold increase in specific activity for shikimate kinase and 101-fold increase for EPSP synthase."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.org/dc/terms/identifier"doi:10.1006/prep.2001.1457"xsd:string
http://purl.uniprot.org/citations/11483005http://purl.org/dc/terms/identifier"doi:10.1006/prep.2001.1457"xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Oliveira J.S."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Oliveira J.S."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Basso L.A."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Basso L.A."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Santos D.S."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Santos D.S."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Pinto C.A."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/author"Pinto C.A."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/name"Protein Expr. Purif."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/name"Protein Expr. Purif."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/pages"430-435"xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/pages"430-435"xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/title"Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/title"Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis."xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/11483005http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/11483005http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11483005
http://purl.uniprot.org/citations/11483005http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11483005