| pubmed-article:17921290 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17921290 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:17921290 | lifeskim:mentions | umls-concept:C0026926 | lld:lifeskim |
| pubmed-article:17921290 | lifeskim:mentions | umls-concept:C0872152 | lld:lifeskim |
| pubmed-article:17921290 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:17921290 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:17921290 | pubmed:dateCreated | 2007-12-6 | lld:pubmed |
| pubmed-article:17921290 | pubmed:abstractText | Mycobacterium tuberculosis utilizes the methylerythritol phosphate (MEP) pathway for biosynthesis of isopentenyl diphosphate and its isomer, dimethylallyl diphosphate, precursors of all isoprenoid compounds. This pathway is of interest as a source of new drug targets, as it is absent from humans and disruption of the responsible genes has shown a lethal phenotype for Escherichia coli. In the MEP pathway, 4-diphosphocytidyl-2-C-methyl-D-erythritol is formed from 2-C-methyl-D-erythritol 4-phosphate (MEP) and CTP in a reaction catalyzed by a 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase (IspD). In the present work, we demonstrate that Rv3582c is essential for M. tuberculosis: Rv3582c has been cloned and expressed, and the encoded protein has been purified. The purified M. tuberculosis IspD protein was capable of catalyzing the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol in the presence of MEP and CTP. The enzyme was active over a broad pH range (pH 6.0 to 9.0), with peak activity at pH 8.0. The activity was absolutely dependent upon divalent cations, with 20 mM Mg2+ being optimal, and replacement of CTP with other nucleotide 5'-triphosphates did not support activity. Under the conditions tested, M. tuberculosis IspD had Km values of 58.5 microM for MEP and 53.2 microM for CTP. Calculated kcat and kcat/Km values were 0.72 min(-1) and 12.3 mM(-1) min(-1) for MEP and 1.0 min(-1) and 18.8 mM(-1) min(-1) for CTP, respectively. | lld:pubmed |
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| pubmed-article:17921290 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17921290 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17921290 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17921290 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17921290 | pubmed:issn | 1098-5530 | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:HunterWilliam... | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:BrennanPatric... | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:BuetowLoriL | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:CrickDean CDC | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:ParishTanyaT | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:KaurDevinderD | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:BrownAmanda... | lld:pubmed |
| pubmed-article:17921290 | pubmed:author | pubmed-author:EohHyungjinH | lld:pubmed |
| pubmed-article:17921290 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17921290 | pubmed:volume | 189 | lld:pubmed |
| pubmed-article:17921290 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17921290 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17921290 | pubmed:pagination | 8922-7 | lld:pubmed |
| pubmed-article:17921290 | pubmed:dateRevised | 2011-5-5 | lld:pubmed |
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| pubmed-article:17921290 | pubmed:meshHeading | pubmed-meshheading:17921290... | lld:pubmed |
| pubmed-article:17921290 | pubmed:meshHeading | pubmed-meshheading:17921290... | lld:pubmed |
| pubmed-article:17921290 | pubmed:meshHeading | pubmed-meshheading:17921290... | lld:pubmed |
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| pubmed-article:17921290 | pubmed:meshHeading | pubmed-meshheading:17921290... | lld:pubmed |
| pubmed-article:17921290 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17921290 | pubmed:articleTitle | Characterization of the Mycobacterium tuberculosis 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase: potential for drug development. | lld:pubmed |
| pubmed-article:17921290 | pubmed:affiliation | Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA. | lld:pubmed |
| pubmed-article:17921290 | pubmed:publicationType | Journal Article | lld:pubmed |
