| RESEARCH |
Scientists studying how Streptococcus pneumoniae regulates the production of isoprenoids have identified a promising new strategy for designing antibiotics to combat this pneumonia-causing bacterium. S. pneumoniae kills more than 3,700 people each day worldwide, and "the threat of multiple-antibiotic-resistant strains of this organism has never been greater," says Thomas S. Leyh of Albert Einstein College of Medicine. Leyh notes that S. pneumoniae makes the isoprenoids it needs to survive from isopentenyl diphosphate, the end product of the mevalonate pathway: Mevalonate is doubly phosphorylated to produce diphosphomevalonate (shown), which is then decarboxylated to yield isopentenyl diphosphate. Upon closer examination of this pathway, Leyh found that diphosphomevalonate potently inhibits the enzyme that carries out the initial phosphorylation of mevalonate by binding to an allosteric site distinct from the enzyme's active site [Biochemistry, published online Dec. 4, http://dx.doi.org/10.1021/bi048075t]. The human version of this enzyme is not inhibited by diphosphomevalonate, indicating that the allosteric site is a promising target for the design of new antimicrobials, he says. |
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