MEDI 161 |
| Lumazine synthase and riboflavin synthase catalyze the last two steps in the biosynthesis of riboflavin (Scheme 1), a vitamin that is involved in many critical biochemical reactions that are essential for maintenance of life. The inhibition of these enzymes represents a very specific strategy for antibiotic drug design, because the targets are not present in human or animal hosts. The detailed mechanisms of lumazine synthase and riboflavin synthase catalysis are not completely known. In order to elucidate these mechanisms, metabolically stable structural probes have been designed based on hypothetical reaction mechanisms and molecular modeling. Replacement of nitrogen of the ribitylamine side chain with oxygen (O-nucleoside), sulfur (S-nucleoside) or an alkene linkage would not be expected to produce gross changes in the orientation of ribityl chain, and the resulting compounds could possibly bind to lumazine synthase. They obviously could not complete the catalytic cycle. The interactions could be studied by enzyme kinetics, X-ray diffraction and NMR. |
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General Poster Session
7:00 PM-9:00 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Medicinal Chemistry |