BIOL 97 |
| The tyrosine aminomutase SgTAM contains the electrophilic cofactor 4-methylideneimidazole-5-one (MIO) and is utilized in the biosynthesis of the ß-tyrosine moiety of the enediyne antitumor antibiotic C-1027. Specifically, this enzyme catalyzes the transformation of L-tyrosine to ß-tyrosine. Unlike the closely related histidine ammonia lyase enzymes, which are responsible for the biosynthesis of urocanates and cinnamates, SgTAM performs additional chemical steps resulting in an overall 2,3 amino shift. The precise mechanistic role of MIO in SgTAM remains unclear. In order to elucidate the function of MIO, we have designed and synthesized a number of inhibitors. Additionally, we have performed mechanistic studies involving the kinetics of the reaction catalyzed by SgTAM in the absence and presence of inhibitors. Current kinetics experiments in combination with structural studies are continuing to provide insights into the mechanism of SgTAM activity.
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |
