BIOL 61 |
| Our research group has been active in the design, synthesis and evaluation of unnatural amino acids as mechanism-based inhibitors for pyridoxal phosphate (PLP)-enzymes. Initial efforts in this area specifically targeted amino acid decarboxylase enzymes. For example, we chose to replace the alpha-proton with a vinyl or halovinyl group, resulting in a quaternary, beta,gamma-unsaturated amino acid design. This was particularly successful in the active site of lysine decarboxylase (JACS, 2007, 129, 258-9). Herein, our general stategies for decarboxylase enzymes will be outlined, as will our more recent efforts to examine PLP enzymes that labilize the C-alpha-H bond. Inhibitor design/synthesis strategies, enzyme purification and inhibition studies will be presented. |
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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 |