BIOL 164 |
| The identification of a novel class of HDACs, the silent information regulator 2 (Sir2 or sirtuin) family of histone/protein deacetylases, has led to the characterization of a NAD+-dependent process that is coupled with the formation of O-acetyl-ADP-ribose as the primary product. Due to the inherent instability of O-acetyl-ADP-ribose, its hydrolysis has hindered efforts thus far to investigate its role in cellular pathways. In an effort to generate a biochemical tool to carry out such investigations, non-hydrolyzable analogs of O-acetyl-ADP-ribose containing an N-acetyl moiety have been generated. The ability of these N-acetyl analogs to mimic the authentic metabolite will be evaluated using known targets of O-acetyl-ADP-ribose. |
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Chemistry and Metabolism
4:30 PM-6:30 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster
Division of Biological Chemistry |