1. Sirtuins Caught in the Act
Brian C. Smith, John M. Denu 
Structure 
Volume 14, Issue 8, Pages (August 2006)
DOI: /j.str
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2. Figure 1 Proposed Mechanism of Sir2 Protein Deacetylases
Acetyl-lysine substrate and nicotinamide adenine dinucleotide bind to Sir2 deacetylases to form a ternary complex. After binding, the reaction proceeds through either an SN1- or SN2-like mechanism to release nicotinamide and produce the O-alkylamidate intermediate resulting from acetyl-lysine carbonyl oxygen attack at the 1′-carbon of the nicotinamide ribose. The O-alkylamidate intermediate is then hydrolyzed through multiple steps to form a product complex from which deacetylated-lysine product and O-acetyl-ADP-ribose are released. The coordinates used to depict the structures in the figure were provided by Kevin Hoff and Cynthia Wolberger (Hoff et al., 2006).
Structure  , DOI: ( /j.str )
Copyright © 2006 Elsevier Ltd Terms and Conditions