Sulfur (S), as the second element in the main group 6A just below oxygen (O), has been often used as an isosteric replacement for O in enzymatic mechanistic studies. In addition, S has also been used as an isosteric replacement for CH2. These S-based mechanistic probes have been used
in the studies with protein enzyme systems such as the sirtuin family of the protein Nε-acyl-lysine deacylases, phosphotransferases, and fatty acid desaturase, as well as various RNA enzymes (ribozymes). These probes are basically the O→S mutants of the corresponding O(or CH2)-containing
substrates for the enzymatic reactions under study. This article will review the significant contributions that the S-based probes have been able to make toward an enhanced mechanistic understanding of different types of the enzyme-catalyzed reactions.
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