Abstract
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.
Keywords: Sulfur-based, mechanistic probes, enzymatic reactions.
Current Medicinal Chemistry
Title:Sulfur-based Mechanistic Probes for Enzyme-catalyzed Reactions
Volume: 20 Issue: 30
Author(s): Weiping Zheng
Affiliation:
Keywords: Sulfur-based, mechanistic probes, enzymatic reactions.
Abstract: 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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Cite this article as:
Zheng Weiping, Sulfur-based Mechanistic Probes for Enzyme-catalyzed Reactions, Current Medicinal Chemistry 2013; 20 (30) . https://dx.doi.org/10.2174/09298673113209990177
DOI https://dx.doi.org/10.2174/09298673113209990177 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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