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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Nepsilon-thioacetyl-lysine: a multi-facet functional probe for enzymatic protein lysine Nepsilon-deacetylation
David G Fatkins1, Andrew D Monnot, Weiping Zheng
1Department of Chemistry, University of Akron, 190 E. Buchtel Commons, Akron, OH 44325, USA.
Bioorganic & Medicinal Chemistry Letters
|May 16, 2006
Abstract:
Peptides containing Nepsilon-thioacetyl-lysine and Nepsilon-acetyl-lysine were evaluated for their de(thio)acetylation catalyzed by human HDAC8 and SIRT1, two distinct protein deacetylases. Nepsilon-Thioacetyl-lysine was found to be a mimic of Nepsilon-acetyl-lysine for HDAC8-catalyzed reaction, but to confer inhibition against SIRT1. These results point to further diverse applications based on Nepsilon-thioacetyl-lysine.
