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Expanding the genetic code with a lysine derivative bearing an enzymatically removable phenylacetyl group
- Reille-Seroussi, Marie, Mayer, Susanne V., Dörner, Wolfgang, Lang, Kathrin, Mootz, Henning D.
- Chemical communications 2019 v.55 no.33 pp. 4793-4796
- Bacillus subtilis, Escherichia coli, chemical reactions, genetic code, lysine, moieties, penicillin amidase, peptides, protein structure, proteins
- We report the genetically encoded incorporation of phenylacetyl protected lysine (PacK) into proteins in Escherichia coli. This unnatural side-chain modification can be enzymatically removed using either penicillin G acylase (PGA) or, surprisingly, the sirtuin SrtN from Bacillus subtilis. Our approach expands the toolbox to reversibly control protein structure and function under very mild and non-denaturing conditions, as demonstrated by triggering the activity of the nonribosomal peptide synthetase GrsA.