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Cover Picture: Design of S ‐Allylcysteine in Situ Production and Incorporation Based on a Novel Pyrrolysyl‐tRNA Synthetase Variant (ChemBioChem 1/2017)
Author(s) -
Exner Matthias P.,
Kuenzl Tilmann,
To Tuyet Mai T.,
Ouyang Zhaofei,
Schwagerus Sergej,
Hoesl Michael G.,
Hackenberger Christian P. R.,
Lensen Marga C.,
Panke Sven,
Budisa Nediljko
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600660
Subject(s) - transfer rna , substrate (aquarium) , amino acid , aminoacyl trna synthetase , enzyme , biochemistry , chemistry , cover (algebra) , genetic code , in situ , substrate specificity , biology , rna , gene , organic chemistry , ecology , mechanical engineering , engineering
The cover picture shows a journey from garlic to genetic code engineering: In this issue, Budisa and co‐workers report in vivo‐specific protein olefination with S ‐allylcysteine (Sac), which is naturally abundant in garlic. Alternatively, it can also be biosynthesized in situ by supplementing the amino acid metabolism of E. coli with allylmercaptan. Sac is recognized and activated by the novel and unique pyrrolysyl‐tRNA synthetase‐based enzyme S ‐allylcysteinyl‐tRNA synthetase (SacRS), which is capable of specifically accepting a small, polar amino acid instead of the long and bulky aliphatic natural substrate. In this way, a biochemical pathway for the production of proteins containing S ‐allylcysteine as a minimal tag or label for chemical protein modification has been established. More information can be found in the communication by S. Panke, N. Budisa et al. on page 85 in Issue 1, 2017 (DOI: 10.1002/cbic.201600537).