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Title: Non‐canonical Amino Acid Substrates of E. coli Aminoacyl‐tRNA Synthetases
Abstract In this comprehensive review, I focus on the twentyE. coliaminoacyl‐tRNA synthetases and their ability to charge non‐canonical amino acids (ncAAs) onto tRNAs. The promiscuity of these enzymes has been harnessed for diverse applications including understanding and engineering of protein function, creation of organisms with an expanded genetic code, and the synthesis of diverse peptide libraries for drug discovery. The review catalogues the structures of all known ncAA substrates for each of the 20E. coliaminoacyl‐tRNA synthetases, including ncAA substrates for engineered versions of these enzymes. Drawing from the structures in the list, I highlight trends and novel opportunities for further exploitation of these ncAAs in the engineering of protein function, synthetic biology, and in drug discovery.  more » « less
Award ID(s):
1904872
PAR ID:
10361259
Author(s) / Creator(s):
 
Publisher / Repository:
Wiley Blackwell (John Wiley & Sons)
Date Published:
Journal Name:
ChemBioChem
Volume:
23
Issue:
1
ISSN:
1439-4227
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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