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Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.

Authors
  • Hartman, Matthew C T1
  • 1 Department of Chemistry and Massey Cancer Center, Virginia Commonwealth University, 1001 W Main St., Richmond, VA 23220, USA.
Type
Published Article
Journal
ChemBioChem
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jan 05, 2022
Volume
23
Issue
1
Identifiers
DOI: 10.1002/cbic.202100299
PMID: 34416067
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

In this comprehensive review, I focus on the twenty E. coli aminoacyl-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 20 E. coli aminoacyl-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. © 2021 Wiley-VCH GmbH.

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