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

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.

SUBMITTER: Hartman MCT

PROVIDER: S-EPMC9651912 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature

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

Hartman Matthew C T MCT

Chembiochem : a European journal of chemical biology 20210922 1

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 ...[more]

PMID: 34416067

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