Fig. 1: E. coli strain for synthesis of noncanonical amino acids and application to genetic code expansion. | Nature Communications

Fig. 1: E. coli strain for synthesis of noncanonical amino acids and application to genetic code expansion.

From: A robust platform streamlining aromatic noncanonical amino acid biosynthesis and genetic code expansion in Escherichia coli

Fig. 1

a Traditional GCE with ncAAs supplements. The orthogonal translation system relies on the extrinsic addition of ncAAs to the medium for protein production. Created in BioRender (https://BioRender.com/cf6rx1z). b Representative ncAAs by de novo biosynthesis for GCE through metabolic engineering. c Representative ncAAs by semisynthesis from precursors for GCE. d The engineered E. coli strain developed in this study utilizes a multi-enzyme cascade pathway to convert a range of aromatic aldehydes into L-aromatic ncAAs. This pathway involves the overexpression of threonine aldolase (LTA), threonine deaminase (LTD), and the native aromatic amino acid aminotransferase (AT) in E. coli. The synthesized ncAAs are then incorporated into the target protein through genetic code expansion (GCE) in situ, facilitated by the expression of exogenous aminoacyl-tRNA synthetase (aaRS) and tRNA. This approach establishes an engineered strain for both ncAA biosynthesis and the production of ncAA-containing proteins. Created in BioRender (https://BioRender.com/9aei6t2).

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