An evolved aminoacyl-tRNA synthetase with atypical polysubstrate specificity.

@article{Young2011AnEA,
  title={An evolved aminoacyl-tRNA synthetase with atypical polysubstrate specificity.},
  author={D. Young and T. Young and M. Jahnz and Insha Ahmad and G. Spraggon and P. Schultz},
  journal={Biochemistry},
  year={2011},
  volume={50 11},
  pages={
          1894-900
        }
}
We have employed a rapid fluorescence-based screen to assess the polyspecificity of several aminoacyl-tRNA synthetases (aaRSs) against an array of unnatural amino acids. We discovered that a p-cyanophenylalanine specific aminoacyl-tRNA synthetase (pCNF-RS) has high substrate permissivity for unnatural amino acids, while maintaining its ability to discriminate against the 20 canonical amino acids. This orthogonal pCNF-RS, together with its cognate amber nonsense suppressor tRNA, is able to… Expand
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References

SHOWING 1-10 OF 30 REFERENCES
Structural plasticity of an aminoacyl-tRNA synthetase active site.
An enhanced system for unnatural amino acid mutagenesis in E. coli.
A general approach for the generation of orthogonal tRNAs.
Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase.
...
1
2
3
...