Abstract
The 2-naphthol analogue of tyrosine, 2-amino-3-(6-hydroxy-2-naphthyl)propanoic acid (NpOH), has been genetically introduced into proteins in Escherichia coli . This is achieved through the directed evolution of orthogonal aminoacyl-tRNA synthetase/tRNA pairs that selectively charge the target amino acid in response to the amber stop codon, UAG. Moreover, chemoselective azo coupling reactions have been revealed between the 2-naphthol group and diazotized aniline derivatives that are substituted with an electron donating moiety. The coupling reactions required a very mild condition (pH 7) with great reaction rate (less than 2 h at 0 °C), high efficiency, and excellent selectivity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acyl-tRNA Synthetases / genetics
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Amino Acyl-tRNA Synthetases / metabolism
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Directed Molecular Evolution / methods
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Escherichia coli / chemistry
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics*
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Escherichia coli Proteins / metabolism
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Methanococcus / enzymology
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Methanococcus / genetics
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Models, Molecular
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Naphthols / chemistry
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Naphthols / metabolism*
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Protein Engineering / methods
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Tyrosine / analogs & derivatives*
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Tyrosine / genetics*
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Tyrosine / metabolism
Substances
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Escherichia coli Proteins
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Naphthols
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Tyrosine
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Amino Acyl-tRNA Synthetases
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2-naphthol