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Unexpectedly fast transfer of positron-emittable artificial substrate into N-terminus of peptide/protein mediated by wild-type L/F-tRNA-protein transferase

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Abstract

This article demonstrates the fastest enzymatic introduction of a positron emission tomography (PET) probe into acceptor peptides/proteins. It is site-specifically introduced at the basic N-terminus of the acceptors by using L/F-transferase in combination with aminoacyl-tRNA synthetase, namely the NEXT-A/PET reaction. Estimated from kinetic analysis, the transfer efficiency of O-(2-fluoromethyl)-l-tyrosine as an artificial amino acid PET probe mediated by the wild-type transferase is almost as good as that of the natural substrate, phenylalanine.

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Acknowledgments

This work was supported by Japan Science and Technology Agency (JST) for the Development of Systems and Technology for Advanced Measurement and Analysis Program (10401005). We sincerely thank Prof. Dr. Masahiko Sisido for giving us many useful suggestions and advices. We also thank Dr. Laura Nelson for careful reading and editing of this manuscript.

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The authors have declared no conflict of interest.

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Correspondence to Masumi Taki.

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Handling Editor: E. Tippmann.

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Taki, M., Kuroiwa, H. Unexpectedly fast transfer of positron-emittable artificial substrate into N-terminus of peptide/protein mediated by wild-type L/F-tRNA-protein transferase. Amino Acids 47, 1279–1282 (2015). https://doi.org/10.1007/s00726-015-1989-y

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  • DOI: https://doi.org/10.1007/s00726-015-1989-y

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