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Biocatalysis

Making selenometabolites nature’s way

Nature Synthesis volume 3, pages 426–427 (2024)Cite this article

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Chemical selenylation of sulfur carrier proteins enables enzymatic incorporation of selenium into small molecules, thereby advancing a biocatalytic method for C–Se bond formation and chemoenzymatic selenometabolite synthesis.

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Fig. 1: Chemical selenylation of sulfur carrier proteins (SCPs) enables enzymatic selenometabolite synthesis.

References

  1. Scott, K. A. & Njardarson, J. T. Top. Curr. Chem. (Cham) 376, 1–34 (2018).

    Article  CAS  Google Scholar 

  2. Nogueira, C. W., Barbosa, N. V. & Rocha, J. B. T. Arch. Toxicol. 95, 1179–1226 (2021).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. Beletskaya, I. P. & Ananikov, V. P. Chem. Rev. 122, 16110–16293 (2022).

    Article  CAS  PubMed  Google Scholar 

  4. Cheng, R. et al. ACS Catal. 11, 3319 (2021).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Goncharenko, K. V. et al. Chem. Eur. J. 26, 1328–1334 (2020).

    Article  CAS  PubMed  Google Scholar 

  6. Kayrouz, C. M., Huang, J., Hauser, N. & Seyedsayamdost, M. R. Nature 610, 199–204 (2022).

    Article  CAS  PubMed  Google Scholar 

  7. Zhang, X. et al. Nat. Synth. https://doi.org/10.1038/s44160-023-00477-2 (2024).

    Article  Google Scholar 

  8. Begley, T. P. et al. Curr. Opin. Chem. Biol. 3, 623–629 (1999).

    Article  CAS  PubMed  Google Scholar 

  9. Ronau, J. A., Beckmann, J. F. & Hochstrasser, M. Cell Res. 26, 441–456 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  10. Burroughs, A. M., Iyer, L. M. & Aravind, L. Proteins. 75, 895–910 (2009).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  11. Serrão, V. H. B. et al. Amino Acids 50, 1145–1167 (2018).

    Article  PubMed  Google Scholar 

Download references

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Authors and Affiliations

  1. Department of Chemistry, Princeton University, Princeton, NJ, USA

    Chase M. Kayrouz & Mohammad R. Seyedsayamdost

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  1. Chase M. Kayrouz
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  2. Mohammad R. Seyedsayamdost
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Correspondence to Mohammad R. Seyedsayamdost.

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The authors declare no competing interests.

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Kayrouz, C.M., Seyedsayamdost, M.R. Making selenometabolites nature’s way. Nat. Synth 3, 426–427 (2024). https://doi.org/10.1038/s44160-024-00483-y

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