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Rational Design and Mutagenesis of Fungal Luciferase from Neonothopanus nambi

  • BIOCHEMISTRY, BIOPHYSICS, AND MOLECULAR BIOLOGY
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Abstract

The recently described bioluminescent system from fungi has great potential for developing highly efficient tools for biomedical research. Luciferase enzyme is one of the most crucial components of this system. The luciferase from Neonothopanus nambi fungus belongs to the novel still undescribed protein family. The structure data for this protein is almost absent. A detailed study of the N. nambi luciferase properties is necessary for the improvement of analytical methods based on the fungal bioluminescent system. Here we present the positions of key amino acid residues and their effect on enzyme function described using bioinformatic and experimental approaches. These results are useful for further fungal luciferase structure determination.

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Funding

This work was supported by the grant from the Russian Science Foundation no. 16-14-00052P, alanine screening was performed by the President grant for leading scientific schools NSh-2605.2020.4.

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Authors and Affiliations

  1. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russia

    K. A. Beregovaya, N. M. Myshkina, T. V. Chepurnykh, A. A. Kotlobay & I. V. Yampolsky

  2. Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russia

    K. V. Purtov, V. N. Petushkov & N. S. Rodionova

Authors
  1. K. A. Beregovaya
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  2. N. M. Myshkina
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  3. T. V. Chepurnykh
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  4. A. A. Kotlobay
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  5. K. V. Purtov
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  6. V. N. Petushkov
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  7. N. S. Rodionova
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  8. I. V. Yampolsky
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Corresponding author

Correspondence to K. V. Purtov.

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This article does not contain any studies involving animals or human participants performed by any of the authors.

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The authors declare that they have no conflict of interest.

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Beregovaya, K.A., Myshkina, N.M., Chepurnykh, T.V. et al. Rational Design and Mutagenesis of Fungal Luciferase from Neonothopanus nambi . Dokl Biochem Biophys 496, 14–17 (2021). https://doi.org/10.1134/S1607672921010026

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  • DOI: https://doi.org/10.1134/S1607672921010026

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