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Construction of a fusion enzyme exhibiting superoxide dismutase and peroxidase activity

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Abstract

A chimeric gene construct encoding human peroxiredoxin 6 and Mn-superoxide dismutase from Escherichia coli was developed. Conditions for expression of the fusion protein in E. coli cell were optimized. Fusing of the enzymes into a single polypeptide chain with peroxiredoxin 6 at the N-terminus (PSH) did not affect their activities. On the contrary, the chimeric protein with reverse order of enzymes (SPH) was not obtained in a water-soluble active form. The active chimeric protein (PSH) exhibiting both peroxidase and superoxide dismutase activities was prepared and its physicochemical properties were characterized.

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Authors and Affiliations

  1. Institute of Cell Biophysics, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

    M. G. Sharapov, V. I. Novoselov & V. K. Ravin

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  1. M. G. Sharapov
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  2. V. I. Novoselov
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  3. V. K. Ravin
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Correspondence to M. G. Sharapov.

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Original Russian Text © M. G. Sharapov, V. I. Novoselov, V. K. Ravin, 2016, published in Biokhimiya, 2016, Vol. 81, No. 4, pp. 571-579.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM15-400, February 14, 2016.

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Sharapov, M.G., Novoselov, V.I. & Ravin, V.K. Construction of a fusion enzyme exhibiting superoxide dismutase and peroxidase activity. Biochemistry Moscow 81, 420–427 (2016). https://doi.org/10.1134/S0006297916040131

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  • DOI: https://doi.org/10.1134/S0006297916040131

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