Construction of a Fusion Enzyme Exhibiting Superoxide Dismutase and Peroxidase Activity

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M. G. Sharapov^*, V. I. Novoselov, and V. K. Ravin

Institute of Cell Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: sharapov.mars@gmail.com

^* To whom correspondence should be addressed.

Received December 8, 2015; Revision received January 19, 2016

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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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KEY WORDS: superoxide dismutase, peroxiredoxin 6, chimeric protein, oxidative stress

DOI: 10.1134/S0006297916040131

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