Construction of a Fusion Enzyme Exhibiting Superoxide Dismutase and Peroxidase Activity.
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.
Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. sharapov.mars@gmail.com.
M G
MG
Sharapov
V I
VI
Novoselov
V K
VK
Ravin
D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D054465:Peroxiredoxin VI / Q000235:genetics / Q000378:metabolism*; D055550:Protein Stability; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D013482:Superoxide Dismutase / Q000235:genetics / Q000378:metabolism*; D013696:Temperature
D029968:Escherichia coli Proteins; D011993:Recombinant Fusion Proteins; C515977:PRDX6 protein, human; D054465:Peroxiredoxin VI; D013482:Superoxide Dismutase