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Mol Biol (Mosk)
2009 Jan 01;433:505-11. doi: 10.1134/s0026893309030194.
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[Cloning, expression and comparative analysis of peroxiredoxine 6 from different species].
Sharapov MG
,
Novoselov VI
,
Ravin VK
.
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Human, rat, Xenopus and Drosophila (Dpx2540 and Dpx6005) cDNA of peroxiredoxins were cloned and expressed in Escherichia coli. Their enzymatic activity, temperature optimum and thermostability were determined. For H2O2 the activity of enzymes decreased in the following order: DPx2540 > > human > Xenopus >rat > DPx6005. For tret-butyl hydroperoxide the order of activity decrease is: DPx2540 = DPx6005 > rat > Xenopus > human. Effectiveness of plasmid DNA protection from oxidative damage mediated by Fenton reaction is: Dpx2540 > Dpx6005 = rat = human > Xenopus. The optimal temperature for activity of all these enzymes is 37 degrees C. Peroxiredoxins from rat, Xenopus and Drosophila (Dpx 6005) retain no less than 50% of activity in a wide temperature range (10-50 degrees C) in contrast to human and Drosophila (Dpx 2540) enzymes with the interval of only 25-45 degrees C. The thermostability of enzymes decreased in the following order: Dpx6005 > or = rat > human > Xenopus > Dpx2540. So, there is negative correlation between activity and stability of peroxiredoxin 6.
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