The protein in question is the Drosophila Pxd Peroxidase and it has been expressed in Pichia Pastoris system. I would like to know if viable expression in an E. coli expression system is possible.
I've never worked with Drosophila Pxd Peroxidase, but of course peroxidases have been expressed in E. coli. Examples include horseradish peroxidase, yeast cytochrome c peroxidase, pea ascorbate peroxidase, Leishmania major peroxidase, etc... I personally like working with a pET expression system and E. coli BL21(DE3) cells.
I'm not familiar with your enzyme, but I am curious as to why it was placed in yeast first? Is it because it is membrane anchored or has PTMs? If it is membrane anchored, it's going to be hit and miss as purification of active membrane bound proteins from ecoli is still not well understood. I would think about how to purify (if that is the intention) before going to far.
Just to add a simple comment. Yes, as said by the three other guys, the expression of a bucnh of peroxidease have been carried out in E. coli. Just to show you how this is most of the time eprformed (because, peroxidases frequently yield inclusion bodies in E coli). Here is an ols paper (old pot makes the best soup, right!):
Biochemical and Biophysical Research Communications
Volume 216, Issue 3, 22 November 1995, Pages 1013–1017
Expression of Fungal Mn Peroxidase in E. Coli and Refolding to Yield Active Enzyme
R.E. Whitwam,
I.G. Gazarian,
M. Tien
Abstract
The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was expressed in Escherichia coli. The portion of the cDNA encoding the enzyme′s signal peptide, not found in the processed holoenzyme, was deleted from the cDNA. The polypeptide was produced as inactive inclusion bodies that could be solubilized in 8 M urea and the reducing agent dithiothreitol. Reconstitution of activity was accomplished by diluting the urea concentration to 2M the presence of hemin, calcium, and oxidized glutathione. All of the additives were required for recovery of activity. The activity of the recombinant enzyme was dependent on both Mn2+ and H2O2.
I am citing this paper, just to show you, dear Victor, the abstract that contains a quite pertinent information on how to proceed for getting nice amounts of functional recombinant peroxidases.