Expression of Cytochrome P450 in bacteria: Enhancing the Degradation of Xenobiotics
SUMMARY OF MAIN FINDINGS
- Transformation of Acinetobacter BD413 and expression of cytochrome P450 was achieved.
- Human CYP3A4 fused to its electron donor CPR was inactive, but capable of binding substrates identified in yeast expression studies. Plant CYP71B1:CPR fusion and Streptomyces griseus CYP105D1 were able to bind the varied xenobiotics studied and were active in the metabolism of a range of compounds. This suggested that Acinetobacter contained an electron donor system able to support the activity of CYP105D1.
- Location of plant CYP71B1:CPR in membrane and CYP105D1 in soluble fractions, respectively, allowed growth of Acinetobacter on xenobiotics when monitored spectrophotometrically and by the release of radiolabelled carbon dioxide after addition of 14C-substrate.
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