Biosynthesis of a steroid metabolite by an engineered Rhodococcus erythropolis strain expressing a mutant cytochrome P450 BM3 enzymeVenkataraman, H., Te Poele, E. M., Rosłoniec, K. Z., Vermeulen, N., Commandeur, J. N. M., van der Geize, R. & Dijkhuizen, L., Jun-2015, In : Applied Microbiology and Biotechnology. 99, 11, p. 4713-4721 9 p.
Research output: Contribution to journal › Article › Academic › peer-review
In the present study, the use of Rhodococcus erythropolis mutant strain RG9 expressing the cytochrome P450 BM3 mutant M02 enzyme has been evaluated for whole-cell biotransformation of a 17-ketosteroid, norandrostenedione, as a model substrate. Purified P450 BM3 mutant M02 enzyme hydroxylated the steroid with >95 % regioselectivity to form 16-β-OH norandrostenedione, as confirmed by NMR analysis. Whole cells of R. erythropolis RG9 expressing P450 BM3 M02 enzyme also converted norandrostenedione into the 16-β-hydroxylated product, resulting in the formation of about 0.35 g/L. Whole cells of strain RG9 itself did not convert norandrostenedione, indicating that metabolite formation is P450 BM3 M02 enzyme mediated. This study shows that R. erythropolis is a novel and interesting host for the heterologous expression of highly selective and active P450 BM3 M02 enzyme variants able to perform steroid bioconversions.
|Number of pages||9|
|Journal||Applied Microbiology and Biotechnology|
|Early online date||16-Dec-2014|
|Publication status||Published - Jun-2015|