Regular ArticleThe Function of Recombinant Cytochrome P450s in IntactEscherichia coliCells: The 17α-Hydroxylation of Progesterone and Pregnenolone by P450c17☆,☆☆
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2008, Bioresource TechnologyCitation Excerpt :Recombinant DNA technology has also been applied to develop an industrially important strain of Escherichia coli by transforming it with recombinant cytochrome-P450s. This mutant was capable of biotransforming progesterone to 3β-hydroxy-5-androsten-17-one (Shet et al., 1997). A mutant strain Rhodococcus erythropolis RG1–UV29 was produced by inactivation of kstD1 and kstD2 genes, which resulted in elimination of 3-ketosteroid-Δ1-dehydrogenase activity of this microorganism, rendering them capable of transforming AD to 9α-hydroxy-androstenedione.
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Supported in part by grants from the USPHS (GM 16488 and ES 07628).
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G. Weber, Ed.
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