Regio- and stereoselective hydroxylation of lithocholic acid (LCA) using CYP107D1 (OleP), a cytochrome P450 monooxygenase from the oleandomycin synthesis pathway of Streptomyces antibioticus.
Co-expression of CYP107D1 from S. antibioticus and the reductase/ferredoxin system PdR/PdX from Pseudomonas putida was performed in Escherichia coli whole cells. In vivo hydroxylation of LCA exclusively yielded the 6β-OH product murideoxycholic acid (MDCA). In resting cells, 19.5% of LCA was converted to MDCA within 24 h, resulting in a space time yield of 0.04 mmol L−1 h−1. NMR spectroscopy confirmed the identity of MDCA as the sole product.
The multifunctional P450 monooxygenase CYP107D1 (OleP) can hydroxylate LCA, forming MDCA as the only product.
Electronic supplementary material
The online version of this article (10.1007/s10529-020-02813-4) contains supplementary material, which is available to authorized users.
https://www.researchpad.co/tools/openurl?pubtype=article&doi=10.1007/s10529-020-02813-4&title=Highly selective bile acid hydroxylation by the multifunctional bacterial P450 monooxygenase CYP107D1 (OleP)&author=&keyword=P450 monooxygenase,Bile acids,Murideoxycholic acid,Lithocholic acid,&subject=Original Research Paper,
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