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Highly selective bile acid hydroxylation by the multifunctional bacterial P450 monooxygenase CYP107D1 (OleP). | LitMetric

Highly selective bile acid hydroxylation by the multifunctional bacterial P450 monooxygenase CYP107D1 (OleP).

Biotechnol Lett

Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.

Published: May 2020

Objective: Regio- and stereoselective hydroxylation of lithocholic acid (LCA) using CYP107D1 (OleP), a cytochrome P450 monooxygenase from the oleandomycin synthesis pathway of Streptomyces antibioticus.

Results: 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 h. NMR spectroscopy confirmed the identity of MDCA as the sole product.

Conclusions: The multifunctional P450 monooxygenase CYP107D1 (OleP) can hydroxylate LCA, forming MDCA as the only product.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7101289PMC
http://dx.doi.org/10.1007/s10529-020-02813-4DOI Listing

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