Abstract
Abstract
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−1 h−1. 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.
Funder
Technologie-Beratungsinstitut GmbH (TBI) Mecklenburg-Vorpommern
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biotechnology,Bioengineering,Applied Microbiology and Biotechnology
Cited by
17 articles.
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