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. 2022 Nov 7;14(1):2132903. doi: 10.1080/19490976.2022.2132903

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© 2022 The Author(s). Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — The baiP gene from L. scindens ATCC 35704 encodes a bile acid 5α-reductase. (a) Formation of bile acid stereoisomers after reduction of 3-oxo-Δ⁴-LCA and 3-oxo-Δ⁴-DCA by 5α-reductase. (b) Gene organization of baiP with genomic context and domain structure of BaiP. (c) Cloning strategy for heterologous expression of N-terminal his-tagged recombinant BaiP in E. coli BL21(DE3). SDS-PAGE confirms expression of 60.5 kDa recombinant BaiP. (d) Representative LC/MS chromatograms after resting cell assay with E. coli BL21(DE3) pETduet_Control or pETduet_BaiP incubated in anaerobic PBS containing 50 μM 3-oxo-Δ⁴-LCA (Top panels 1 & 2) or 50 μM 3-oxo-Δ⁴-DCA (Bottom panels 3 & 4). Standards are shown in Panel 5 (bottom). (e) Time course of 3-oxo-allo-LCA production by the E. coli BL21(DE3) pETduet_BaiP strain. Data points indicate the mean concentration of 3-oxo-allo-LCA ± SD (three biological replicates).