ArticleFrontiers in chemistry2021
Exploring the Potential of Cytochrome P450 CYP109B1 Catalyzed Regio-and Stereoselective Steroid Hydroxylation.
Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 29 citations in OpenAlex.
- Functional characterization of steroid hydroxylation by cytochrome P450 enzymes from Rhodococcus erythropolis KB1.Microbial cell factories · 2026Article
- Structure-Function Analysis of the Steroid-Hydroxylating Cytochrome P450 109 (CYP109) Enzyme Family.International journal of molecular sciences · 2025Article
- Functional characterization and unraveling the structural determinants of novel steroid hydroxylase CYP154C7 fromHeliyon · 2024Article
- Efficient stereoselective hydroxylation of deoxycholic acid by the robust whole-cell cytochrome P450 CYP107D1 biocatalyst.Synthetic and systems biotechnology · 2023Article
- Review
- HApplied and environmental microbiology · 2023Article
- Recent trends in biocatalysis.Chemical Society reviews · 2021Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
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Abstract
Cytochrome P450 enzyme CYP109B1 is a versatile biocatalyst exhibiting hydroxylation activities toward various substrates. However, the regio- and stereoselective steroid hydroxylation by CYP109B1 is far less explored. In this study, the oxidizing activity of CYP109B1 is reconstituted by coupling redox pairs from different sources, or by fusing it to the reductase domain of two self-sufficient P450 enzymes P450RhF and P450BM3 to generate the fused enzyme. The recombinant
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