ArticleJournal of industrial microbiology & biotechnology2017
In vitro reconstitution of the cyclosporine specific P450 hydroxylases using heterologous redox partner proteins.
Article in Journal of industrial microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Unveiling cytochrome P450 enzymes that catalyze steroid side-chain cleavage in bacteria.Nature communications · 2025Article
- Genome mining and characterization of a heme-dependent enzyme catalyzing intermolecular Nitrogen-Nitrogen bond formation in hydrazinosuccinic acid biosynthesis.Synthetic and systems biotechnology · 2025Article
- Prokaryotic expression and characterization of artificial self-sufficient CYP120A monooxygenases.Applied microbiology and biotechnology · 2023Article
- Efficient hydroxylation of flavonoids by using whole-cell P450 sca-2 biocatalyst inFrontiers in bioengineering and biotechnology · 2023Article
- Three pairs of surrogate redox partners comparison for Class I cytochrome P450 enzyme activity reconstitution.Communications biology · 2022Article
- Article
- Exploring the Potential of Cytochrome P450 CYP109B1 Catalyzed Regio-and Stereoselective Steroid Hydroxylation.Frontiers in chemistry · 2021Article
- Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications.The Journal of biological chemistry · 2020Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytochrome P450 enzymes (CYPs) CYP-sb21 from Sebekia benihana and CYP-pa1 from Pseudonocardia autotrophica are able to hydroxylate the immunosuppressant cyclosporin A (CsA) in a regioselective manner, giving rise to the production of two hair-stimulating agents (with dramatically attenuated immunosuppressant activity), γ-hydroxy-N-methyl-L-Leu4-CsA (CsA-4-OH) and γ-hydroxy-N-methyl-L-Leu9-CsA (CsA-9-OH). Recently, the in vitro activity of CYP-sb21 was identified using several surrogate redox partner proteins. Herein, we reconstituted the in vitro activity of CYP-pa1 for the first time via a similar strategy. Moreover, the supporting activities of a set of ferredoxin (Fdx)/ferredoxin reductase (FdR) pairs from the cyanobacterium Synechococcus elongatus PCC 7942 were comparatively analyzed to identify the optimal redox systems for these two CsA hydroxylases. The results suggest the great value of cyanobacterial redox partner proteins for both academic research and industrial application of P450 biocatalysts.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.