ArticleACS omega2020
Altering the Regioselectivity of Cytochrome P450 BM3 Variant M13 toward Genistein through Protein Engineering and Variation of Reaction Conditions.
Article in ACS omega, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Biosynthesis of eriodictyol in citrus waster by endowing P450BM3 activity of naringenin hydroxylation.Applied microbiology and biotechnology · 2024Article
- Lapatinib Suppresses HER2-Overexpressed Cholangiocarcinoma and Overcomes ABCB1- Mediated Gemcitabine Chemoresistance.Frontiers in oncology · 2022Article
- A Promiscuous Bacterial P450: The Unparalleled Diversity of BM3 in Pharmaceutical Metabolism.International journal of molecular sciences · 2021Review
- Hemoprotein Catalyzed Oxygenations: P450s, UPOs, and Progress toward Scalable Reactions.JACS Au · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biocatalysts responsible for the enzymatic synthesis of hydroxygenisteins, derivatives of genistein with multiple activities, usually show regioselective promiscuity, hydroxylating genistein to form a mixture of multiple products, which, in turn, results in a cumbersome separation and purification. Hence, it is highly desired to explore the underlying mechanism regulating the regioselectivity of hydroxylases. M13 is a variant of cytochrome P450 BM3 with oxidant activity toward genistein. Herein, genistein was demonstrated to be hydroxylated by M13 to form a mixture of 3'-hydroxygenistein (3'-OHG) and 8-hydroxygenistein (8-OHG), each giving 4% conversion with a ratio of 1:1. Protein engineering toward M13 was thus performed to improve its regioselectivity. When isoleucine at position 86 was mutated into cysteine, the resultant variant M13I86C displayed improved regioselectivity toward 3'-OHG with an increased conversion of 8.5%. The double mutation M13I86CP18W further boosted the conversion of 3'-OHG to 9.6%, and the ratio of 3'-OHG to 8-OHG increased to 12:1. Conversely, both CoCl
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Registered trials
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