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• W3213441382 startingPage "106025" @default.
• W3213441382 abstract "Nowadays, 17β-estradiol (E2) biodegradation pathway has still not been identified in bacteria. To bridge this gap, we have described a novel E2 degradation pathway in Rhodococcus sp. P14 in this study, which showed that estradiol could be first transferred to estrone (E1) and thereby further converted into 16-hydroxyestrone, and then transformed into opened estrogen D ring. In order to identify the genes, which may be responsible for the pathway, transcriptome analysis was performed during E2 degradation in strain P14. The results showed that the expression of a short-chain dehydrogenase (SDR) gene and a CYP123 gene in the same gene cluster could be induced significantly by E2. Based on gene analysis, this gene cluster was found to play an important role in transforming E2 to 16-hydroxyestrone. The function of CYP123 was unknown before this study, and was found to harbor the activity of 16-estrone hydratase. Moreover, the global response to E2 in strain P14 was also analyzed by transcriptome analysis. It was observed that various genes involved in the metabolism processes, like the TCA cycle, lipid and amino acid metabolism, as well as glycolysis showed a significant increase in mRNA levels in response to strain P14 that can use E2 as the single carbon source. Overall, this study provides us an in depth understanding of the E2 degradation mechanisms in bacteria and also sheds light about the ability of strain P14 to effectively use E2 as the major carbon source for promoting its growth." @default.
• W3213441382 created "2021-11-22" @default.
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• W3213441382 date "2022-01-01" @default.
• W3213441382 modified "2023-10-16" @default.
• W3213441382 title "Identification of an important function of CYP123: Role in the monooxygenase activity in a novel estradiol degradation pathway in bacteria" @default.
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• W3213441382 doi "https://doi.org/10.1016/j.jsbmb.2021.106025" @default.
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• W3213441382 hasPublicationYear "2022" @default.
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