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Genetic fusion of P450 BM3 and formate dehydrogenase towards self-sufficient biocatalysts with enhanced activityстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 15 декабря 2021 г.
- Авторы: Kokorin A., Parshin P.D., Bakkes P.J., Pometun A.A., Tishkov V.I., Urlacher V.B.
- Журнал: Scientific reports
- Том: 11
- Номер: 1
- Год издания: 2021
- Издательство: Nature Publishing Group
- Местоположение издательства: United Kingdom
- Номер статьи: 21706
- DOI: 10.1038/s41598-021-00957-5
- Аннотация: Fusion of multiple enzymes to multifunctional constructs has been recognized as a viable strategy to improve enzymatic properties at various levels such as stability, activity and handling. In this study, the genes coding for cytochrome P450 BM3 from B. megaterium and formate dehydrogenase from Pseudomonas sp. were fused to enable both substrate oxidation catalyzed by P450 BM3 and continuous cofactor regeneration by formate dehydrogenase within one construct. The order of the genes in the fusion as well as the linkers that bridge the enzymes were varied. The resulting constructs were compared to individual enzymes regarding substrate conversion, stability and kinetic parameters to examine whether fusion led to any substantial improvements of enzymatic properties. Most noticeably, an activity increase of up to 3-fold was observed for the fusion constructs with various substrates which were partly attributed to the increased diflavin reductase activity of the P450 BM3. We suggest that P450 BM3 undergoes conformational changes upon fusion which resulted in altered properties, however, no NADPH channeling was detected for the fusion constructs.
- Добавил в систему: Тишков Владимир Иванович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Scientific_Reports_2021_11_21706.pdf | Scientific_Reports_2021_11_21706.pdf | 1,3 МБ | 19 января 2022 [tishkov] |