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Structure–Functional Examination of Novel Ribonucleoside Hydrolase C (RihC) from Limosilactobacillus reuteri LR1статья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 15 февраля 2024 г.
- Авторы: Shaposhnikov Leonid A., Chikurova Natalia Yu, Atroshenko Denis L., Savin Svyatoslav S., Kleymenov Sergei Yu, Chernobrovkina Alla V., Pometun Evgenii V., Minyaev Mikhail E., Matyuta Ilya O., Hushpulian Dmitry M., Boyko Konstantin M., Tishkov Vladimir I., Pometun Anastasia A.
- Журнал: International Journal of Molecular Sciences
- Том: 25
- Номер: 1
- Год издания: 2024
- Издательство: MDPI
- Местоположение издательства: Basel, Switzerland
- Первая страница: 1
- Последняя страница: 21
- Номер статьи: 538
- DOI: 10.3390/ijms25010538
- Аннотация: Ribonucleoside hydrolase C (RihC, EC 3.2.2.1, 3.2.2.2, 3.2.2.3, 3.2.2.7, 3.2.2.8) belongs to the family of ribonucleoside hydrolases Rih and catalyzes the cleavage of ribonucleosides to nitrogenous bases and ribose. RihC is one of the enzymes that are synthesized by lactobacilli in response to the presence of Klebsiella. To characterize this protein from Limosilactobacillus reuteri LR1, we cloned and expressed it. The activity of the enzyme was studied towards a wide range of substrates, including ribonucleosides, deoxyribonucleosides as well as an arabinoside. It was shown that the enzyme is active only with ribonucleosides and arabinoside, with the best substrate being uridine. The thermal stability of this enzyme was studied, and its crystal structure was obtained, which demonstrated the tetrameric architecture of the enzyme and allowed to shed light on a correlation between its structure and enzymatic activity. Comprehensive comparisons of all known RihC structures, both existing crystal structures and computed model structures from various species, were made, allowing for the identification of structural motifs important for enzyme functioning.
- Добавил в систему: Шапошников Леонид Александрович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | ijms-25-00538-v2.pdf | 4,8 МБ | 2 января 2024 [Shaposhnikov_leo] | |
| 2. | Заключение о возможности открытого публикования | Ekspertnoe_MolecularSci.PDF | 1,2 МБ | 11 января 2024 [Natalia_Chikurova] |