Structure–Functional Examination of Novel Ribonucleoside Hydrolase C (RihC) from Limosilactobacillus reuteri LR1

Structure–Functional Examination of Novel Ribonucleoside Hydrolase C (RihC) from Limosilactobacillus reuteri LR1 Научная публикация

Журнал

International Journal of Molecular Sciences
ISSN: 1661-6596 , E-ISSN: 1422-0067

Вых. Данные

Год: 2024, Том: 25, Номер: 1, Номер статьи : 538, Страниц : DOI: 10.3390/ijms25010538

Авторы

Shaposhnikov Leonid A. ^1,2 , Chikurova Natalia Yu. ^1,2 , Atroshenko Denis L. ^1,2,3 , Savin Svyatoslav S. ^1,2 , Kleymenov Sergei Yu. ^1,4 , Chernobrovkina Alla V. ² , Pometun Evgenii V. ⁵ , Minyaev Mikhail E. ⁶ , Matyuta Ilya O. ¹ , Hushpulian Dmitry M. ¹ , Boyko Konstantin M. ¹ , Tishkov Vladimir I. ^1,2,7 , Pometun Anastasia A. ^1,2,3

Организации

1	Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences, Leninsky Avenue, 33/2, Moscow 119071, Russia
2	Department of Chemistry, Lomonosov Moscow State University, Leninskie Gory, 1–3, Moscow 119991, Russia
3	Institute of Medicine, Peoples’ Friendship University of Russia Named after Patrice Lumumba, Miklouho-Maklaya, 8, Moscow 117198, Russia
4	Koltzov Institute of Developmental Biology of Russian Academy of Sciences, Vavilova, 26, Moscow 119334, Russia
5	Department of Analytical, Physical and Colloidal Chemistry, A.P. Nelyubin Institute of Pharmacy, Sechenov First Moscow State Medical University, Trubetskaya St., 8, Building 2, Moscow 119048, Russia
6	N. D. Zelinsky Institute of Organic Chemistry Russian Academy of Sciences, Leninsky Avenue, 47, Moscow 119991, Russia
7	Faculty of Biology and Biotechnology, National Research University Higher School of Economics, Profsoyuznaya St., 33, Building 4, Moscow 117418, Russia

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.

Shaposhnikov L.A. , Chikurova N.Y. , Atroshenko D.L. , Savin S.S. , Kleymenov S.Y. , Chernobrovkina A.V. , Pometun E.V. , Minyaev M.E. , Matyuta I.O. , Hushpulian D.M. , Boyko K.M. , Tishkov V.I. , Pometun A.A.
Structure–Functional Examination of Novel Ribonucleoside Hydrolase C (RihC) from Limosilactobacillus reuteri LR1
International Journal of Molecular Sciences. 2024. V.25. N1. 538 . DOI: 10.3390/ijms25010538 WOS Scopus OpenAlex

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