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Catalytically important flavin linked through a phosphoester bond in a eukaryotic fumarate reductaseстатья
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: 28 июня 2018 г.
- Авторы: Serebryakova M.V., Bertsova Y.V., Sokolov S.S., Kolesnikov A.A., Baykov A.A., Bogachev A.V.
- Журнал: Biochimie
- Том: 149
- Год издания: 2018
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 34
- Последняя страница: 40
- DOI: 10.1016/j.biochi.2018.03.013
- Аннотация: One of the three domains of kinetoplastid NADH:fumarate oxidoreductase (FRD) is homologous to bacterial flavin transferase that catalyzes transfer of FMN residue from FAD to threonine in flavoproteins. Leptomonas pyrrhocoris FRD produced in yeast cells, which lack flavin transferase gene in their proteome, reduces fumarate in the presence of NADH and contains an FMN residue covalently linked to a Ser9 residue. The conserved flavinylation motif of FRD, D3(g/s)x(s/t)(s/g)AS9, is similar to the Dxx(s/t)gAT motif recognized by flavin transferase in prokaryotic proteins. Ser9 replacement abolished the flavinylation and fumarate reductase activity of FRD. These findings suggest that the flavinylation is important for the activity of FRD and that this post-translational modification is carried out by the own flavin transferase domain.
- Добавил в систему: Богачев Александр Валерьевич