A1 Refereed original research article in a scientific journal

Enzymatic Synthesis of the C-glycosidic Moiety of Nogalamycin R




AuthorsSiitonen Vilja, Nji Wandi Benjamin, Törmänen Akke-Pekka, Metsä-Ketelä Mikko

PublisherACS Chemical Biology

Publication year2018

JournalACS Chemical Biology

Journal acronymACS Chem. Biol.

Volume13

Issue9

First page 2433

Last page2437

Number of pages5

ISSN1554-8929

eISSN1554-8937

DOIhttps://doi.org/10.1021/acschembio.8b00658(external)

Web address https://pubs.acs.org/doi/10.1021/acschembio.8b00658(external)

Self-archived copy’s web addresshttps://research.utu.fi/converis/portal/detail/Publication/35427475(external)


Abstract

Carbohydrate moieties are essential for the biological activity of
anthracycline anticancer agents such as nogalamycin, which contains l-nogalose and l-nogalamine units. The former of these is attached through a canonical O-glycosidic linkage, but the latter is connected via an unusual dual linkage composed of C–C and O-glycosidic bonds. In this work, we have utilized enzyme immobilization techniques and synthesized l-rhodosamine-thymidine diphosphate (TDP) from α-d-glucose-1-TDP
using seven enzymes. In a second step, we assembled the dual linkage
system by attaching the aminosugar to an anthracycline aglycone acceptor
using the glycosyl transferase SnogD and the α-ketoglutarate dependent
oxygenase SnoK. Furthermore, our work indicates that the auxiliary
P450-type protein SnogN facilitating glycosylation is surprisingly
associated with attachment of the neutral sugar l-nogalose rather than the aminosugar l-nogalamine in nogalamycin biosynthesis.


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