Biomimetic S ‐Adenosylmethionine Regeneration Starting from Multiple Byproducts Enables Biocatalytic Alkylation with Radical SAM Enzymes **

Abstract: S‐Adenosylmethionine (SAM) is an enzyme cofactor involved in methylation, aminopropyl transfer, and radical reactions. This versatility renders SAM‐dependent enzymes of great interest in biocatalysis. The usage of SAM analogues adds to this diversity. However, high cost and instability of the cofactor impedes the investigation and usage of these enzymes. While SAM regeneration protocols from the methyltransferase (MT) byproduct S‐adenosylhomocysteine are available, aminopropyl transferases and radical SAM enzymes are not covered. Here, we report a set of efficient one‐pot systems to supply or regenerate SAM and SAM analogues for all three enzyme classes. The systems’ flexibility is showcased by the transfer of an ethyl group with a cobalamin‐dependent radical SAM MT using S‐adenosylethionine as a cofactor. This shows the potential of SAM (analogue) supply and regeneration for the application of diverse chemistry, as well as for mechanistic studies using cofactor analogues.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Biomimetic S ‐Adenosylmethionine Regeneration Starting from Multiple Byproducts Enables Biocatalytic Alkylation with Radical SAM Enzymes ** ; day:04 ; month:04 ; year:2023 ; extent:12
ChemBioChem ; (04.04.2023) (gesamt 12)

Creator
Gericke, Lukas
Mhaindarkar, Dipali
Karst, Lukas C.
Jahn, Sören
Kuge, Marco
Mohr, Michael K. F.
Gagsteiger, Jana
Cornelissen, Nicolas V.
Wen, Xiaojin
Mordhorst, Silja
Jessen, Henning Jacob
Rentmeister, Andrea
Seebeck, Florian Peter
Layer, Gunhild
Lönarz, Christoph
Andexer, Jennifer Nina

DOI
10.1002/cbic.202300133
URN
urn:nbn:de:101:1-2023040415280566038266
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
14.08.2025, 11:01 AM CEST

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