FOR5596 - SAM-dependent enzyme chemistry

@for5596.bsky.social

"Unfolding the potential of SAM-dependent enzyme chemistry" Research group funded by the DFG https://for5596.uni-freiburg.de/

Our new ChemBioChem article is out! It explores chemo- and regioselectivity in SAM-dependent aromatic C-methyltransferases. We show that SfmM2 and NapB5 catalyze context-dependent C-dimethylation as well as C- and O-methylation of flavonoids, governed by binding geometry and nucleophile positioning.

Context‐Dependent Chemoselectivity of Aromatic C‐Methyltransferases

Chemoselectivity is context-dependent: The SAM-dependent C-MTs SfmM2 and NapB5 from streptomycetes catalyze the C- and/or O-dimethylation of aromatic substrates, including l-tyrosine and flavonoids. ...

chemistry-europe.onlinelibrary.wiley.com

Late greetings from the Annual Conference of the Association for General and Applied Microbiology (VAAM), 22.-25.03.2026, Berlin. Our FOR5596 group member Tingyi Zhan presented her work on 'SAM- and cobalamin- dependent conversion of estrogens into androgens'. Thank you for the great talk!

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Our new J. Nat. Prod. review is out! It explores how enzymes install methyl groups into sugars of natural products; driving structural diversity and biological activity. Enzymatic strategies enable targeted creation of new chemical structures. Congrats to all authors from FOR5596!

Glucose 6-phosphate: the diversity of C-methylation in sugar moieties within natural product biosynthesis

Covering: Up to 2026Methylation is one of the most frequent and functionally significant modifications in natural product biosynthesis. This transformation generally involves the cosubstrate S-adenosy...

pubs.rsc.org

Greetings from the 38th Irsee Natural Product Symposium in Irsee, Germany. We had the pleasure of organizing a SAM session featuring Prof. Dr. Jörg Pietruszka, Prof. Dr. Andreas Kirschning, and Dr. Anna Vagstad as guest speakers. Thank you for the inspiring talks and stimulating discussions!

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We are organizing a session on SAM-dependent enzymes at the 38th Irsee Natural Product Symposium, February 25-27, 2026. We are pleased to welcome the following speakers: Prof. Andrea Rentmeister, Prof. Jörg Pietruszka, and Prof. Andreas Kirschning. Please spread the news and join us in Irsee!

Ever wondered why prenylation and methylation use different cofactor scaffolds? We now show that the SAM scaffold enables both: Chimeric cofactors enable methyltransferase-catalyzed prenylation: Chem www.cell.com/chem/fulltex... Kudos to @nicocorn.bsky.social & Arne Hoffmann and all authors 👌👏🤩

Chimeric cofactors enable methyltransferase-catalyzed prenylation

In nature, many methyltransferases (C1) use S-adenosyl-l-methionine (AdoMet or SAM) as a cofactor for methyl transfer, whereas prenyltransferases (C5) use dimethylallyl diphosphate (DMAPP). We enginee...

cell.com