FOR5596 - SAM-dependent enzyme chemistry

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!

Congratulations on this excellent publication!

We are excited to report an E. coli strain with an artificial SAM-cycle (pubs.acs.org/articlesonre...). Congratulations to Zhong, Wen and Seseg for their excellent team effort.

We took a deeper look at "Kinetic Modeling and Parametrization of Cascade Reactions with NMRPy and PySCeS" with Prof. Johann Rohwer. Thank you for the insightful talk and fruitful discussions.

In Vitro Characterization of the Aromatic SAM-Dependent C-Methyltransferase NapB5 Aromatic polyketide synthase (PKS) products undergo diverse tailoring reactions in the biosynthesis of natural products. S-Adenosyl-l-methionine (SAM)-dependent C-methyltransferases (C-MTs) play a key...

Our new J. Nat. Prod. study is out! Discover how the enzyme NapB5 achieves precise dual C-methylation and expands natural-product diversity across Actinomycetes.

Congratulation to all authors from FOR5596! @andexerlab.bsky.social

Late greetings from the Science Days at Europa-Park! We are impressed by all the motivated school kids interested in STEM! Thank you to all our team members for your help!

SCIENCE & TECHNOLOGIE Science & Technologie führt Kinder und Jugendliche an Themen in den Bereichen Wissenschaft und Technologie heran.

science-days.de

We are preparing for the Science Days at Europa-Park (23.-25.10.25). We are encouraging pupils to pursue STEM!

Greetings from all of our members at the three-day annual meeting in St. Peter in 2025. Thank you for a successfull year filled with hard work, collaboration, great ideas and a lot of motivation for our future research.

We are also looking forward to the presentations by Dr. Anna Vagstad and our group member, Tenure-Track Professor Dr. Lena Barra @barra-lab.bsky.social, at the Young Researchers Session in Irsee.

@rentmeisterlab.bsky.social

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!

Greetings to all the doctoral researchers of the FOR5596 research unit who spent the last week at a summer school in Berlin!

Congratulations to FOR5596 member Andrea @rentmeisterlab.bsky.social for receiving the Wittig-Grignard Award!! 🎉

Of course, also greetings to @seebecklab.bsky.social @nicocorn.bsky.social and all the other authors <3

Biomimetic S‐Adenosylmethionine Regeneration Starting from Multiple Byproducts Enables Biocatalytic Alkylation with Radical SAM Enzymes** The biomimetic regeneration system for S-adenosylmethionine (SAM) and SAM analogues presented is based on the salvage of the adenine moiety and in situ supply of d-ribose and polyphosphate. It is com...

Congratulations to all the authors of this paper, which just ranked in the top 10% of the most viewed papers published in ChemBioChem in 2023! We are very excited to be able to build on this amazing work in our FOR5596 research group.

@andexerlab.bsky.social @rentmeisterlab.bsky.social

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...

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 👌👏🤩

New FOR5596 paper from the Müller, Garcia Borràs and Andexer groups!

How to Tell an N from an O: Controlling the Chemoselectivity of Methyltransferases S-Adenosyl-l-methionine (SAM)-dependent methyltransferases (MTs) are important enzymes in numerous biological pathways. They share a common SN2 mechanism but act on different nucleophilic substrates i...

If you want to know how to tell an N from an O, you can get some ideas in our new paper. This was a great team effort, introducing us to new methods: MD w/ Ferran Feixas & Marc Garcia Borràs (Girona) + HDX-MS w/ Wieland Steinchen & Gert Bange @bangebalcony.bsky.social
pubs.acs.org/doi/10.1021/...

logo of research group FOR 5596 on SAM-dependent enzyme chemistry showing the chemical structure of S-adenosylmethionine

FOR 5596 is now on BlueSky! Follow us to stay informed about our collaborative project "Unfolding the potential of SAM-dependent enzyme chemistry".