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FOR5596 - SAM-dependent enzyme chemistry

@for5596.bsky.social
14 followers 18 following 24 posts

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

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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 24/08/2026
Our new Natural Product Report Viewpoint is out! It explores why SAM is not just SAM: beyond the canonical diastereomer, non-canonical forms exist; and many SAM-enzymes surprisingly tolerate them. What does this mean for enzyme evolution & biosynthesis? doi.org/10.1039/d6np...
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 19/08/2026
Greetings from our Summer School in Cologne Three days of science, exchange & inspiration. Including a visit to Bayer AG. Grateful for the connections made and conversations had across our research groups. Already looking forward to the next one!
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 28/04/2026
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.
chemistry-europe.onlinelibrary.wiley.com
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. ...
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 15/04/2026
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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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 20/03/2026
We organized a SAM session at the GDCh Biochemistry Conference 2026 in Würzburg. Research insights and results on the diversity of SAM-dependent enzymes were presented by several FOR5596 group members. Thank you all for the fruitfull discussions!
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 20/03/2026
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!
pubs.rsc.org
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...
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 03/03/2026
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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Reposted by FOR5596 - SAM-dependent enzyme chemistry
seebecklab.bsky.social @seebecklab.bsky.social · 12/12/2025
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.
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 01/12/2025
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.
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 17/11/2025
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
pubs.acs.org
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...
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 04/11/2025
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!
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 22/10/2025
We are preparing for the Science Days at Europa-Park (23.-25.10.25). We are encouraging pupils to pursue STEM!
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 14/10/2025
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.
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 08/09/2025
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!
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 02/07/2025
Greetings to all the doctoral researchers of the FOR5596 research unit who spent the last week at a summer school in Berlin!
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 30/04/2025
Congratulations to FOR5596 member Andrea @rentmeisterlab.bsky.social for receiving the Wittig-Grignard Award!! 🎉
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 17/04/2025
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
chemistry-europe.onlinelibrary.wiley.com
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...
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Reposted by FOR5596 - SAM-dependent enzyme chemistry
RentmeisterLab @rentmeisterlab.bsky.social · 09/04/2025
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 👌👏🤩
cell.com
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...
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Reposted by FOR5596 - SAM-dependent enzyme chemistry
AndexerLab @andexerlab.bsky.social · 04/04/2025
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/...
pubs.acs.org
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...
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FOR5596 - SAM-dependent enzyme chemistry @for5596.bsky.social · 02/04/2025
FOR 5596 is now on BlueSky! Follow us to stay informed about our collaborative project "Unfolding the potential of SAM-dependent enzyme chemistry".
logo of research group FOR 5596 on SAM-dependent enzyme chemistry showing the chemical structure of S-adenosylmethionine
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