The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Enzymatic Synthesis of l ‐Methionine Analogues and Application in a Methyltransferase Catalysed Alkylation Cascade**
Open accessPublished version of a preprint
Abstract
Chemical modification of small molecules is a key step for the development of pharmaceuticals. S ‐adenosyl‐ l ‐methionine (SAM) analogues are used by methyltransferases (MTs) to transfer alkyl, allyl and benzyl moieties chemo‐, stereo‐ and regioselectively onto nucleophilic substrates, enabling an enzymatic way for specific derivatisation of a wide range of molecules. l ‐Methionine analogues are required for the synthesis of SAM analogues. Most of these are not commercially available. In nature, O ‐acetyl‐ l ‐homoserine sulfhydrolases (OAHS) catalyse the synthesis of l ‐methionine from O ‐acetyl‐ l ‐homoserine or l ‐homocysteine, and methyl mercaptan. Here, we investigated the substrate scope of Sc OAHS from Saccharomyces cerevisiae for the production of l ‐methionine analogues from l ‐homocysteine and organic thiols. The promiscuous enzyme was used to synthesise nine different l ‐methionine analogues with modifications on the thioether residue up to a conversion of 75 %. Sc OAHS was combined with an established MT dependent three‐enzyme alkylation cascade, allowing transfer of in total seven moieties onto two MT substrates. For ethylation, conversion was nearly doubled with the new four‐enzyme cascade, indicating a beneficial effect of the in situ production of l ‐methionine analogues with Sc OAHS.
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Cited by
Jockmann, E., Subrizi, F., Mohr, M. K. F., Carter, E. M., Hebecker, P. M., Popadić, D., Hailes, H. C., & Andexer, J. N. (2023) · ChemCatChem · doi:10.1002/cctc.202300930 · Cited by 19
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Metadata
- Authors
- Mohr, M. K. F., Saleem‐Batcha, R., Cornelissen, N. V., & Andexer, J. N.
- Affiliations
- University of Freiburg (DE)
- Institute of Pharmaceutical Sciences University of Freiburg Albertstr. 25 79104 Freiburg Germany
- University of Münster (DE)
- Corresponding author
- Andexer, Jennifer N.
- Venue
- Chemistry – A European Journal
- Publisher
- Wiley
- Published
- 2023-07-19
- Volume
- 29
- Issue
- 46
- Pages
- e202301503-e202301503
- ISSN
- 0947-6539 (ISSN-L)
- 1521-3765
- OpenAlex
- W4378373738
- Cited by
- 16
- References
- 34
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 6 · 2023: 1
- FWCI
- 1.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Chemistry - A European Journal (publishedVersion, other-oa)
- ChemRxiv (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, cc-by-nc-nd)
- FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
- Funders
- European Research Council (716966)
- Deutsche Forschungsgemeinschaft (Heisenberg Program)
- Deutsche Bundesstiftung Umwelt (PhD Scholarship)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Physical Sciences › Chemistry › Organic Chemistry › Asymmetric Synthesis and Catalysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- methyltransferase, Saccharomyces cerevisiae, L-homocysteine, enzymatic synthesis, substrate scope, ethylation
- MeSH terms
- Alkylation, Catalysis, Homocysteine, Homoserine, Methionine, Methyltransferases, S-Adenosylmethionine
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