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Publications

2024

  • Enzymatic synthesis of S-adenosyl-L-homocysteine and its nucleoside analogs from racemic homocysteine thiolactone; Wen, X.,Leopold, V., Seebeck, F. P.; Chem. Sci. 2024.
  • https://doi.org/10.1002/cbic.202400258
  • Efficient Transferase Engineering for SAM Analog Synthesis from Iodoalkanes; Schülke, K. H., Fröse, J. S., Klein, A., Garcia-Borràs, M., Hammer, S. C.; ChemBioChem 2024.
    https://doi.org/10.1002/cbic.202400079

Important Preparatory Work (until 2023)

  • Biomimetic S-Adenosylmethionine Regeneration Starting from Multiple Byproducts Enables Biocatalytic Alkylation with Radical SAM Enzymes;
    Gericke, L., Mhaindarkar, D., Karst, L. C., Jahn, S., Kuge, M., Mohr, M. K. F., Gagsteiger, J., Cornelissen, N. V., Wen, X., Mordhorst, S., Jessen, H. J., Rentmeister, A., Seebeck, F. P., Layer, G., Lönarz, C., Andexer, J.; ChemBioChem 2023, 24 (9), e202300133
    https://doi.org/10.1002/cbic.202300133

  • Expanding the Substrate Scope of N- and O-Methyltransferases from Plants for Chemoselective Alkylation;
    Jockmann, E., Subrizi, F., Mohr, M. K. F., Carter, E. M., Hebecker, P. M., Popadić, D., Hailes, H. C., Andexer, J. N.; ChemCatChem 2023, 15 (22), e20230930.
    https://doi.org/10.1002/cctc.202300930
  • EnzymeML: Seamless Data Flow and Modeling of Enzymatic Data
    Lauterbach, S., Dienhart, H., Range, J., Malzacher, S., Spöring, J. D., Rother, D., Pinto, M. F., Martins, P., Lagerman, C. E., Bommarius, A. S., Høst, A. V., Woodley, J. M., Ngubane, S., Kudanga, T., Bergmann, F. T., Rohwer, J. M., Iglezakis, D., Weidemann, A., Wittig, U., Kettner, C., Swainston, N., Schnell, S., Pleiss; J. Nat. Methods 2023, 20 (3), 400-402.
    https://doi.org/10.1038/s41592-022-01763-1
  • Enzymatic Synthesis of l-Methionine Analogues and Application in a Methyltransferase Catalysed Alkylation Cascade;
    Mohr, M. K. F., Saleem-Batcha, R., Cornelissen, N., Andexer, J. N.; Chem. Eur. J. 2023, 29 (46), e202301503.
    https://doi.org/10.1002/chem.202301503
  • Noncanonical Functions of Enzyme Cofactors as Building Blocks in Natural Product Biosynthesis;
    Barra, L., Awakawa, T., Abe, I.; JACS Au 2022, 2, 9, 1950–1963.
    https://doi.org/10.1021/jacsau.2c00391

  • EnzymeML—a Data Exchange Format for Biocatalysis and Enzymology;
    Range, J., Halupczok, C., Lohmann, J., Swainston, N., Kettner, C., Bergmann, F. T., Weidemann, A., Wittig, U., Schnell, S., Pleiss, J.; FEBS J. 2022, 289 (19), 5864–5874.
    https://doi.org/10.1111/FEBS.16318
  • Biocatalytic One-Carbon Transfer - A Review;
    Germer, P., Andexer, J. N., Müller, M.; Synthesis 2022, 54 (20), 4401-4425
    https://doi.org/10.1055/s-0040-1719884
  • Selective Biocatalytic N-Methylation of Unsaturated Heterocycles
    Ospina, F., Schülke, K. H., Soler, J., Klein, A., Prosenc, B., Garcia-Borràs, M., Hammer, S. C.; Angew. Chem. Int. Ed. 2022, 61, e202213056.
    https://doi.org/10.1002/anie.202213056
  • β-NAD as a building block in natural product biosynthesis;
    Barra, L., Awakawa, T., Shirai, K., Hu, Z., Bashiri, G., Abe, I.; Nature 2021, 600, 754–758.
    https://doi.org/10.1038/s41586-021-04214-7
  • Engineered Enzymes Enable Selective N-Alkylation of Pyrazoles With Simple Haloalkanes;
    Bengel, L. L., Aberle, B., Egler-Kemmerer, A.-N., Kienzle, S., Hauer, B., Hammer, S. C.; Angew. Chem. Int. Ed. 2021, 60, 5554–5560.
    https://doi.org/10.1002/anie.202014239
  • Progress Curve Analysis within BioCatNet: Comparing Kinetic Models for Enzyme-Catalyzed Self-Ligation;
    Buchholz, P. C. F., Ohs, R., Spiess, A. C., Pleiss, J.; Biotechnol. J. 2019, 14 (3), 1–8.
    https://doi.org/10.1002/biot.201800183
  • Asymmetric C-Alkylation by the S-Adenosylmethionine-Dependent Methyltransferase SgvM;
    Sommer-Kamann, C.; Fries, A.; Mordhorst, S.; Andexer J. N.; Müller, M.; Angew. Chem. Int. Ed.; 2017, 56, 4033–4036.