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Publications Andexer Lab

2025
E. Jockmann, H. Girame, W. Steinchen, K. Kind, G. Bange, K. Tittmann, M. Müller, F. Feixas, M. Garcia-Borràs, J. N. Andexer, ACS Catal. 2025, 15, 8, 6410-6425, DOI: 10.1021/acscatal.5c00834.
M. K. F. Mohr, A. Satanowski, S. N. Lindner, T. J. Erb, J. N. Andexer, Microb. Cell Fact. 2025, 24, 55,
DOI: 10.1186/s12934-025-02674-4.
P. Germer, J. N. Andexer, Trendberichte Organische Chemie 2024: Enzymreaktionen, Nachr. Chem. 2025, 73, 46-47, DOI: 10.1002/nadc.20254147860.
M. Kuge, M. Keppler, F. Friedrich, R. Saleem-Batcha, J. Winter, I. Prucker, P. Germer, S. Gerhardt, O. Einsle, M. Jung, H. J. Jessen, J. N. Andexer, ChemBioChem 2025, DOI: 10.1002/cbic.202400970.
This research article has been highlighted as VIP (Very Important Paper) in ChemBioChem 2025.
2024
M. K. F. Mohr, P. Benčić, J. N. Andexer, Doping In Vivo Alkylation in E. coli by Introducing the Direct Sulfurylation Pathway of S. cerevisiae, Angew. Chem. Int. Ed. 2024, DOI: 10.1002/anie.202414598.
C. Sommer-Kamann, J. Breiltgens, Z. Zou, S. Gerhardt, R. Saleem-Batcha, F. Kemper, O. Einsle, J. N. Andexer, M. Müller, ChemBioCHem 2024, DOI: 10.1002/cbic.202400258.
LH. Köppl, D. Popadić, R. Saleem-Batcha, P. Germer, J. N. Andexer, Commun Biol 2024,
DOI: 10.1038/s42003-024-06078-9.
J. N. Andexer, P. Germer, Trendberichte Organische Chemie 2024: Enzymreaktionen, Nachr. Chem. 2024, 72, 49, DOI: 10.1002/nadc.20244139258.
2023
E. Abdelraheem, E. Jockmann, J. Li, S. Guenter, J. N. Andexer, P-L. Hagedoorn, U. Hanefeld, Enzymatic S-Methylation of Thiols Catalyzed by Different O-Methyltransferases, ChemCatChem 2023,
DOI: 10.1002/cctc.202301217.
E. Jockmann, F. Subrizi, M. K. F. Mohr, E. M. Carter, P. M. Hebecker, D. Popadić, H. C. Hailes, J. N. Andexer, Expanding the Substrate Scope of N- and O-Methyltransferases from Plants for Chemoselective Alkylation, ChemCatChem 2023, DOI: 10.1002/cctc.202300930.
P. Benčić, M. Keppler, M. Kuge, D. Qiu, L. M. Schütte, M. Häner, K. Strack, H. J. Jessen, J. N. Andexer, C. Loenarz, Non-canonical nucleosides: Biomimetic triphosphorylation, incorporation into mRNA and effects on translation and structure, The FEBS Journal 2023, DOI 10.1111/febs.16889.
M. K. F. Mohr, R. Saleem-Batcha, N. V. Cornelissen, J. N. Andexer, Enzymatic Synthesis of L-Methionine Analogues and Application in a Methyltransferase Catalysed Alkylation Cascade, Chemistry – A European Journal 2023, DOI: 10.1002/chem.202301503.
L. Gericke, D. Mhaindarkar, L. C. Karst, S. Jahn, M. Kuge, M. K. F. Mohr, J. Gagsteiger, N. V. Cornelissen, X. Wen, S. Mordhorst, H. J. Jessen, A. Rentmeister, F. P. Seebeck, G. Layer, C. Loenarz, J. N. Andexer, Biomimetic S-Adenosylmethionine Regeneration Starting from Multiple Byproducts Enables Biocatalytic Alkylation with Radical SAM Enzymes, ChemBioChem 2023, DOI: 10.1002/cbic.202300133.
P. Germer, W. Hüttel, J. N. Andexer, Trendberichte Organische Chemie 2023: Enzymreaktionen, Nachr. Chem. 2023, 71, 49, DOI: 10.1002/nadc.20234135542.
2022
M. Keppler, S. Moser, H. J. Jessen, C. Held, J. N. Andexer, Make or break: the thermodynamic equilibrium of polyphosphate kinase-catalysed reactions, Beilstein J. Org. Chem. 2022, DOI: 10.3762/bjoc.18.134.
T. M. Haas, B.-J. Laventie, S. Lagies, C. Harter, I. Prucker, D. Ritz, R. Saleem-Batcha, D. Qiu, W. Hüttel, J. Andexer, B. Kammerer, U. Jenal, H. J. Jessen, Photoaffinity Capture Compounds to Profile the Magic Spot Nucleotide, Angew. Chem. Int. Ed. 2022, DOI: 10.1002/anie.202201731.
This research article has been highlighted as Hot Paper in Biological Activity.
E. Abdelraheem, B. Thair, R. F. Varela, E. Jockmann, D. Popadić, H. C. Hailes, J. M. Ward, A. M. Iribarren, E. S. Lewkowicz, J. N. Andexer, P. Hagedoorn, U. Hanefeld, Methyltransferases: Functions and Applications,  ChemBioChem 2022, DOI: 10.1002/cbic.202200212.
This research article has been highlighted as VIP (Very Important Paper) in ChemBioChem 2022.
A. Fries, L. Mazzaferro, P. Bisel, F. Hubrich, J. N. Andexer, M. Müller, Biosynthesis of Menaquinone in E. coli: Identification of an Elusive Isomer of SEPHCHC, ChemBiochem 2022, 23, e202200181,
DOI: 10.1002/cbic.202200181.
J. Gagsteiger, S. Jahn, L. Heidinger, L. Gericke, J. N. Andexer, T. Friedrich, C. Loenarz, G. Layer, A Cobalamin-Dependent Radical SAM Enzyme Catalyzes the Unique Cα-Methylation of Glutamine in Methyl-Coenzyme M Reductase, Angew. Chem. Int. Ed. 2022, 134, e202204198, DOI: 10.1002/ange.202204198.
This research article has been highlighted as Hot Paper in Metalloproteins.
P. Germer, J. N. Andexer, M. Müller, Biocatalytic One-Carbon Transfer – A Review, Synthesis 2022, 54, 4401–4425, DOI: 10.1055/s-0040-1719884.
W. Hüttel, J. N. Andexer, Trendberichte Organische Chemie 2022: Enzymreaktionen, Nachr. Chem. 2022, 70, 63, DOI: 10.1002/nadc.20224122453
2021
F. Subrizi, Y. Wang, B. Thair, D. Méndez-Sánchez, R. Roddan, M. Cárdenas-Fernández, J. Siegrist, M. Richter, J. N. Andexer, J. M. Ward, H. C. Hailes, Multienzyme One-Pot Cascades Incorporating Methyltransferases for the Strategic Diversification of Tetrahydroisoquinoline Alkaloids, Angewandte Chemie 2021, DOI: 10.1002/ange.202104476.
M. Becker, P. Nikel, J. N. Andexer, S. Lütz, K. Rosenthal, A Multi-Enzyme Cascade Reaction for the Production of 2’3’‑cGAMP. Biomolecules 2021, DOI: 10.3390/biom11040590.
D. Popadić, D. Mhaindarkar, M. H. N. Dang Thai, H. C. Hailes, S. Mordhorst, J. N. Andexer, A bicyclic S-adenosylmethionine regeneration system applicable with different nucleosides or nucleotides as cofactor building blocks. RSC Chem. Biol. 2021, DOI 10.1039/D1CB00033K.
This research article received the RSC Outstanding Paper Award 2021.
F. Hubrich, M. Müller, J. N. Andexer, Chorismate- and isochorismate converting enzymes: versatile catalysts acting on an important metabolic node. Chem. Commun. 2021, DOI 10.1039/D0CC08078K.
J. N. Andexer, W. Hüttel, Trendberichte Organische Chemie 2021: Enzymreaktionen, Nachr. Chem. 2021, 69, 61, DOI: 10.1002/nadc.20214105947.
2020
R. Roddan, A. Sula, D. Méndez-Sánchez, F. Subrizi, B. R. Lichman, J. Broomfield, M. Richter, J. N. Andexer, J. M. Ward, N. H. Keep, H. C. Hailes. Single step syntheses of (1S)-aryl-tetrahydroisoquinolines by norcoclaurine synthases. Commun. Chem. 2020, 3, 1–10, DOI: 10.1038/s42004-020-00416-8.
C. Jacoby, J. Krull, J. Andexer, N. Jehmlich, M. von Bergen, T. Brüls, M. Boll. Channeling C1 Metabolism toward S-Adenosylmethionine-Dependent Conversion of Estrogens to Androgens in Estrogen-Degrading Bacteria. mBio 2020, 11, DOI 10.1128/mBio.01259-20.
J. N. Andexer, A. Rentmeister. Challenging nature’s preference for methylation. Nat. Chem. 2020, 12, 791–792, DOI: 10.1038/s41557-020-0533-1.
S. Mordhorst, J. N. Andexer. Round, round we go – strategies for enzymatic cofactor regeneration. Nat. Prod. Rep. 2020, DOI: 10.1039/D0NP00004C.
W. Hüttel, J. N. Andexer, Trendberichte Organische Chemie 2020: Enzymreaktionen, Nachr. Chem. 2020, 68, 69–70, DOI: 10.1002/nadc.20204095515.
2019
G. A. Strohmeier, A. Schwarz, J. N. Andexer, M. Winkler. Co-factor demand and regeneration in the enzymatic one-step reduction of carboxylates to aldehydes in cell-free systems. J. Biotechnol. 2019, DOI 10.1016/j.jbiotec.2019.10.016.
M. J. Grüninger, P. C. F. Buchholz, S. Mordhorst, P. Strack, M. Müller, F. Hubrich, J. Pleiss, J. N. Andexer. Chorismatases - the family is growing. Org. Biomol. Chem. 2019, 17, 2092–2098. DOI 10.1039/C8OB03038C.
S. Mordhorst, J. Singh, M. K. F. Mohr, R. Hinkelmann, M. Keppler, H. J. Jessen, J. N. Andexer. Several Polyphosphate Kinase 2 Enzymes Catalyse the Production of Adenosine 5′-Polyphosphates. ChemBioChem 2019, 20, 1019–1022, DOI: 10.1002/cbic.201800704.
S. Lüdeke, J. N. Andexer, Trendberichte Organische Chemie 2019: Enzymreaktionen, Nachr. Chem. 2019, 67, 75–77, DOI: 10.1002/nadc.20194085243.
2018
J. N. Andexer, Enzymatische Methylierung in vitro: im Kreis herum oder „nur“ geradeaus?. Biospektrum 24, 556–557 (2018), DOI: 10.1007/s12268-018-0955-0.
A. E. Parnell, S. Mordhorst, F. Kemper, M. Giurrandino, J. P. Prince, N. J. Schwarzer, A. Hofer, D. Wohlwend, H. J. Jessen, S. Gerhardt, O. Einsle, P. C. F. Oyston, J. N. Andexer and P. L. Roach. Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures. PNAS 2018, 115, 3350–3355, DOI: 10.1073/pnas.1710741115.
S. Lüdeke, J. N. Andexer, Trendberichte Organische Chemie 2017: Enzymreaktionen, Nachr. Chem. 2018, 66, 278–279, DOI: 10.1002/nadc.20184072148.
2017 S. Mordhorst, A. Maurer, D. Popadić, J. Brech, J. N. Andexer. A Flexible Polyphosphate-Driven Regeneration System for Coenzyme A Dependent Catalysis. ChemCatChem 2017, 9, 4164,
DOI: doi.org/10.1002/cctc.201700848.
C. Sommer-Kamann, A. Fries, S. Mordhorst, J. N. Andexer, M. Müller. Asymmetric C-Alkylation by the S-Adenosylmethionine-Dependent Methyltransferase SgvM. Angew. Chem. 2017, 129, 4091,
DOI: 10.1002/ange.201609375.
S. Mordhorst, J. Siegrist, M. Müller, M. Richter, J. N. Andexer. Catalytic Alkylation Using a Cyclic S-Adenosylmethionine Regeneration System. Angew. Chem. Int. Ed. 2017, 156, 4037–4041,
DOI: 10.1002/anie.201611038. This research article has been highlighted as Hot Paper in Biocatalysis.
J. Siegrist, J. Netzer, S. Mordhorst, L. Karst, S. Gerhardt, O.Einsle, M.Richter, J. N. Andexer. Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity. FEBS Letters 2017, 591, 312–321, DOI: 10.1002/1873-3468.12530.
W. Hüttel, J. N. Andexer, Trendberichte Organische Chemie 2016: Enzymreaktionen und katalytisch aktive Proteine, Nachr. Chem. 2017, 65, 302–304, DOI: 10.1002/nadc.20174059831.
2016 W. Hüttel, J. N. Andexer, Trendberichte Organische Chemie: Enzymreaktionen, Nachr. Chem. 2016, 64, 289–291, DOI: 10.1002/nadc.20164047492.
2015 J. Siegrist, S. Aschwanden, S. Mordhorst, L. Thöny-Meyer, M. Richter, J. N. Andexer. Regiocomplementary O-Methylation of Catechols by Using Three-Enzyme Cascades ChemBioChem 2015, 16, 2576–2579,
DOI: 10.1002/cbic.201500410. The research article is being featured on the back cover.
J. N. Andexer and M.Richter. Emerging Enzymes for ATP Regeneration in Biocatalytic Processes. ChemBioChem 2015, 16, 380–386, DOI: 10.1002/cbic.201402550.
W. Hüttel, J. N. Andexer, Trendberichte Organische Chemie 2014: Enzymreaktionen, Nachr. Chem. 2015, 63, 300–303, DOI: 10.1002/nadc.201590092.
2014 F. Hubrich, M. Müller, J. N. Andexer. In vitro production and purification of isochorismate using a two-enzyme cascade. J. Biotechnol. 2014, 191, 93–98, DOI: 10.1016/j.jbiotec.2014.06.003.
J. N. Andexer, W. Hüttel. Trendberichte Organische Chemie 2013: Enzymreaktionen, Nachr. Chem. 2014, 62, 278–280, DOI: 10.1002/nadc.201490086.
N. Kandziora, J. N. Andexer, S. J. Moss, B. Wilkinson, P. F. Leadlay, F. Hahn. Uncovering the origin of Z-configured double bonds in polyketides: intermediate E-double bond formation during borrelidin biosynthesis. Chemical Science 2014, 5, 3563–3567, DOI: 10.1039/C4SC00883A.
2013 P. Juneja, F. Hubrich, K. Diederichs, W. Welte, J.N. Andexer. Mechanistic Implications for the Chorismatase FkbO Based on the Crystal Structure. J. Mol. Biol. 2013, 426, 105–115, DOI: 10.1016/j.jmb.2013.09.006.
J. Schlesier, J. Siegrist, S. Gerhardt, A. Erb, S. Blaesi, M. Richter, O. Einsle, J.N. Andexer. Structural and functional characterisation of the methionine adenosyltransferase from Thermococcus kodakarensis. BMC Struct. Biol. 2013, 13, 22, DOI: 10.1186/1472-6807-13-22.
J. N. Andexer, M. Müller: Trendberichte Organische Chemie 2012: Enzymreaktionen, Nachr. Chem. 2013, 61, 286–288, DOI: 10.1002/nadc.201390087.
F. Hubrich, S. Mordhorst, J. N. Andexer. Cinnamic acid derivatives as inhibitors for chorismatases and isochorismatases. Bioorg. Med. Chem. Lett. 2013, 23, 1477–1481, DOI: 10.1016/j.bmcl.2012.12.059.
2012 J. N. Andexer, N. Staunig, T. Eggert, C. Kratky, M. Pohl, K. Gruber. Hydroxynitrile lyases with α/β-hydrolase fold: two enzymes with almost identical 3D-structures but opposite enantioselectivities and different reaction mechanisms. ChemBioChem. 2012, 13, 1932–1939, DOI: 10.1002/cbic.201200239.
J. N. Andexer, M. Müller: Trendberichte Organische Chemie 2011: Enzymreaktionen, Nachr. Chem. 2012, 60, 294–296, DOI: 10.1002/nadc.201290119.
2011 O. Vergnolle, F. Hahn, A. Baerga-Ortiz, P. F. Leadlay, J. N. Andexer. Stereoselectivity of Isolated Dehydratase Domains of the Borrelidin Polyketide Synthase: Implications for cis Double Bond Formation. ChemBioChem. 2011, 12, 1011–1014, DOI: 10.1002/cbic.201100011.
J. N. Andexer, S. G. Kendrew, M. Nur-e-Alam, O. Lazos, T. A. Foster, A.-S. Zimmermann, T. D. Warneck, D. Suthar, N. J. Coates, F. E. Koehn, J. S. Skotnicki, G. T. Carter, M. A. Gregory, C. J. Martin, S. J. Moss, P. F. Leadlay, B. Wilkinson. Biosynthesis of the immunosuppressants FK506, FK520, and rapamycin involves a previously undescribed family of enzymes acting on chorismate. Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 4776–4781, DOI: 10.1073/pnas.1015773108.
2009 J.N. Andexer, J. von Langermann, U. Kragl, M. Pohl. How to overcome limitations in biotechnological processes - examples from hydroxynitrile lyase applications. Trends Biotechnol. 2009, 27, 599–607,
DOI: 10.1016/j.tibtech.2009.07.005.
J.-K. Guterl, J.N. Andexer, T. Sehl, J. von Langermann, I. Frindi-Wosch, T. Rosenkranz, J. Fitter, K. Gruber, U. Kragl, T. Eggert, M. Pohl. Uneven Twins: Comparison of two enantio¬complementary hydroxynitrile-lyases with an α/β-hydrolase fold. J. Biotechnol. 2009, 141, 166–173, DOI: 10.1016/j.jbiotec.2009.03.010.
2008 T. Eggert, S. A. Funke, J. N. Andexer, M. T. Reetz, K.-E. Jaeger. Evolution of Enantioselective Bacillus subtilis Lipase. In: S. Lutz, U. T. Bornscheuer (eds), Protein Engineering Handbook, WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. 2008, DOI: 10.1002/9783527634026.ch17.
2007 J. Andexer, J. von Langermann, A. Mell, M. Bocola, U. Kragl, T. Eggert, M. Pohl. An R-selective Hydroxynitrile Lyase from Arabidopsis thaliana with an α/β-hydrolase fold. Angew. Chem., Int. Ed. 2007, 46, 8679–8681, DOI: 10.1002/anie.200701455.
2006 T. Eggert, J. Andexer. (R)-Hydroxynitril-Lyase aus Brassicaceen. Patent Application DE 10 2006 058 373 A1 und WO 2008 067807 A2. 2006
J. Andexer, J.-K. Guterl, M. Pohl, T. Eggert. A high-throughput screening assay for hydroxynitrile lyase activity. Chem. Commun. 2006, 40, 4201–4203, DOI: 10.1039/B607863J.