Supporting Information
| Supporting Information File 1: Details of materials and methods and additional figures and tables. | ||
| Format: PDF | Size: 1014.1 KB | Download |
Cite the Following Article
Make or break: the thermodynamic equilibrium of polyphosphate kinase-catalysed reactions
Michael Keppler, Sandra Moser, Henning J. Jessen, Christoph Held and Jennifer N. Andexer
Beilstein J. Org. Chem. 2022, 18, 1278–1288.
https://doi.org/10.3762/bjoc.18.134
How to Cite
Keppler, M.; Moser, S.; Jessen, H. J.; Held, C.; Andexer, J. N. Beilstein J. Org. Chem. 2022, 18, 1278–1288. doi:10.3762/bjoc.18.134
Download Citation
Citation data can be downloaded as file using the "Download" button or used for copy/paste from the text window
below.
Citation data in RIS format can be imported by all major citation management software, including EndNote,
ProCite, RefWorks, and Zotero.
Presentation Graphic
| Picture with graphical abstract, title and authors for social media postings and presentations. | ||
| Format: PNG | Size: 9.1 MB | Download |
Citations to This Article
Up to 20 of the most recent references are displayed here.
Scholarly Works
- Kuge, M.; Keppler, M.; Friedrich, F.; Saleem-Batcha, R.; Winter, J.; Prucker, I.; Germer, P.; Gerhardt, S.; Einsle, O.; Jung, M.; Jessen, H. J.; Andexer, J. N. Structural Insights into Broad-Range Polyphosphate Kinase 2-II Enzymes Applicable for Pyrimidine Nucleoside Diphosphate Synthesis. Chembiochem : a European journal of chemical biology 2025, 26, e202400970. doi:10.1002/cbic.202400970
- Kuge, M.; Keppler, M.; Friedrich, F.; Saleem-Batcha, R.; Winter, J.; Prucker, I.; Germer, P.; Gerhardt, S.; Einsle, O.; Jung, M.; Jessen, H. J.; Andexer, J. N. Structural Insights into Broad-Range Polyphosphate Kinase 2-II Enzymes Applicable for Pyrimidine Nucleoside Diphosphate Synthesis. Cold Spring Harbor Laboratory 2024. doi:10.1101/2024.11.26.625422
- Höfmann, S.; Schmerling, C.; Stracke, C.; Niemeyer, F.; Schaller, T.; Snoep, J. L.; Bräsen, C.; Siebers, B. The archaeal family 3 polyphosphate kinase reveals a function of polyphosphate as energy buffer under low energy charge. 2024. doi:10.1101/2024.08.28.610084
- Mitton-Fry, R. M.; Eschenbach, J.; Schepers, H.; Rasche, R.; Erguven, M.; Kümmel, D.; Rentmeister, A.; Cornelissen, N. V. Chemo-enzymatic production of base-modified ATP analogues for polyadenylation of RNA. Chemical science 2024, 15, 13068–13073. doi:10.1039/d4sc03769c
- Querengässer, T.; Wenzlaff, J.; Loderer, C. Broadening the Substrate Scope of a Polyphosphate Kinase for Canonical and Non‐Canonical Nucleotides. ChemCatChem 2024, 16. doi:10.1002/cctc.202400181
- Li, Z.-L.; Sun, C.-Q.; Qing, Z.-L.; Li, Z.-M.; Liu, H.-L. Engineering the thermal stability of a polyphosphate kinase by ancestral sequence reconstruction to expand the temperature boundary for an industrially applicable ATP regeneration system. Applied and environmental microbiology 2024, 90, e0157423. doi:10.1128/aem.01574-23
- Siedentop, R.; Prenzel, T.; Waldvogel, S. R.; Rosenthal, K.; Lütz, S. Reaction Engineering and Comparison of Electroenzymatic and Enzymatic ATP Regeneration Systems. ChemElectroChem 2023, 10. doi:10.1002/celc.202300332
- Benčić, P.; Keppler, M.; Kuge, M.; Qiu, D.; Schütte, L. M.; Häner, M.; Strack, K.; Jessen, H. J.; Andexer, J. N.; Loenarz, C. Non-canonical nucleosides: Biomimetic triphosphorylation, incorporation into mRNA and effects on translation and structure. The FEBS journal 2023, 290, 4899–4920. doi:10.1111/febs.16889
- Siedentop, R.; Siska, M.; Möller, N.; Lanzrath, H.; von Lieres, E.; Lütz, S.; Rosenthal, K. Bayesian Optimization for an ATP-Regenerating In Vitro Enzyme Cascade. Catalysts 2023, 13, 468. doi:10.3390/catal13030468
