Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures
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- Alice E. Parnell
- Chemistry, University of Southampton, Southampton, Hampshire SO17 1BJ, United Kingdom;
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- Silja Mordhorst
- Institute of Pharmaceutical Sciences, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany;
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- Florian Kemper
- Institute of Biochemistry, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany;
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- Mariacarmela Giurrandino
- Chemistry, University of Southampton, Southampton, Hampshire SO17 1BJ, United Kingdom;
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- Josh P. Prince
- Chemistry, University of Southampton, Southampton, Hampshire SO17 1BJ, United Kingdom;
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- Nikola J. Schwarzer
- Institute of Biochemistry, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany;
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- Alexandre Hofer
- Organic Chemistry Institute, University of Zürich, 8057 Zürich, Switzerland;
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- Daniel Wohlwend
- Institute of Biochemistry, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany;
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- Henning J. Jessen
- Organic Chemistry Institute, University of Zürich, 8057 Zürich, Switzerland;
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- Stefan Gerhardt
- Institute of Biochemistry, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany;
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- Oliver Einsle
- Institute of Biochemistry, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany;
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- Petra C. F. Oyston
- Institute for Life Sciences, University of Southampton, Southampton, Hampshire SO17 1BJ, United Kingdom;
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- Jennifer N. Andexer
- Institute of Pharmaceutical Sciences, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany;
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- Peter L. Roach
- Chemistry, University of Southampton, Southampton, Hampshire SO17 1BJ, United Kingdom;
書誌事項
- 公開日
- 2018-03-12
- 権利情報
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- http://www.pnas.org/site/aboutpnas/licenses.xhtml
- DOI
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- 10.1073/pnas.1710741115
- 公開者
- National Academy of Sciences
この論文をさがす
説明
<jats:title>Significance</jats:title> <jats:p>Polyphosphate kinases (PPKs) are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of novel antibiotics. The detailed knowledge of the mechanism of action and structure–function relationships of these enzymes is of utmost importance for the identification and design of new pharmaceutically active compounds and the rational improvement of lead structures. In addition, PPKs use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5′-mono- as well as 5′-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 115 (13), 3350-3355, 2018-03-12
National Academy of Sciences

