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On the flexibility of the cellular amination network in E. coli

View ORCID ProfileHelena Schulz-Mirbach, View ORCID ProfileAlexandra Müller, Tong Wu, View ORCID ProfilePascal Pfister, Selçuk Aslan, Lennart Schada von Borzyskowski, Tobias J. Erb, View ORCID ProfileArren Bar-Even, View ORCID ProfileSteffen N. Lindner
doi: https://doi.org/10.1101/2022.01.25.477661
Helena Schulz-Mirbach
1Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam, Germany
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  • ORCID record for Helena Schulz-Mirbach
Alexandra Müller
1Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam, Germany
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Tong Wu
1Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam, Germany
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Pascal Pfister
2Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Str. 10, D-35043 Marburg, Germany
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  • ORCID record for Pascal Pfister
Selçuk Aslan
1Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam, Germany
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Lennart Schada von Borzyskowski
2Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Str. 10, D-35043 Marburg, Germany
3Institute of Biology Leiden, Leiden University, Sylviusweg 72, 2333 BE Leiden, The Netherlands
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Tobias J. Erb
2Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Str. 10, D-35043 Marburg, Germany
4Center for Synthetic Microbiology (SYNMIKRO), Karl-von-Frisch-Str. 16, D-35043 Marburg, Germany
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Arren Bar-Even
1Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam, Germany
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Steffen N. Lindner
1Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam, Germany
5Department of Biochemistry, Charité Universitätsmedizin, Virchowweg 6, 10117 Berlin, Germany
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  • For correspondence: lindner@mpimp-golm.mpg.de
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Abstract

Ammonium (NH4+) is essential to generate the nitrogenous building blocks of life. It gets assimilated via the canonical biosynthetic routes to glutamate and is further distributed throughout metabolism via a network of transaminases. To study the flexibility of this network, we constructed an Escherichia coli glutamate auxotrophic strain. This strain allowed us to systematically study which amino acids serve as amine source and found that several amino acids complement the auxotrophy, either by producing glutamate via transamination reactions or by their conversion to glutamate. In this network, we identified aspartate transaminase AspC as a major connector between many amino acids and glutamate. Additionally, we extended the transaminase network by the amino acids β-alanine, alanine, glycine and serine as new amine sources and identified D-amino acid dehydrogenase (DadA) as an intracellular amino acid sink removing substrates from transaminase reactions. Finally, ammonium assimilation routes producing aspartate or leucine were introduced. Our study reveals the high flexibility of the cellular amination network, both in terms of transaminase promiscuity and adaptability to new connections and ammonium entry points.

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Posted January 27, 2022.
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On the flexibility of the cellular amination network in E. coli
Helena Schulz-Mirbach, Alexandra Müller, Tong Wu, Pascal Pfister, Selçuk Aslan, Lennart Schada von Borzyskowski, Tobias J. Erb, Arren Bar-Even, Steffen N. Lindner
bioRxiv 2022.01.25.477661; doi: https://doi.org/10.1101/2022.01.25.477661
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On the flexibility of the cellular amination network in E. coli
Helena Schulz-Mirbach, Alexandra Müller, Tong Wu, Pascal Pfister, Selçuk Aslan, Lennart Schada von Borzyskowski, Tobias J. Erb, Arren Bar-Even, Steffen N. Lindner
bioRxiv 2022.01.25.477661; doi: https://doi.org/10.1101/2022.01.25.477661

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