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Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo

Author

Listed:
  • Maren Nattermann

    (Max Planck Institute for Terrestrial Microbiology)

  • Sebastian Wenk

    (Max Planck Institute of Molecular Plant Physiology)

  • Pascal Pfister

    (Max Planck Institute for Terrestrial Microbiology)

  • Hai He

    (Max Planck Institute for Terrestrial Microbiology)

  • Seung Hwan Lee

    (University of South Florida)

  • Witold Szymanski

    (Institute of Translational Proteomics, Philipps University)

  • Nils Guntermann

    (Institute of Technical and Macromolecular Chemistry, RWTH Aachen University)

  • Fayin Zhu

    (University of South Florida)

  • Lennart Nickel

    (Ruprecht Karl University)

  • Charlotte Wallner

    (Philipps University)

  • Jan Zarzycki

    (Max Planck Institute for Terrestrial Microbiology)

  • Nicole Paczia

    (Max Planck Institute for Terrestrial Microbiology)

  • Nina Gaißert

    (Festo SE & Co. KG)

  • Giancarlo Franciò

    (Institute of Technical and Macromolecular Chemistry, RWTH Aachen University)

  • Walter Leitner

    (Institute of Technical and Macromolecular Chemistry, RWTH Aachen University
    Max Planck Institute for Chemical Energy Conversion)

  • Ramon Gonzalez

    (University of South Florida)

  • Tobias J. Erb

    (Max Planck Institute for Terrestrial Microbiology
    Center for Synthetic Microbiology (SYNMIKRO))

Abstract

Formate can be envisioned at the core of a carbon-neutral bioeconomy, where it is produced from CO2 by (electro-)chemical means and converted into value-added products by enzymatic cascades or engineered microbes. A key step in expanding synthetic formate assimilation is its thermodynamically challenging reduction to formaldehyde. Here, we develop a two-enzyme route in which formate is activated to formyl phosphate and subsequently reduced to formaldehyde. Exploiting the promiscuity of acetate kinase and N-acetyl-γ-glutamyl phosphate reductase, we demonstrate this phosphate (Pi)-based route in vitro and in vivo. We further engineer a formyl phosphate reductase variant with improved formyl phosphate conversion in vivo by suppressing cross-talk with native metabolism and interface the Pi route with a recently developed formaldehyde assimilation pathway to enable C2 compound formation from formate as the sole carbon source in Escherichia coli. The Pi route therefore offers a potent tool in expanding the landscape of synthetic formate assimilation.

Suggested Citation

  • Maren Nattermann & Sebastian Wenk & Pascal Pfister & Hai He & Seung Hwan Lee & Witold Szymanski & Nils Guntermann & Fayin Zhu & Lennart Nickel & Charlotte Wallner & Jan Zarzycki & Nicole Paczia & Nina, 2023. "Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38072-w
    DOI: 10.1038/s41467-023-38072-w
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    References listed on IDEAS

    as
    1. Elad Noor & Hulda S Haraldsdóttir & Ron Milo & Ronan M T Fleming, 2013. "Consistent Estimation of Gibbs Energy Using Component Contributions," PLOS Computational Biology, Public Library of Science, vol. 9(7), pages 1-11, July.
    2. Philipp Keller & Michael A. Reiter & Patrick Kiefer & Thomas Gassler & Lucas Hemmerle & Philipp Christen & Elad Noor & Julia A. Vorholt, 2022. "Generation of an Escherichia coli strain growing on methanol via the ribulose monophosphate cycle," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
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