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

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 Gaißert, Giancarlo Franciò, Walter Leitner, Ramon Gonzalez and Tobias J. Erb ()
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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
Ramon Gonzalez: University of South Florida
Tobias J. Erb: Max Planck Institute for Terrestrial Microbiology

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-38072-w

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