MassIVE MSV000091532

Partial Public PXD041037

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

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Description

To realize a carbon-neutral bioeconomy, the concept of electrobiocatalysis has been developed, in which CO2 is first chemically reduced to formate and subsequently assimilated by enzymatic cascades or engineered microbes. A key step in the assimilation of formate is its reduction into formaldehyde, which is chemically challenging. Here, we developed a two-enzyme route in which formate is activated into formyl phosphate and reduced by NAD(P)H into formaldehyde. Exploiting the promiscuity of acetate kinase and N-acetyl--glutamyl phosphate reductase, we demonstrate the phosphate (Pi) route in vitro and in vivo. We further engineered a formyl phosphate reductase variant with improved formyl phosphate conversion in vivo by suppressing cross-talk with native metabolism. We further show that the Pi route can be interfaced with a recently developed formaldehyde assimilation pathway (FORCE pathway) to provide a thermodynamically and kinetically highly efficient route from formate into C2-compounds. [doi:10.25345/C5FX7477P] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: lc-msms, Escherichia, formaldehyde, formate

Contact

Principal Investigators:
(in alphabetical order) 		Tobias Erb, Max Planck Institute for Terrestrial Microbiology, Germany
Submitting User: Wszymanski

Publications

Nattermann M, Wenk S, Pfister P, He H, Lee SH, Szymanski W, Guntermann N, Zhu F, Nickel L, Wallner C, Zarzycki J, Paczia N, Gaißert N, Franciò G, Leitner W, Gonzalez R, Erb TJ.
Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo.
Nat Commun. 2023 May 9;14(1):2682. Epub 2023 May 9.

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