{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Nattermann M"],"pubmed_abstract":["Formate can be envisioned at the core of a carbon-neutral bioeconomy, where it is produced from CO<sub>2</sub> 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 (P<sub>i</sub>)-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 an"],"journal":["Nature communications"],"pagination":["2682"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10170137"],"repository":["biostudies-literature"],"pubmed_title":["Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo."],"pmcid":["PMC10170137"],"pubmed_authors":["Guntermann N","Francio G","Wenk S","He H","Lee SH","Zhu F","Pfister P","Wallner C","Leitner W","Gaißert N","Gonzalez R","Erb TJ","Szymanski W","Nattermann M","Nickel L","Zarzycki J","Paczia N"],"additional_accession":[]},"is_claimable":false,"name":"Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo.","description":"Formate can be envisioned at the core of a carbon-neutral bioeconomy, where it is produced from CO<sub>2</sub> 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 (P<sub>i</sub>)-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 an","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2026-05-28T08:21:38.734Z","creation":"2025-04-05T21:08:29.275Z"},"accession":"S-EPMC10170137","cross_references":{"pubmed":["37160875"],"doi":["10.1038/s41467-023-38072-w"]}}