{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kraußer F"],"funding":["Bundesministerium f?r Bildung und Forschung","Deutsche Forschungsgemeinschaft"],"pagination":["1250-1263"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12012885"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(4)"],"pubmed_abstract":["Adenosine triphosphate (ATP)-dependent <i>in vitro</i> bioprocesses, such as cell-free protein synthesis and the production of phosphorylated fine chemicals, are of considerable industrial significance. However, their implementation is mainly hindered by the high cost of ATP. We propose and demonstrate the feasibility of a cell-free ATP regeneration system based on the <i>in situ</i> generation of the high-energy compound acetyl phosphate from low-cost d-fructose and inorganic phosphate substrates. The enzyme cascade chains d-fructose phosphoketolase, d-erythrose isomerase, d-erythrulose phosphoketolase, and glycolaldehyde phosphoketolase activities theoretically enabling production of 3 mol ATP per mol of d-fructose. Through a semirational engineering approach and the screening of nine si"],"journal":["ACS synthetic biology"],"pubmed_title":["Cell-Free Reaction System for ATP Regeneration from d-Fructose."],"pmcid":["PMC12012885"],"funding_grant_id":["031B1245A","450319558"],"pubmed_authors":["Voland J","Liese A","Walther T","Kundoch JO","Ohde D","Topham CM","Kraußer F","Lilienthal L","Rabe K"],"additional_accession":[]},"is_claimable":false,"name":"Cell-Free Reaction System for ATP Regeneration from d-Fructose.","description":"Adenosine triphosphate (ATP)-dependent <i>in vitro</i> bioprocesses, such as cell-free protein synthesis and the production of phosphorylated fine chemicals, are of considerable industrial significance. However, their implementation is mainly hindered by the high cost of ATP. We propose and demonstrate the feasibility of a cell-free ATP regeneration system based on the <i>in situ</i> generation of the high-energy compound acetyl phosphate from low-cost d-fructose and inorganic phosphate substrates. The enzyme cascade chains d-fructose phosphoketolase, d-erythrose isomerase, d-erythrulose phosphoketolase, and glycolaldehyde phosphoketolase activities theoretically enabling production of 3 mol ATP per mol of d-fructose. Through a semirational engineering approach and the screening of nine si","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-06-01T21:07:49.491Z","creation":"2025-07-03T03:05:13.342Z"},"accession":"S-EPMC12012885","cross_references":{"pubmed":["40143462"],"doi":["10.1021/acssynbio.4c00877"]}}