{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Olson NM"],"funding":["NCI NIH HHS","NIGMS NIH HHS"],"pagination":["110014"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10187777"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["261-262"],"pubmed_abstract":["Current experiments that rely on biosynthetic metabolic protein labeling with <sup>19</sup>F often require fluorinated amino acids, which in the case of 2- and 3-fluorotyrosine can be expensive. However, using these amino acids has provided valuable insight into protein dynamics, structure, and function. Here, we develop a new in-cell method for fluorinated tyrosine generation from readily available substituted phenols and subsequent metabolic labeling of proteins in a single bacterial expression culture. This approach uses a dual-gene plasmid encoding for a model protein BRD4(D1) and a tyrosine phenol lyase from <i>Citrobacter freundii</i>, which catalyzes the formation of tyrosine from phenol, pyruvate, and ammonium. Our system demonstrated both enzymatic fluorotyrosine production and ex"],"journal":["Journal of fluorine chemistry"],"pubmed_title":["Development of a single culture <i>E. coli</i> expression system for the enzymatic synthesis of fluorinated tyrosine and its incorporation into proteins."],"pmcid":["PMC10187777"],"funding_grant_id":["P30 CA077598","T32 GM008347","R35 GM140837"],"pubmed_authors":["Smanski MJ","Olson NM","Peterson KE","Pomerantz WCK","Johnson JA","Heinsch SC","Marshall AP","Carlson EE"],"additional_accession":[]},"is_claimable":false,"name":"Development of a single culture <i>E. coli</i> expression system for the enzymatic synthesis of fluorinated tyrosine and its incorporation into proteins.","description":"Current experiments that rely on biosynthetic metabolic protein labeling with <sup>19</sup>F often require fluorinated amino acids, which in the case of 2- and 3-fluorotyrosine can be expensive. However, using these amino acids has provided valuable insight into protein dynamics, structure, and function. Here, we develop a new in-cell method for fluorinated tyrosine generation from readily available substituted phenols and subsequent metabolic labeling of proteins in a single bacterial expression culture. This approach uses a dual-gene plasmid encoding for a model protein BRD4(D1) and a tyrosine phenol lyase from <i>Citrobacter freundii</i>, which catalyzes the formation of tyrosine from phenol, pyruvate, and ammonium. Our system demonstrated both enzymatic fluorotyrosine production and ex","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-05-28T22:57:53.583Z","creation":"2024-10-16T17:02:42.015Z"},"accession":"S-EPMC10187777","cross_references":{"pubmed":["37197608"],"doi":["10.1016/j.jfluchem.2022.110014"]}}