Fluorinases represent the only known biological catalysts capable of forming carbon-fluorine bonds, but their slow catalytic rate limits their broader application. In this study, two fluorinases, FlA and FlA, were identified from a pool of 12 718 nonredundant proteins using a genome-mining approach, with FlA showing high catalytic activity. Both newly identified fluorinases contain a Phe50 residue in place of the Trp50 typically found in fluorinases. Structural and mutagenesis studies revealed that the Trp50 or Phe50 residue at this position is crucial for fluorinase activity. This work highlights the utility of genomic enzymology in expanding the repertoire of biocatalysts for fluorination chemistry.
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