A Nonconventional Archaeal Fluorinase Identified by in Silico Mining for Enhanced Fluorine Biocatalysis

Isabel Pardo, David Bednar, Patricia Calero, Daniel C. Volke, Jiří Damborský, Pablo I. Nikel*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

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Abstract

Fluorinases, the only enzymes known to catalyze the transfer of fluorine to an organic molecule, are essential catalysts for the biological synthesis of valuable organofluorines. However, the few fluorinases identified so far have low turnover rates that hamper biotechnological applications. Here, we isolated and characterized putative fluorinases retrieved from systematic in silico mining and identified a nonconventional archaeal enzyme from Methanosaeta sp. that mediates the fastest SN2 fluorination rate reported to date. Furthermore, we demonstrate enhanced production of fluoronucleotides in vivo in a bacterial host engineered with this archaeal fluorinase, paving the way toward synthetic metabolism for efficient biohalogenation.

Original languageEnglish
JournalACS Catalysis
Volume12
Issue number11
Pages (from-to)6570-6577
Number of pages8
ISSN2155-5435
DOIs
Publication statusPublished - 2022

Keywords

  • Biocatalysis
  • Fluorinase
  • Fluorine
  • Metabolic engineering
  • Organofluorine
  • Synthetic biology
  • Synthetic metabolism

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