A Nonconventional Archaeal Fluorinase Identified by In SilicoMining for Enhanced Fluorine Biocatalysis br

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Authors

PARDO Isabel BEDNÁŘ David CALERO Patricia VOLKE Daniel C DAMBORSKÝ Jiří NIKEL Pablo I.

Year of publication 2022
Type Article in Periodical
Magazine / Source ACS Catalysis
MU Faculty or unit

Faculty of Science

Citation
Web https://pubs.acs.org/doi/10.1021/acscatal.2c01184
Doi http://dx.doi.org/10.1021/acscatal.2c01184
Keywords fluorinase; fluorine; organofluorine; synthetic biology; biocatalysis; metabolic engineering; synthetic metabolism
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Description Fluorinases, the only enzymes known to catalyze thetransfer offluorine to an organic molecule, are essential catalysts forthe biological synthesis of valuable organofluorines. However, the fewfluorinases identified so far have low turnover rates that hamperbiotechnological applications. Here, we isolated and characterizedputativefluorinases retrieved from systematic in silico mining andidentified a nonconventional archaeal enzyme fromMethanosaetasp.that mediates the fastest SN2fluorination rate reported to date.Furthermore, we demonstrate enhanced production offluoronucleo-tides in vivo in a bacterial host engineered with this archaealfluorinase, paving the way toward synthetic metabolism for efficientbiohalogenation.
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