A Nonconventional Archaeal Fluorinase Identified by In SilicoMining for Enhanced Fluorine Biocatalysis br
| Authors | |
|---|---|
| Year of publication | 2022 |
| Type | Article in Periodical |
| Magazine / Source | ACS Catalysis |
| MU Faculty or unit | |
| 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 |
| Attached files | |
| 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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