Abstract
The fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C–F bond. We now report that the enzyme will accept 2′-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C–F bond formation.
Original language | English |
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Pages (from-to) | 1458-1460 |
Number of pages | 3 |
Journal | Organic & Biomolecular Chemistry |
Issue number | 8 |
DOIs | |
Publication status | Published - 2006 |