Recent developments on the fluorinase from Streptomyces cattleya

This is a summary of a lecture presented at the 100th Anniversary, Moissan Symposium in Paris on Friday, 10 November 2006. The lecture highlighted recent developments on the enzyme structure, mechanism and biotransformation prospects of the fluorinase enzyme identified in 2002 from the bacterium Streptomyces cattleya. Over-expression of the enzyme has allowed it to be used as a catalyst for 18F-incorporation during the synthesis of potential ligands for positron emission tomography (PET) applications.

Graphical abstractThe fluorinase from Streptomyces cattleya was isolated in 2002. This enzyme is unusual in that it can catalyse the formation of a C–F bond from inorganic fluoride. The fluorinase has been purified, cloned and over-expressed and it has been the subject of structural and mechanistic studies. The fluorinase has been used as an catalyst for the incorporation of 18F into ribose. This review summarises recent progress on the chemistry and biochemistry of this enzyme. Figure optionsDownload full-size imageDownload as PowerPoint slide