Organofluorine compounds are widely prepared throughout the chemicals industry, but their prepararion generally requires harsh fluorinating reagents and non-aqueous solvents. On the other hand, biology has hardly exploited organofluorine compounds. A very few organisms synthesize organofluorine metabolites, suggesting they have evolved a mechanism to overcome the kinetic desolvation barrier to utilizing F-(aq). Here, the purification and crystallization of an enzyme from Streptomyces cattleya which is responsible for the synthesis of the C-F bond during fluoroacetate and 4-fluorothreonine biosynthesis is reported. The protein crystallizes in space group C2221, with unit-cell parameters a = 75.9, b = 130.3, c = 183.4 Å, [alpha] = [beta] = [gamma] = 90°. Data were recorded to 1.9 Å at the ESRF. The structure of the protein should provide important insights into the biochemical process of C-F bond formation.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - 2003|
- 5'-fluoro-5'-deoxyadenosine synthase
- Organofluorine compounds
Dong, C., Deng, H., Dorward, M., Schaffrath, C., O’Hagan, D., & Naismith, J. H. (2003). Crystallization and X-ray diffraction of 5'-fluoro-5'-deoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya. Acta Crystallographica Section D: Biological Crystallography, 59(12), 2292-2293. https://doi.org/10.1107/S0907444903019826