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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 C222 1, with unit-cell parameters a = 75.9, b = 130.3, c = 183.4 Å, α = β = γ = 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.

Original publication

DOI

10.1107/S0907444903019826

Type

Journal article

Journal

Acta Crystallographica - Section D Biological Crystallography

Publication Date

01/12/2003

Volume

59

Pages

2292 - 2293