The stereochemical course of the recently isolated fluorination enzyme from Streptomyces cattleya has been evaluated. The enzyme mediates a reaction between the fluoride ion and S- adenosyl-L-methionine (SAM) to generate 5'-fluoro-5'-deoxyadenosine (5'-FDA). Preparation of (5'R)-[5-(2)H(1)]-ATP generated (5'R)-[5-(2)H(1)]-5'-FDA in a coupled enzyme assay involving SAM synthase and the fluorinase. The stereochemical analysis of the product relied on (2)H NMR analysis in a chiral liquid-crystalline medium. It is concluded that the enzyme catalyses the fluorination with an inversion of configuration consistent with an S(N)2 reaction mechanism.
- bioorganic chemistry
- NMR spectroscopy
Cadicamo, C. D., Courtieu, J., Deng, H., Meddour, A., & O'Hagan, D. (2004). Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an SN2 reaction mechanism. ChemBioChem, 5(5), 685-690. https://doi.org/10.1002/cbic.200300839