Abstract
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.
Original language | English |
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Pages (from-to) | 685-690 |
Number of pages | 6 |
Journal | ChemBioChem |
Volume | 5 |
Issue number | 5 |
Early online date | 28 Apr 2004 |
DOIs | |
Publication status | Published - 3 May 2004 |
Keywords
- bioorganic chemistry
- fluorine
- NMR spectroscopy
- stereochemistry