Enzymatic Fluorination in Streptomyces cattleya Takes Place with an Inversion of Configuration Consistent with an S N 2 Reaction Mechanism

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...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2004-05, Vol.5 (5), p.685-690
Main Authors: Cadicamo, Cosimo D., Courtieu, Jacques, Deng, Hai, Meddour, Abdelkrim, O'Hagan, David
Format: Article
Language:English
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Summary: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.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200300839