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Enzymatic Fluorination in Streptomyces cattleya Takes Place with an Inversion of Configuration Consistent with an S N 2 Reaction Mechanism
Author(s) -
Cadicamo Cosimo D.,
Courtieu Jacques,
Deng Hai,
Meddour Abdelkrim,
O'Hagan David
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200300839
Subject(s) - mechanism (biology) , streptomyces , enzyme , inversion (geology) , chemistry , stereochemistry , combinatorial chemistry , computational chemistry , biochemistry , biology , physics , bacteria , genetics , paleontology , quantum mechanics , structural basin
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.