Enzymatic Fluorination in Streptomyces cattleya Takes Place with an Inversion of Configuration Consistent with an SN2 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)-[5-²H₁]-ATP generate...

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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
Subjects:
bioorganic chemistry
Catalysis
Fluorides - chemistry
fluorine
Methionine Adenosyltransferase - chemistry
Molecular Structure
NMR spectroscopy
Nucleic Acid Conformation
S-Adenosylmethionine - chemical synthesis
S-Adenosylmethionine - chemistry
stereochemistry
Stereoisomerism
Streptomyces - enzymology
Streptomyces - metabolism
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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)-[5-²H₁]-ATP generated (5′R)-[5-²H₁]-5′-FDA in a coupled enzyme assay involving SAM synthase and the fluorinase. The stereochemical analysis of the product relied on ²H 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 SN2 reaction mechanism.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200300839