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-(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.
Cadicamo
Cosimo D
CD
School of Chemistry and Centre for Biomolecular Sciences, University of St Andrews, St Andrews, Fife, KY16 9ST, UK.
Courtieu
Jacques
J
Deng
Hai
H
Meddour
Abdelkrim
A
O'Hagan
David
D
D002384:Catalysis; D005459:Fluorides / Q000737:chemistry*; D008716:Methionine Adenosyltransferase / Q000737:chemistry*; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D012436:S-Adenosylmethionine / Q000138:chemical synthesis / Q000737:chemistry*; D013237:Stereoisomerism; D013302:Streptomyces / Q000201:enzymology* / Q000378:metabolism
D012436:S-Adenosylmethionine; D008716:Methionine Adenosyltransferase; D005459:Fluorides