Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an SN2 reaction mechanism

Cosimo Damiano Cadicamo, J Courtieu, H Deng, A Meddour, David O'Hagan

Research output: Contribution to journalArticlepeer-review

58 Citations (Scopus)

Abstract

The stereochemical course of the recently isolated fluorination enzyme from Streptomyces cattleya has been evaluated. The enzyme mediates a reaction between fluoride ion and S-adenosyl-L-methionine (SAM) to generate 5'-fluoro-5'-deoxy-adenosine (5'-FDA). Preparation of (5'R)-[5-H-2(1)]-ATP generated (5'-R)-[5-H-2(1)]-5'-FDA in a coupled enzyme assay involving SAM synthase and the fluorinase. The stereochemical analysis of the product relied on H-2 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 languageEnglish
Pages (from-to)685-690
Number of pages6
JournalChemBioChem
Volume5
Issue number5
DOIs
Publication statusPublished - 3 May 2004

Keywords

  • bioorganic chemistry
  • fluorine
  • NMR spectroscopy
  • stereochemistry
  • LIQUID-CRYSTALLINE SOLVENT
  • ENANTIOMERIC ANALYSIS
  • BOND FORMATION
  • BAKERS-YEAST
  • BIOSYNTHESIS
  • 4-FLUOROTHREONINE
  • FLUOROACETATE
  • METHIONINE
  • ADENOSINE
  • ACID

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