Isolation and characterisation of 5'-fluorodeoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya

FEBS Lett. 2003 Jul 17;547(1-3):111-4. doi: 10.1016/s0014-5793(03)00688-4.


5'-fluorodeoxyadenosine synthase, a C-F bond-forming enzyme, has been purified from Streptomyces cattleya. The enzyme mediates a reaction between inorganic fluoride and S-adenosyl-L-methionine (SAM) to generate 5'-fluoro-5'-deoxyadenosine. The molecular weight of the monomeric protein is shown to be 32.2 kDa by electrospray mass spectrometry. The kinetic parameters for SAM (K(m) 0.42 mM, V(max) 1.28 U/mg) and fluoride ion (K(m) 8.56 mM, V(max) 1.59 U/mg) have been evaluated. Both S-adenosyl-L-homocysteine (SAH) and sinefungin were explored as inhibitors of the enzyme. SAH emerged as a potent competitive inhibitor (K(i) 29 microM) whereas sinefungin was only weakly inhibitory.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biotransformation
  • Kinetics
  • Molecular Sequence Data
  • Pentosyltransferases / chemistry
  • Pentosyltransferases / isolation & purification
  • Pentosyltransferases / metabolism*
  • Peptide Fragments / chemistry
  • S-Adenosylmethionine / metabolism
  • S-Adenosylmethionine / pharmacokinetics
  • Spectrometry, Mass, Electrospray Ionization
  • Streptomyces / enzymology*


  • Peptide Fragments
  • S-Adenosylmethionine
  • 5'-fluorodeoxyadenosine synthase
  • Pentosyltransferases