Schaffrath Christoph, Deng Hai, O'Hagan David
School of Chemistry and Centre for Biomolecular Sciences, University of St Andrews, North Haugh, KY16 9ST, St Andrews, UK.
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.
