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

C Schaffrath, H Deng, David O'Hagan

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58 Citations (Scopus)

Abstract

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'-deoxy-adenosine. 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 muM) whereas sinefungin was only weakly inhibitory. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)111-114
Number of pages4
JournalFEBS Letters
Volume547
Issue number1-3
DOIs
Publication statusPublished - 17 Jul 2003

Keywords

  • 5 '-fluorodeoxyadenosine synthase
  • S-adenosyl-L-methionine
  • fluoride ion
  • S-adenosyl-L-homocysteine
  • Streptomyces cattleya
  • NATURAL-PRODUCTS
  • BIOSYNTHESIS
  • 4-FLUOROTHREONINE
  • FLUOROACETATE
  • ACID

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