A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates

FEBS Lett. 2007 Jun 26;581(16):2889-93. doi: 10.1016/j.febslet.2007.05.031. Epub 2007 May 22.


Fnq26 from Streptomyces cinnamonensis DSM 1042 is a new member of the recently identified CloQ/Orf2 class of prenyltransferases. The enzyme was overexpressed in E. coli and purified to apparent homogeneity, resulting in a soluble, monomeric protein of 33.2 kDa. The catalytic activity of Fnq26 is independent of the presence of Mg(2+) or other divalent metal ions. With flaviolin (2,5,7-trihydroxy-1,4-naphthoquinone) as substrate, Fnq26 catalyzes the formation of a carbon-carbon-bond between C-3 (rather than C-1) of geranyl diphosphate and C-3 of flaviolin, i.e. an unusual "reverse" prenylation. With 1,3-dihydroxynaphthalene and 4-hydroxybenzoate as substrates Fnq26 catalyzes O-prenylations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids, Aromatic / metabolism*
  • Catalysis
  • Dimethylallyltranstransferase / genetics
  • Dimethylallyltranstransferase / isolation & purification
  • Dimethylallyltranstransferase / metabolism*
  • Escherichia coli / genetics
  • Magnesium / pharmacology*
  • Models, Biological
  • Protein Prenylation* / drug effects
  • Sequence Analysis, Protein
  • Solubility
  • Streptomyces / enzymology*
  • Substrate Specificity
  • Transformation, Bacterial


  • Amino Acids, Aromatic
  • Dimethylallyltranstransferase
  • Magnesium