The Aspergillus nidulans enzyme TdiB catalyzes prenyltransfer to the precursor of bioactive asterriquinones

Fungal Genet Biol. 2008 Mar;45(3):302-9. doi: 10.1016/j.fgb.2007.09.004. Epub 2007 Sep 25.

Abstract

The asterriquinones represent a class of ascomycete metabolic products whose significance stems from remarkable and useful pharmacological activities, among those antiretroviral (e.g., against the HI-virus), antitumor, and antidiabetes properties. Recently, the first genetic locus for an asterriquinone, the clustered terrequinone genes tdiA-E, was identified during a genome-wide screen in Aspergillus nidulans for "orphan" natural product biosynthesis loci. Here, we describe overexpression and characterization of TdiB, which catalyzes the reverse prenylation event during terrequinone A biosynthesis, which is the transfer of dimethylallyl diphosphate to carbon atom 2' of the intermediate didemethylasterriquinone D, to yield asterriquinone C-1. TdiB does not depend on the presence of divalent metal cations for catalysis and lacks the canonical prenyl diphosphate binding motif (D/N)DXXD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus nidulans / enzymology
  • Aspergillus nidulans / genetics
  • Aspergillus nidulans / metabolism*
  • Catalysis
  • Chromatography, High Pressure Liquid
  • Chromatography, Liquid
  • Dimethylallyltranstransferase / genetics
  • Dimethylallyltranstransferase / metabolism*
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Genetic Complementation Test
  • Indoles / chemistry
  • Indoles / metabolism
  • Kinetics
  • Mass Spectrometry
  • Molecular Structure
  • Mutation
  • Sequence Analysis, DNA

Substances

  • Fungal Proteins
  • Indoles
  • terrequinone A
  • asterriquinone
  • Dimethylallyltranstransferase