Cytochrome P450 as dimerization catalyst in diketopiperazine alkaloid biosynthesis

Chembiochem. 2014 Mar 21;15(5):656-9. doi: 10.1002/cbic.201300751.

Abstract

As dimeric natural products frequently exhibit useful biological activities, identifying and understanding their mechanisms of dimerization is of great interest. One such compound is (−)-ditryptophenaline, isolated from Aspergillus flavus, which inhibits substance P receptor for potential analgesic and anti-inflammatory activity. Through targeted gene knockout in A. flavus and heterologous yeast gene expression, we determined for the first time the gene cluster and pathway for the biosynthesis of a dimeric diketopiperazine alkaloid. We also determined that a single cytochrome P450, DtpC, is responsible not only for pyrroloindole ring formation but also for concurrent dimerization of N-methylphenylalanyltryptophanyl diketopiperazine monomers into a homodimeric product. Furthermore, DtpC exhibits relaxed substrate specificity, allowing the formation of two new dimeric compounds from a non-native monomeric precursor, brevianamide F. A radical-mediated mechanism of dimerization is proposed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaloids / chemistry
  • Alkaloids / genetics
  • Alkaloids / metabolism*
  • Aspergillus flavus / chemistry
  • Aspergillus flavus / genetics
  • Aspergillus flavus / metabolism*
  • Biological Products / chemistry
  • Biological Products / metabolism
  • Biosynthetic Pathways
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / metabolism*
  • Diketopiperazines / chemistry
  • Diketopiperazines / metabolism*
  • Dimerization
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Multigene Family

Substances

  • Alkaloids
  • Biological Products
  • Diketopiperazines
  • Fungal Proteins
  • Cytochrome P-450 Enzyme System