Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme

Angew Chem Int Ed Engl. 2021 May 10;60(20):11423-11429. doi: 10.1002/anie.202100969. Epub 2021 Apr 8.

Abstract

The polyketide synthase (PKS)-like protein TerB, consisting of inactive dehydratase, inactive C-methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6-hydroxymellein, a key pathway intermediate during the biosynthesis of various fungal natural products. The catalytically inactive dehydratase domain of TerB appears to mediate productive interactions with TerA, demonstrating a new mode of trans-interaction between iterative PKS components.

Keywords: iterative polyketide synthase; ketoreductase; mellein; terrein; trans-acting domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldo-Keto Reductases / chemistry
  • Aldo-Keto Reductases / metabolism*
  • Hydro-Lyases / chemistry
  • Hydro-Lyases / metabolism*
  • Isocoumarins / chemistry
  • Isocoumarins / metabolism*
  • Methyltransferases / chemistry
  • Methyltransferases / metabolism*
  • Molecular Structure

Substances

  • Isocoumarins
  • 6-hydroxymellein
  • Aldo-Keto Reductases
  • Methyltransferases
  • Hydro-Lyases