Docking domain-mediated subunit interactions in natural product megasynth(et)ases

J Ind Microbiol Biotechnol. 2021 Jun 4;48(3-4):kuab018. doi: 10.1093/jimb/kuab018.

Abstract

Polyketide synthase (PKS) and non-ribosomal peptide synthetase (NRPS) multienzymes produce numerous high value metabolites. The protein subunits which constitute these megasynth(et)ases must undergo ordered self-assembly to ensure correct organisation of catalytic domains for the biosynthesis of a given natural product. Short amino acid regions at the N- and C-termini of each subunit, termed docking domains (DDs), often occur in complementary pairs, which interact to facilitate substrate transfer and maintain pathway fidelity. This review details all structurally characterised examples of NRPS and PKS DDs to date and summarises efforts to utilise DDs for the engineering of biosynthetic pathways.

Keywords: Biosynthesis; Non-ribosomal peptide synthetase; Polyketide synthase.

Publication types

  • Review

MeSH terms

  • Biological Products / chemistry*
  • Biological Products / metabolism
  • Humans
  • Peptide Synthases / chemistry*
  • Peptide Synthases / metabolism
  • Polyketide Synthases / chemistry*
  • Polyketide Synthases / metabolism

Substances

  • Biological Products
  • Polyketide Synthases
  • Peptide Synthases
  • non-ribosomal peptide synthase