Tweezing the cofactor preference of gymnosperm pinene synthase

Biosci Biotechnol Biochem. 2018 Jun;82(6):1058-1061. doi: 10.1080/09168451.2018.1459465.

Abstract

The cellular activities of gymnosperms monoterpene synthases are largely compromised due to their requirement for manganese, which is deficient in microbial cells. Through site-saturation mutagenesis of the residue adjacent to metal-binding glutamate, we found that pinene synthase is highly mutable at this position yet drastically alter their metal binding preference, thereby quickly improving the cellular performance in heterologous hosts.

Keywords: Metal dependency; metabolic engineering; protein engineering; synthetic biology.

MeSH terms

  • Chlorides / chemistry
  • Intramolecular Lyases / genetics
  • Intramolecular Lyases / metabolism*
  • Manganese Compounds / chemistry
  • Mutagenesis
  • Protein Engineering

Substances

  • Chlorides
  • Manganese Compounds
  • Intramolecular Lyases
  • pinene cyclase I
  • manganese chloride