Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway

Org Lett. 2014 Oct 17;16(20):5382-5. doi: 10.1021/ol502596z. Epub 2014 Oct 2.

Abstract

Ergothioneine is a histidine thiol derivative. Its mycobacterial biosynthetic pathway has five steps (EgtA-E catalysis) with two novel reactions: a mononuclear nonheme iron enzyme (EgtB) catalyzed oxidative C-S bond formation and a PLP-mediated C-S lyase (EgtE) reaction. Our bioinformatic and biochemical analyses indicate that the fungus Neurospora crassa has a more concise ergothioneine biosynthetic pathway because its nonheme iron enzyme, Egt1, makes use of cysteine instead of γ-Glu-Cys as the substrate. Such a change of substrate preference eliminates the competition between ergothioneine and glutathione biosyntheses. In addition, we have identified the N. crassa C-S lyase (NCU11365) and reconstituted its activity in vitro, which makes the future ergothioneine production through metabolic engineering feasible.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biosynthetic Pathways
  • Catalysis
  • Dipeptides / metabolism
  • Ergothioneine / biosynthesis*
  • Ergothioneine / chemistry
  • Ergothioneine / metabolism*
  • Histidine / analogs & derivatives
  • Histidine / metabolism
  • Molecular Structure
  • Neurospora crassa / chemistry
  • Neurospora crassa / enzymology*
  • Neurospora crassa / metabolism
  • Oxidation-Reduction

Substances

  • Dipeptides
  • Histidine
  • Ergothioneine
  • gamma-glutamylcysteine