Discovery and characterization of new O-methyltransferase from the genome of the lignin-degrading fungus Phanerochaete chrysosporium for enhanced lignin degradation

Enzyme Microb Technol. 2016 Jan:82:66-73. doi: 10.1016/j.enzmictec.2015.08.016. Epub 2015 Aug 28.

Abstract

Using bioinformatic homology search tools, this study utilized sequence phylogeny, gene organization and conserved motifs to identify members of the family of O-methyltransferases from lignin-degrading fungus Phanerochaete chrysosporium. The heterologous expression and characterization of O-methyltransferases from P. chrysosporium were studied. The expressed protein utilized S-(5'-adenosyl)-L-methionine p-toluenesulfonate salt (SAM) and methylated various free-hydroxyl phenolic compounds at both meta and para site. In the same motif, O-methyltransferases were also identified in other white-rot fungi including Bjerkandera adusta, Ceriporiopsis (Gelatoporia) subvermispora B, and Trametes versicolor. As free-hydroxyl phenolic compounds have been known as inhibitors for lignin peroxidase, the presence of O-methyltransferases in white-rot fungi suggested their biological functions in accelerating lignin degradation in white-rot basidiomycetes by converting those inhibitory groups into non-toxic methylated phenolic ones.

Keywords: Free-phenolic compounds; Lignin peroxidase; O-Methyltransferase; White-rot fungi.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biodegradation, Environmental
  • Cloning, Molecular
  • Coriolaceae / enzymology
  • DNA, Fungal / genetics
  • Escherichia coli
  • Fungal Proteins / genetics
  • Fungal Proteins / isolation & purification*
  • Fungal Proteins / metabolism
  • Genes, Fungal
  • Lignin / metabolism*
  • Methylation
  • Methyltransferases / genetics
  • Methyltransferases / isolation & purification*
  • Methyltransferases / metabolism
  • Models, Molecular
  • Phanerochaete / enzymology*
  • Phanerochaete / genetics
  • Phenols / metabolism
  • Protein Conformation
  • Recombinant Fusion Proteins / metabolism
  • S-Adenosylmethionine / metabolism
  • Species Specificity
  • Substrate Specificity

Substances

  • DNA, Fungal
  • Fungal Proteins
  • Phenols
  • Recombinant Fusion Proteins
  • S-Adenosylmethionine
  • Lignin
  • Methyltransferases