The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases

FEMS Microbiol Lett. 2000 Oct 1;191(1):37-43. doi: 10.1111/j.1574-6968.2000.tb09316.x.

Abstract

We report cloning and sequencing of gene ps1 encoding a versatile peroxidase combining catalytic properties of lignin peroxidase (LiP) and manganese peroxidase (MnP) isolated from lignocellulose cultures of the white-rot fungus Pleurotus eryngii. The gene contains 15 putative introns, and the deduced amino acid sequence consists of a 339-residue mature protein with a 31-residue signal peptide. Several putative response elements were identified in the promoter region. Amino acid residues involved in oxidation of Mn(2+) and aromatic substrates by direct electron transfer to heme and long-range electron transfer from superficial residues as predicted by analogy with Phanerochaete chrysosporium MnP and LiP, respectively. A dendrogram is presented illustrating sequence relationships between 29 fungal peroxidases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cellulose / metabolism*
  • Cloning, Molecular*
  • Culture Media
  • Fungi / enzymology
  • Fungi / genetics
  • Genes, Fungal
  • Lignin / metabolism*
  • Molecular Sequence Data
  • Peroxidase / chemistry
  • Peroxidase / genetics
  • Peroxidase / metabolism*
  • Pleurotus / enzymology*
  • Pleurotus / genetics
  • Pleurotus / growth & development
  • Sequence Alignment
  • Sequence Analysis, DNA

Substances

  • Culture Media
  • lignocellulose
  • Cellulose
  • Lignin
  • Peroxidase

Associated data

  • GENBANK/AF175710