Molecular characterization of lignin peroxidase from the white-rot basidiomycete Trametes cervina: a novel fungal peroxidase

FEMS Microbiol Lett. 2010 Mar;304(1):39-46. doi: 10.1111/j.1574-6968.2009.01880.x. Epub 2009 Dec 17.

Abstract

The lignin peroxidase (LiP) from Trametes cervina was cloned, characterized, and identified as a novel fungal peroxidase. The sequence of T. cervina LiP encodes the essential amino acids for shaping the heme cavity and calcium-binding sites, which are conserved in plant and fungal peroxidases. However, a sequence homology analysis showed that T. cervina LiP has two unique features: it lacks the conserved tryptophan residue corresponding to the substrate-oxidation site (Trp171) of Phanerochaete chrysosporium LiP and it has a tyrosine residue (Tyr181) that has never been reported in other lignin peroxidases. A tertiary model of T. cervina LiP showed that Tyr181 sterically adjacent to the 6-propionate group of heme is surrounded by acidic amino acids and is exposed to the exterior. These attributes indicate that Tyr181 could be a T. cervina LiP substrate-oxidation site. A phylogenetic analysis showed that T. cervina LiP does not cluster with any other fungal peroxidases, suggesting that it is a unique molecule that is evolutionarily distant from other peroxidases. Thus, we concluded that T. cervina LiP could be a novel secreted peroxidase, among those produced by fungi, with a new oxidation mechanism probably involving Tyr181.

MeSH terms

  • Amino Acid Sequence
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Peroxidases / chemistry
  • Peroxidases / genetics*
  • Peroxidases / metabolism
  • Sequence Analysis, DNA
  • Trametes / classification
  • Trametes / enzymology*
  • Trametes / genetics
  • Tryptophan / chemistry
  • Tyrosine / chemistry

Substances

  • Fungal Proteins
  • Tyrosine
  • Tryptophan
  • Peroxidases
  • lignin peroxidase