Characterization of a laccase gene from the white-rot fungus Trametes versicolor and structural features of basidiomycete laccases

Research output: Contribution to journalArticle

Abstract

A gene coding for the multi-copper phenol oxidase laccase has been isolated from the white-rot basidiomycete Trametes oersicolor. The gene, which is preceded by a TATA box and a pyrimidine-rich region, is predicted to contain ten introns. The mature translation product, preceded by a 22-residue signal peptide, should consist of 498 residues. Comparisons with Edman degradation data of peptides from T. versicolor laccase strongly suggest that two disulfide bridges are formed by Cys-85/Cys-487 and Cys-117/Cys-205, respectively. The encoded protein contains five Cys, and the sequence surrounding the remaining Cys-452 is consistent with its involvement in the ligation of type-1 copper. Alignment of sequences indicates that T. versicolor laccase displays a Phe at the position corresponding to a residue (Met in ascorbate oxidase and azurin) considered important for the reduction potential of type-1 copper proteins.

Details

Authors
  • Leif Jönsson
  • Kjell Sjöström
  • Ingrid Häggström
  • Per-Olof Nyman
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences

Keywords

  • Laccase, Phenol oxidase, Multi-copper enzyme, White-rot fungus, Lignin degradation, (T. versicolor)
Original languageEnglish
Pages (from-to)210-215
JournalBBA - Protein Structure and Molecular Enzymology
Volume1251
Issue number2
Publication statusPublished - 1995
Publication categoryResearch
Peer-reviewedYes