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Isolation of cDNA and genomic fragments encoding the major manganese peroxidase isozyme from the white rot basidiomycetePleurotus ostreatus


We have isolated the cDNA and genomic sequences encoding the major isozyme of manganese peroxidase, MnP3, from the white rot basidiomycetePleurotus ostreatus strain IS1. The genemnp3 is interrupted by 10 introns and encodes a mature protein of 357 amino acid residues with a 26-amino-acid signal peptide. The amino acid residues known to be involved in peroxidase function and those that form the Mn-binding site in thePanerochaete chrysosporium MnP isozyme are conserved in MnP3. Comparison of the deduced primary structure of MnP3 with those of other peroxidases from various white rot fungi suggested that MnPs fromP. ostreatus andTrametes versicolor belong to a subgroup that is more similar to the lignin peroxidases than MnPs fromP. chrysosporium orCeriporiopsis subvermispora.


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Correspondence to Masaaki Kuwahara.

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Irie, T., Honda, Y., Ha, H. et al. Isolation of cDNA and genomic fragments encoding the major manganese peroxidase isozyme from the white rot basidiomycetePleurotus ostreatus . J Wood Sci 46, 230–233 (2000).

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Key words

  • Lignin degradation
  • White rot fungi
  • Ligninolytic enzyme
  • Edible mushroom
  • Heme protein