Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan.

Pleurotus eryngii

SpeciesKing Oyster, Eryngii

JournalArchives of biochemistry and biophysics

Year2019

Key points

Dye-decolorizing peroxidase (DyP) from Auricularia auricula-judae and versatile peroxidase (VP) from Pleurotus eryngii oxidize the three mononitrophenol isomers
Both enzymes have been overexpressed in Escherichia coli and in vitro activated
Despite their very different three-dimensional structures, the nitrophenol oxidation site is located at a solvent-exposed aromatic residue in both DyP (Trp377) and VP (Trp164), as revealed by liquid chromatography coupled to mass spectrometry and kinetic analyses of nitrophenol oxidation by the native enzymes and their tryptophan-less variants (the latter showing 10-60 fold lower catalytic efficiencies)

From the paper

Abstract

Dye-decolorizing peroxidase (DyP) from Auricularia auricula-judae and versatile peroxidase (VP) from Pleurotus eryngii oxidize the three mononitrophenol isomers. Both enzymes have been overexpressed in Escherichia coli and in vitro activated. Despite their very different three-dimensional structures, the nitrophenol oxidation site is located at a solvent-exposed aromatic residue in both DyP (Trp377) and VP (Trp164), as revealed by liquid chromatography coupled to mass spectrometry and kinetic analyses of nitrophenol oxidation by the native enzymes and their tryptophan-less variants (the latter showing 10-60 fold lower catalytic efficiencies).

Citation

Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT (2019). Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan. Archives of biochemistry and biophysics https://doi.org/10.1016/j.abb.2019.05.010 PMID: 31095936

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