Wood Ear, Kikurage · 2019 · Research Support, Non U.S. Gov'T
Low relevanceDifferent fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan.
Auricularia auricula-judae
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)
Metadata-grounded summary
Citation 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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