Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan.

08:00 EDT 13th May 2019 | BioPortfolio

Summary of "Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan."

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).


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This article was published in the following journal.

Name: Archives of biochemistry and biophysics
ISSN: 1096-0384


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