Basidiomycete DyPs: Genomic diversity, structural–functional aspects, reaction mechanism and environmental significance

• Published in: Archives of biochemistry and biophysics Vol. 574; pp. 66 - 74
• Main Authors: Linde, Dolores, Ruiz-Dueñas, Francisco J., Fernández-Fueyo, Elena, Guallar, Victor, Hammel, Kenneth E., Pogni, Rebecca, Martínez, Angel T.
• Format: Journal Article Publication
• Language: English
• Published: United States Elsevier Inc 15.05.2015; Elsevier
• Subjects: anthraquinones; Auricularia auricula; Basidiomycota - enzymology; Basidiomycota - genetics; Bjerkandera adusta; Catalytic Domain; Catalytic tryptophan; CDE superfamily; Color; Coloring Agents - metabolism; Dye-decolorizing peroxidases; dyes; electron transfer; Enginyeria mecànica; Escherichia coli; fungi; genes; Genetic code; genetic variation; Genome, Fungal; Genètica bioquímica; heme; Impacte ambiental; Irpex lacteus; lignin; Ligninolysis; Long-range electron transfer; Molecular structure; oxidation; peroxidase; Peroxidases - chemistry; Peroxidases - genetics; Peroxidases - metabolism; Phylogeny; Polyporaceae; Protein Conformation; Protein Folding; proteins; Reaction mechanism; reaction mechanisms; redox potential; site-directed mutagenesis; Substituted anthraquinone breakdown; tryptophan; Àrees temàtiques de la UPC; Substituted anthraquinone breakdown; Long-range electron transfer; Dye-decolorizing peroxidases; Molecular structure; Ligninolysis; Reaction mechanism; CDE superfamily; Catalytic tryptophan

[Display omitted] •Dye-decolorizing peroxidase (DyP) genes were mined from basidiomycete genomes.•Structural–functional studies show a conserved tryptophan involved in catalysis.•Marginal activity after tryptophan substitution suggests additional oxidation sites.•DyP one-electron oxidation likely su...