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Título

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

AutorLinde, Dolores ; Ruiz-Dueñas, F. J. ; Fernández-Fueyo, Elena ; Guallar, Victor; Hammel, Kenneth E.; Pogni, Rebecca; Martínez, Ángel T.
Palabras claveDye-decolorizing peroxidases
CDE superfamily
Molecular structure
Reaction mechanism
Catalytic tryptophan
Long-range electron transfer;
Substituted anthraquinone breakdown
Ligninolysis
Fecha de publicación28-ene-2015
EditorElsevier
CitaciónArch Biochem Biophys 574: 66-74 (2015)
ResumenThe first enzyme with dye-decolorizing peroxidase (DyP) activity was described in 1999 from an arthroconidial culture of the fungus Bjerkandera adusta. However, the first DyP sequence had been deposited three years before, as a peroxidase gene from a culture of an unidentified fungus of the family Polyporaceae (probably Irpex lacteus). Since the first description, fewer than ten basidiomycete DyPs have been purified and characterized, but a large number of sequences are available from genomes. DyPs share a general fold and heme location with chlorite dismutases and other DyP-type related proteins (such as Escherichia coli EfeB), forming the CDE superfamily. Taking into account the lack of an evolutionary relationship with the catalase-peroxidase superfamily, the observed heme pocket similarities must be considered as a convergent type of evolution to provide similar reactivity to the enzyme cofactor. Studies on the Auricularia auricula-judae DyP showed that high-turnover oxidation of anthraquinone type and other DyP substrates occurs via long-range electron transfer from an exposed tryptophan (Trp377, conserved in most basidiomycete DyPs), whose catalytic radical was identified in the H2O2-activated enzyme. The existence of accessory oxidation sites in DyP is suggested by the residual activity observed after site-directed mutagenesis of the above tryptophan. DyP degradation of substituted anthraquinone dyes (such as Reactive Blue 5) most probably proceeds via typical one-electron peroxidase oxidations and product breakdown without a DyP-catalyzed hydrolase reaction. Although various DyPs are able to break down phenolic lignin model dimers, and basidiomycete DyPs also present marginal activity on nonphenolic dimers, a significant contribution to lignin degradation is unlikely because of the low activity on high redox-potential substrates.
Descripción16 p.-6 fig.
Versión del editorhttp://dx.doi.org/ 10.1016/j.abb.2015.01.018
URIhttp://hdl.handle.net/10261/121046
DOI10.1016/j.abb.2015.01.018
ISSN0003-9861
E-ISSN1096-0384
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