Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/121046
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Basidiomycete DyPs: Genomic diversity, structural-functional aspects, reaction mechanism and environmental significance |
Autor: | Linde, Dolores CSIC ORCID ; Ruiz-Dueñas, F. J. CSIC ORCID ; Fernández-Fueyo, Elena CSIC ORCID; Guallar, Victor; Hammel, Kenneth E.; Pogni, Rebecca; Martínez, Ángel T. CSIC ORCID | Palabras clave: | Dye-decolorizing peroxidases CDE superfamily Molecular structure Reaction mechanism Catalytic tryptophan Long-range electron transfer; Substituted anthraquinone breakdown Ligninolysis |
Fecha de publicación: | 28-ene-2015 | Editor: | Elsevier | Citación: | Arch Biochem Biophys 574: 66-74 (2015) | Resumen: | The 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. | Descripción: | 16 p.-6 fig. | Versión del editor: | http://dx.doi.org/ 10.1016/j.abb.2015.01.018 | URI: | http://hdl.handle.net/10261/121046 | DOI: | 10.1016/j.abb.2015.01.018 | ISSN: | 0003-9861 | E-ISSN: | 1096-0384 |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
2015-Linde-ABB-revised.pdf | Postprint | 2,23 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
69
checked on 10-mar-2024
WEB OF SCIENCETM
Citations
64
checked on 22-feb-2024
Page view(s)
411
checked on 19-abr-2024
Download(s)
308
checked on 19-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Este item está licenciado bajo una Licencia Creative Commons