dc.contributor |
Barcelona Supercomputing Center |
dc.contributor.author |
Linde, Dolores |
dc.contributor.author |
Ruiz-Dueñas, Francisco J. |
dc.contributor.author |
Fernandez-Fueyo, Elena |
dc.contributor.author |
Guallar, Víctor |
dc.contributor.author |
Hammel, Kenneth E. |
dc.contributor.author |
Pogni, Rebecca |
dc.contributor.author |
Martínez, Angel T. |
dc.date |
2015-05-15 |
dc.identifier.citation |
Linde, Dolores [et al.]. Basidiomycete DyPs: Genomic diversity, structural–functional aspects, reaction mechanism and environmental significance. "Archives of Biochemistry and Biophysics", 15 Maig 2015, vol. 574, p. 66-74. |
dc.identifier.citation |
0003-9861 |
dc.identifier.citation |
10.1016/j.abb.2015.01.018 |
dc.identifier.uri |
http://hdl.handle.net/2117/84145 |
dc.language.iso |
eng |
dc.publisher |
Elsevier |
dc.relation |
http://www.sciencedirect.com/science/article/pii/S0003986115000430 |
dc.relation |
info:eu-repo/grantAgreement/ES/1PE/CTQ2013-48287 |
dc.relation |
info:eu-repo/grantAgreement/EC/FP7/613549/EU/Optimized oxidoreductases for medium and large scale industrial biotransformations/INDOX |
dc.rights |
Attribution-NonCommercial-NoDerivs 4.0 International License |
dc.rights |
https://creativecommons.org/licenses/by-nc-nd/4.0/ |
dc.rights |
info:eu-repo/semantics/openAccess |
dc.subject |
Àrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental |
dc.subject |
Genetic code |
dc.subject |
Dye-decolorizing peroxidases |
dc.subject |
CDE superfamily |
dc.subject |
Molecular structure |
dc.subject |
Reaction mechanism |
dc.subject |
Catalytic tryptophan |
dc.subject |
Long-range electron transfer |
dc.subject |
Substituted anthraquinone breakdown |
dc.subject |
Ligninolysis |
dc.subject |
Genètica bioquímica |
dc.title |
Basidiomycete DyPs: Genomic diversity, structural–functional aspects, reaction mechanism and environmental significance |
dc.type |
info:eu-repo/semantics/publishedVersion |
dc.type |
info:eu-repo/semantics/article |
dc.description.abstract |
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 |
dc.description.abstract |
This work was supported by the INDOX (KBBE-2013-7-613549; www.indoxproject.eu) European project, the BIO2011-26694
(HIPOP) and CTQ2013-48287 projects of the Spanish Ministry of Economy and Competitiveness (MINECO), and the PRIN 2009-STNWX3 project of the Italian Ministry of Education, University and Research (MIUR). FJR-D thanks a Ramón y Cajal contract of
MINECO. The authors thank Verónica Sáez-Jiménez for data on Reactive Blue 5 decolorization by VP and its heme-channel
variants. |
dc.description.abstract |
Peer Reviewed |