title: Basidiomycete DyPs: Genomic diversity, structural-functional aspects, reaction mechanism and environmental significance.
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.
authors: Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain.
authors: Dolores
authors: D
authors: Linde
authors: Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain.
authors: Francisco J
authors: FJ
authors: Ruiz-Dueñas
authors: Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain.
authors: Elena
authors: E
authors: Fernández-Fueyo
authors: Joint BSC-CRG-IRB Research Program in Computational Biology, Barcelona Supercomputing Center, Jordi Girona 29, E-08034 Barcelona, Spain; ICREA, Passeig Lluís Companys 23, E-08010 Barcelona, Spain.
authors: Victor
authors: V
authors: Guallar
authors: US Forest Products Laboratory, One Gifford Pinchot Drive, Madison, WI 53726, USA.
authors: Kenneth E
authors: KE
authors: Hammel
authors: Dept. Biotechnologies, Chemistry and Pharmacy, University of Siena, I-53100 Siena, Italy.
authors: Rebecca
authors: R
authors: Pogni
authors: Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain. Electronic address: ATMartinez@cib.csic.es.
authors: Angel T
authors: AT
authors: Martínez
mesh_terms: D001487:Basidiomycota / Q000201:enzymology* / Q000235:genetics; D020134:Catalytic Domain; D003116:Color; D004396:Coloring Agents / Q000378:metabolism; D016681:Genome, Fungal; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D004396:Coloring Agents; D010544:Peroxidases
keywords: CDE superfamily; Catalytic tryptophan; Dye-decolorizing peroxidases; Ligninolysis; Long-range electron transfer; Molecular structure; Reaction mechanism; Substituted anthraquinone breakdown