ArticleBiochemistry and biophysics reports2023
Unexpected diversity of dye-decolorizing peroxidases.
Article in Biochemistry and biophysics reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Recombinant DyP peroxidases for green synthesis and characterization of poly(pyrogallol).Scientific reports · 2026Article
- Review
- Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase.Applied and environmental microbiology · 2026Article
- Encapsulins: catalysis inside a shell.Current opinion in microbiology · 2025Review
- Structural and Biochemical Characterization of a Widespread Enterobacterial Peroxidase Encapsulin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Lignin-Degrading Enzymes and the Potential ofMicroorganisms · 2025Review
- Biological Upcycling of Plastics Waste.Annual review of chemical and biomolecular engineering · 2024Review
- pH-dependent and whole-cell catalytic decolorization of dyes using recombinant dye-decolorizing peroxidase from Rhodococcus jostii.Bioprocess and biosystems engineering · 2024Article
- Dye-Decolorizing Peroxidase ofACS omega · 2024Article
- A bacterial cold-active dye-decolorizing peroxidase from an Antarctic Pseudomonas strain.Applied microbiology and biotechnology · 2023Article
- Heterologous expression, purification and structural features of nativeFrontiers in chemistry · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dye-decolorizing peroxidase (DyP)-type peroxidases are a family of heme-containing peroxidases. Because DyP-type peroxidases can degrade recalcitrant anthraquinone dyes and lignin, their potential applications in the treatment of wastewater containing dyes and lignin degradation are expected. Although many DyP-type peroxidases have been characterized experimentally, most of the reported DyP-type peroxidases are from basidiomycetous fungi and bacteria. Therefore, the taxonomic distribution of the DyP-type peroxidases remains unclear. In this study, we analyzed the phylogenetic tree using all DyP-type peroxidase sequences available in the InterPro database. The findings mainly divided this family into three classes. Metazoa and Archaea also have the genes coding for DyP-type peroxidases, and the sequences belonging to two subclasses have the pyruvate formate lyase or cytochrome P450 domain in addition to the DyP domain. This study reveals differences in the conservation of important residues among classes. The findings will accelerate research on the DyP-type peroxidase family.
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Registered trials
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