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Unexpected diversity of dye-decolorizing peroxidases

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. Althou...

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Detalles Bibliográficos
Autores principales: Yoshida, Toru, Sugano, Yasushi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9719856/
https://www.ncbi.nlm.nih.gov/pubmed/36478894
http://dx.doi.org/10.1016/j.bbrep.2022.101401
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author Yoshida, Toru
Sugano, Yasushi
author_facet Yoshida, Toru
Sugano, Yasushi
author_sort Yoshida, Toru
collection PubMed
description 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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spelling pubmed-97198562022-12-06 Unexpected diversity of dye-decolorizing peroxidases Yoshida, Toru Sugano, Yasushi Biochem Biophys Rep Research Article 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. Elsevier 2022-12-02 /pmc/articles/PMC9719856/ /pubmed/36478894 http://dx.doi.org/10.1016/j.bbrep.2022.101401 Text en © 2022 The Authors. Published by Elsevier B.V. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Yoshida, Toru
Sugano, Yasushi
Unexpected diversity of dye-decolorizing peroxidases
title Unexpected diversity of dye-decolorizing peroxidases
title_full Unexpected diversity of dye-decolorizing peroxidases
title_fullStr Unexpected diversity of dye-decolorizing peroxidases
title_full_unstemmed Unexpected diversity of dye-decolorizing peroxidases
title_short Unexpected diversity of dye-decolorizing peroxidases
title_sort unexpected diversity of dye-decolorizing peroxidases
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9719856/
https://www.ncbi.nlm.nih.gov/pubmed/36478894
http://dx.doi.org/10.1016/j.bbrep.2022.101401
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