ArticleApplied microbiology and biotechnology2010
A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily.
Article in Applied microbiology and biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 192 citations in OpenAlex.
- Recombinant DyP peroxidases for green synthesis and characterization of poly(pyrogallol).Scientific reports · 2026Article
- Microbial Lignin Valorization to Protocatechuic Acid and Catechol: Biofunneling Pathways and Metabolic Engineering Strategies.Biomolecules · 2026Review
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- Activity assays for flavoprotein oxidases: an overview.Applied microbiology and biotechnology · 2025Review
- Kraft Lignin Decomposition by Forest Soil BacteriumJournal of microbiology and biotechnology · 2024Article
- Review
- Structural basis for peroxidase encapsulation inside the encapsulin from the Gram-negative pathogen Klebsiella pneumoniae.Nature communications · 2024Article
- Dye-Decolorizing Peroxidase ofACS omega · 2024Article
- A Secreted Lignin Peroxidase Required for Fungal Growth and Virulence and Related to Plant Immune Response.International journal of molecular sciences · 2022Article
- Peroxidase-producing actinobacteria from Algerian environments and insights from the genome sequence of peroxidase-producing Streptomyces sp. S19.International microbiology : the official journal of the Spanish Society for Microbiology · 2022Article
- Design and Engineering of an Efficient Peroxidase Using Myoglobin for Dye Decolorization and Lignin Bioconversion.International journal of molecular sciences · 2021Article
- Loops around the Heme Pocket Have a Critical Role in the Function and Stability ofInternational journal of molecular sciences · 2021Article
- First Dye-Decolorizing Peroxidase from an Ascomycetous Fungus Secreted byBiomolecules · 2021Article
- Characterization of Class V DyP-Type Peroxidase SaDyP1 fromInternational journal of molecular sciences · 2021Article
- SERR Spectroelectrochemistry as a Guide for Rational Design of DyP-Based Bioelectronics Devices.International journal of molecular sciences · 2021Article
- Structural and Biochemical Characterization of a Dye-Decolorizing Peroxidase fromInternational journal of molecular sciences · 2021Article
- Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase.The FEBS journal · 2021Article
- DyP-Type Peroxidases: Recent Advances and Perspectives.International journal of molecular sciences · 2021Review
- Cryo-EM structure ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases.International journal of molecular sciences · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DyP-type peroxidases comprise a novel superfamily of heme-containing peroxidases which is unrelated to the superfamilies of known peroxidases and of which only a few members have been characterized in some detail. Here, we report the identification and characterization of a DyP-type peroxidase (TfuDyP) from the thermophilic actinomycete Thermobifida fusca. Biochemical characterization of the recombinant enzyme showed that it is a monomeric, heme-containing, thermostable, and Tat-dependently exported peroxidase. TfuDyP is not only active as dye-decolorizing peroxidase as it also accepts phenolic compounds and aromatic sulfides. In fact, it is able to catalyze enantioselective sulfoxidations, a type of reaction that has not been reported before for DyP-type peroxidases. Site-directed mutagenesis was used to determine the role of two conserved residues. D242 is crucial for catalysis while H338 represents the proximal heme ligand and is essential for heme incorporation. A genome database analysis revealed that DyP-type peroxidases are frequently found in bacterial genomes while they are extremely rare in other organisms. Most of the bacterial homologs are potential cytosolic enzymes, suggesting metabolic roles different from dye degradation. In conclusion, the detailed biochemical characterization reported here contributes significantly to our understanding of these enzymes and further emphasizes their biotechnological potential.
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