ArticleThe Journal of biological chemistry2015
Characterization of Dye-decolorizing Peroxidase (DyP) from Thermomonospora curvata Reveals Unique Catalytic Properties of A-type DyPs.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 128 citations in OpenAlex.
- Dye-Decolorizing Peroxidase for Lignin Depolymerization: a Comprehensive Review on Enzyme Structural Characteristics, Reaction-Influencing Factors and Efficiency-Enhancing Strategies.Applied biochemistry and biotechnology · 2026Review
- Recombinant DyP peroxidases for green synthesis and characterization of poly(pyrogallol).Scientific reports · 2026Article
- Review
- 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
- The oligomeric states of dye-decolorizing peroxidases from Streptomyces lividans and their implications for mechanism of substrate oxidation.Protein science : a publication of the Protein Society · 2024Article
- Dye-Decolorizing Peroxidase ofACS omega · 2024Article
- Biochemical, Biophysical, and Structural Analysis of an Unusual DyP from the ExtremophileMolecules (Basel, Switzerland) · 2024Article
- Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases.BBA advances · 2024Article
- Fungal bioprocessing for circular bioeconomy: Exploring lignocellulosic waste valorization.Mycology · 2024Review
- Characterization of Two Marine Lignin-Degrading Consortia and the Potential Microbial Lignin Degradation Network in Nearshore Regions.Microbiology spectrum · 2023Article
- Unexpected diversity of dye-decolorizing peroxidases.Biochemistry and biophysics reports · 2023Article
- Heterologous expression, purification and structural features of nativeFrontiers in chemistry · 2023Article
- Properties, Physiological Functions and Involvement of Basidiomycetous Alcohol Oxidase in Wood Degradation.International journal of molecular sciences · 2022Review
- Genome Functional Analysis of the Psychrotrophic Lignin-Degrading BacteriumFrontiers in microbiology · 2022Article
- Unveiling molecular details behind improved activity at neutral to alkaline pH of an engineered DyP-type peroxidase.Computational and structural biotechnology journal · 2022Article
- Design and Engineering of an Efficient Peroxidase Using Myoglobin for Dye Decolorization and Lignin Bioconversion.International journal of molecular sciences · 2021Article
- Direct Electrochemical Generation of Catalytically Competent Oxyferryl Species of Classes I and P Dye Decolorizing Peroxidases.International journal of molecular sciences · 2021Article
- Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Review
- Cryptic metabolisms in anoxic subseafloor sediment.Environmental microbiology reports · 2021Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Dye-decolorizing peroxidases (DyPs) comprise a new family of heme peroxidases, which has received much attention due to their potential applications in lignin degradation. A new DyP from Thermomonospora curvata (TcDyP) was identified and characterized. Unlike other A-type enzymes, TcDyP is highly active toward a wide range of substrates including model lignin compounds, in which the catalytic efficiency with ABTS (kcat(app)/Km(app) = (1.7 × 10(7)) m(-1) s(-1)) is close to that of fungal DyPs. Stopped-flow spectroscopy was employed to elucidate the transient intermediates as well as the catalytic cycle involving wild-type (wt) and mutant TcDyPs. Although residues Asp(220) and Arg(327) are found necessary for compound I formation, His(312) is proposed to play roles in compound II reduction. Transient kinetics of hydroquinone (HQ) oxidation by wt-TcDyP showed that conversion of the compound II to resting state is a rate-limiting step, which will explain the contradictory observation made with the aspartate mutants of A-type DyPs. Moreover, replacement of His(312) and Arg(327) has significant effects on the oligomerization and redox potential (E°') of the enzyme. Both mutants were found to promote the formation of dimeric state and to shift E°' to a more negative potential. Not only do these results reveal the unique catalytic property of the A-type DyPs, but they will also facilitate the development of these enzymes as lignin degraders.
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