Results 11 to 20 of about 17,549 (202)

Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase. [PDF]

open access: yesFEBS J, 2021
Dye‐decolorizing peroxidases (DyPs) constitute a superfamily of heme‐containing peroxidases that are related neither to animal nor to plant peroxidase families. These are divided into four classes (types A, B, C, and D) based on sequence features.
Zitare UA   +5 more
europepmc   +5 more sources

Structural and Biochemical Characterization of a Dye-Decolorizing Peroxidase from Dictyostelium discoideum. [PDF]

open access: yesInt J Mol Sci, 2021
A novel cytoplasmic dye-decolorizing peroxidase from Dictyostelium discoideum was investigated that oxidizes anthraquinone dyes, lignin model compounds, and general peroxidase substrates such as ABTS efficiently.
Rai A   +10 more
europepmc   +10 more sources

Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O-glycosides. [PDF]

open access: yesAppl Environ Microbiol
Dye-decolorizing peroxidases are heme peroxidases with a broad range of substrate specificity. Their physiological function is still largely unknown, but a role in the depolymerization of plant cell wall polymers has been widely proposed.
Välimets S   +6 more
europepmc   +5 more sources

Fungal dye-decolorizing peroxidase diversity: roles in either intra- or extracellular processes. [PDF]

open access: yesAppl Microbiol Biotechnol, 2022
Fungal dye-decolorizing peroxidases (DyPs) have found applications in the treatment of dye-contaminated industrial wastes or to improve biomass digestibility.
Adamo M   +10 more
europepmc   +9 more sources

Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17 [PDF]

open access: yesBiotechnology for Biofuels, 2021
Background Dye-decolorizing peroxidases (DyPs) represent a novel family of heme peroxidases that use H2O2 as the final electron acceptor to catalyze the oxidation of various organic compounds.
Liuqing Li   +6 more
doaj   +3 more sources

Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete [PDF]

open access: yesAMB Express, 2018
Irpex lacteus F17 is well-known for its ability to degrade recalcitrant aromatic pollutants, which mainly results from the action of the manganese peroxidase (MnP) that it is able to produce.
Zihong Duan   +4 more
doaj   +3 more sources

Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus. [PDF]

open access: yesAMB Express, 2017
The coding sequence of a peroxidase from the secretome of Pleurotus sapidus was cloned from a cDNA library. Bioinformatic analyses revealed an open reading frame of 1551 bp corresponding to a primary translation product of 516 amino acids.
Lauber C   +5 more
europepmc   +5 more sources

Accelerated directed evolution of dye-decolorizing peroxidase using a bacterial extracellular protein secretion system (BENNY) [PDF]

open access: yesBioresources and Bioprocessing, 2019
Background Dye-decolorizing peroxidases (DyPs) are haem-containing peroxidases that show great promises in industrial biocatalysis and lignocellulosic degradation.
Abdulrahman H. A. Alessa   +7 more
doaj   +3 more sources

Unexpected diversity of dye-decolorizing peroxidases

open access: yesBiochemistry and Biophysics Reports, 2023
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 ...
Toru Yoshida, Yasushi Sugano
doaj   +3 more sources

Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound I in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB. [PDF]

open access: yesACS Catal, 2022
Controlling the reactivity of high-valent Fe(IV)–O catalytic intermediates, Compounds I and II, generated in heme enzymes upon reaction with dioxygen or hydrogen peroxide, is important for function.
Lučić M   +8 more
europepmc   +2 more sources

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