DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases. - Wikidata - wikimedia - TriplyDB

DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases.

DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases.

http://www.wikidata.org/entity/Q31132803

about

A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120 Crystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157 The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue First Crystal Structure of a Fungal High-redox Potential Dye-decolorizing Peroxidase: SUBSTRATE INTERACTION SITES AND LONG-RANGE ELECTRON TRANSFER Distal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase: ARGININE BUT NOT ASPARTATE IS ESSENTIAL FOR PEROXIDASE ACTIVITY Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability Anabaena sp. DyP-type peroxidase is a tetramer consisting of two asymmetric dimers A 14.7 kDa protein from Francisella tularensis subsp. novicida (named FTN_1133), involved in the response to oxidative stress induced by organic peroxides, is not endowed with thiol-dependent peroxidase activity Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme Redox thermodynamics of high-spin and low-spin forms of chlorite dismutases with diverse subunit and oligomeric structures.Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)Characterization of Dye-decolorizing Peroxidase (DyP) from Thermomonospora curvata Reveals Unique Catalytic Properties of A-type DyPs.Coordination of frontline defense mechanisms under severe oxidative stress.Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase.Application of a novel alkali-tolerant thermostable DyP-type peroxidase from Saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp.The Escherichia coli protein YfeX functions as a porphyrinogen oxidase, not a heme dechelatase Evolutionary relationships between heme-binding ferredoxin α + β barrels.A survey of schistosome protein domain types: insights into unique biological properties.Characterization of a novel dye-decolorizing peroxidase (DyP)-type enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw.Production of dioxygen in the dark: dismutases of oxyanions.Actinobacterial peroxidases: an unexplored resource for biocatalysis.Adventures in Rhodococcus - from steroids to explosives.DyP-type peroxidases: a promising and versatile class of enzymes.The ligninolytic peroxidases in the genus Pleurotus: divergence in activities, expression, and potential applications.Expression, purification and crystallization of a dye-decolourizing peroxidase from Dictyostelium discoideum.Biotechnological and Biochemical Utilization of Lignin.Unleashing the potential of ligninolytic bacterial contributions towards pulp and paper industry: key challenges and new insights.Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.Encapsulins: molecular biology of the shell.New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications.Chemistry and Molecular Dynamics Simulations of Heme b-HemQ and Coproheme-HemQ.The DyP-type peroxidase DtpA is a Tat-substrate required for GlxA maturation and morphogenesis in Streptomyces.Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus.Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study.Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases.Identification and molecular characterization of a novel DyP-type peroxidase from Pseudomonas aeruginosa PKE117.Peroxidase production and ligninolytic potentials of fresh water bacteria Raoultella ornithinolytica and Ensifer adhaerens.Kinetic characterisation of a dye decolourising peroxidase from Streptomyces lividans: new insight into the mechanism of anthraquinone dye decolourisation.

P2860

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P2860

DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases.

http://www.wikidata.org/entity/Q31132803

description

2007 nî lūn-bûn

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2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

DyP, a unique dye-decolorizing ...... dine of classical peroxidases.

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DyP, a unique dye-decolorizing ...... dine of classical peroxidases.

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type

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DyP, a unique dye-decolorizing ...... dine of classical peroxidases.

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DyP, a unique dye-decolorizing ...... dine of classical peroxidases.

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DyP, a unique dye-decolorizing ...... dine of classical peroxidases.

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DyP, a unique dye-decolorizing ...... dine of classical peroxidases.

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P1433

Journal of Biological Chemistry

P1476

DyP, a unique dye-decolorizing ...... dine of classical peroxidases.

@en

P2093

Atsushi Ichiyanagi

http://www.w3.org/2001/XMLSchema#string

Makoto Shoda

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Riichi Muramatsu

http://www.w3.org/2001/XMLSchema#string

Takao Sato

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Yasushi Sugano

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P2860

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

CONFIDENCE LIMITS ON PHYLOGENIES: AN APPROACH USING THE BOOTSTRAP.

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Conversion of an engineered potassium-binding site into a calcium-selective site in cytochrome c peroxidase

The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui

The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme

The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid

Crystal structure of horseradish peroxidase C at 2.15 A resolution

Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH

The CCP4 suite: programs for protein crystallography

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scholarly article

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10.1074/JBC.M706996200

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P433

50

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P478

282

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P577

2007-10-10T00:00:00Z

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P698

17928290

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