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Improved Manganese-Oxidizing Activity of DypB, a Peroxidase from a Lignolytic Bacterium

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Biofuels and Biomass‐To‐Liquid Fuels in the Biorefinery: Catalytic Conversion of Lignocellulosic Biomass using Porous Materials

inferredcites →https://doi.org/10.1006/fgbi.1999.1150openalex-snapshot

Biodegradation of Lignin by White Rot Fungi

inferredcites →https://doi.org/10.1007/s00018-008-8651-8openalex-snapshot

DyP-type peroxidases comprise a novel heme peroxidase family

inferredcites →https://doi.org/10.1007/s002260100089openalex-snapshot

Oxidation of hardwood kraft-lignin to phenolic derivatives with oxygen as oxidant

inferredcites →https://doi.org/10.1007/s00253-007-1261-9openalex-snapshot

Novel peroxidases of Marasmius scorodonius degrade β-carotene

inferredcites →https://doi.org/10.1007/s00253-009-2173-7openalex-snapshot

DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes

inferredcites →https://doi.org/10.1016/0003-9861(85)90217-6openalex-snapshot

Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidiomycete, Phanerochaete chrysosporium

inferredcites →https://doi.org/10.1016/0307-4412(95)90181-7openalex-snapshot

Analysis of enzyme kinetic data

inferredcites →https://doi.org/10.1016/j.jinorgbio.2010.02.011openalex-snapshot

Ultrahigh (0.93Å) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: Implications for the catalytic mechanism

inferredcites →https://doi.org/10.1016/j.jmb.2011.02.047openalex-snapshot

Chlorite Dismutases, DyPs, and EfeB: 3 Microbial Heme Enzyme Families Comprise the CDE Structural Superfamily

inferredcites →https://doi.org/10.1016/s0021-9258(18)35893-9openalex-snapshot

Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators.

inferredcites →https://doi.org/10.1016/s0168-1656(01)00394-7openalex-snapshot

Fungal peroxidases: molecular aspects and applications

inferredcites →https://doi.org/10.1016/s1074-5521(97)90291-xopenalex-snapshot

Construction and characterization of a manganese-binding site in cytochrome c peroxidase: towards a novel manganese peroxidase

inferredcites →https://doi.org/10.1021/bi00136a011openalex-snapshot

Oxidation of phenolic arylglycerol .beta.-aryl ether lignin model compounds by manganese peroxidase from Phanerochaete chrysosporium: oxidative cleavage of an .alpha.-carbonyl model compound

inferredcites →https://doi.org/10.1021/bi002104sopenalex-snapshot

The Role of Glu39 in MnII Binding and Oxidation by Manganese Peroxidase from Phanerochaete chrysoporium

inferredcites →https://doi.org/10.1021/bi101892zopenalex-snapshot

Identification of DypB from Rhodococcus jostii RHA1 as a Lignin Peroxidase

inferredcites →https://doi.org/10.1021/bi200427hopenalex-snapshot

Characterization of Dye-Decolorizing Peroxidases from Rhodococcus jostii RHA1

inferredcites →https://doi.org/10.1021/bi990666+openalex-snapshot

Redesign of Cytochrome c Peroxidase into a Manganese Peroxidase: Role of Tryptophans in Peroxidase Activity

inferredcites →https://doi.org/10.1021/cb300383yopenalex-snapshot

Identification and Characterization of a Multifunctional Dye Peroxidase from a Lignin-Reactive Bacterium

inferredcites →https://doi.org/10.1021/cr900354uopenalex-snapshot

The Catalytic Valorization of Lignin for the Production of Renewable Chemicals

inferredcites →https://doi.org/10.1021/ja203972qopenalex-snapshot

Discovery and Characterization of Heme Enzymes from Unsequenced Bacteria: Application to Microbial Lignin Degradation

inferredcites →https://doi.org/10.1039/c1np00042jopenalex-snapshot

Pathways for degradation of lignin in bacteria and fungi

inferredcites →https://doi.org/10.1073/pnas.1119912109openalex-snapshot

Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis

inferredcites →https://doi.org/10.1074/jbc.m111.332171openalex-snapshot

Distal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase

inferredcites →https://doi.org/10.1107/s0907444905036693openalex-snapshot

Scaling and assessment of data quality

inferredcites →https://doi.org/10.1107/s0907444905039107openalex-snapshot

The integration of macromolecular diffraction data

inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot

Features and development of Coot

inferredcites →https://doi.org/10.1107/s0907444910048675openalex-snapshot

iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM

inferredcites →https://doi.org/10.1107/s0907444994003112openalex-snapshot

The CCP4 suite: programs for protein crystallography

inferredcites →https://doi.org/10.1107/s0907444996012255openalex-snapshot

Refinement of Macromolecular Structures by the Maximum-Likelihood Method

inferredcites →https://doi.org/10.1111/j.1574-6968.1999.tb13354.xopenalex-snapshot

Degradation of a non-phenolic β-O-4 substructure and of polymeric lignin model compounds by laccase ofCoriolus versicolorin the presence of 1-hydroxybenzotriazole

inferredcites →https://doi.org/10.1126/science.221.4611.661openalex-snapshot

Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium Burds

inferredcites →https://doi.org/10.1126/science.2563171openalex-snapshot

Effects of Buried Ionizable Amino Acids on the Reduction Potential of Recombinant Myoglobin

inferredcites →https://doi.org/10.1128/aem.54.12.3057-3063.1988openalex-snapshot

Characterization of an extracellular lignin peroxidase of the lignocellulolytic actinomycete Streptomyces viridosporus

inferredcites →https://doi.org/10.1128/aem.62.10.3679-3686.1996openalex-snapshot

Manganese-Dependent Cleavage of Nonphenolic Lignin Structures by Ceriporiopsis subvermispora in the Absence of Lignin Peroxidase

inferredcites →https://doi.org/10.1128/aem.63.2.815-815.1997openalex-snapshot

Manganese-Dependent Cleavage of Nonphenolic Lignin Structures by Ceriporiopsis subvermispora in the Absence of Lignin Peroxidase

inferredcites →https://doi.org/10.1128/aem.66.4.1754-1758.2000openalex-snapshot

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

inferredcites →https://doi.org/10.1128/aem.67.10.4588-4593.2001openalex-snapshot

Conversion of Milled Pine Wood by Manganese Peroxidase from Phlebia radiata

inferredcites →https://doi.org/10.1515/hfsg.1986.40.1.51openalex-snapshot

Herstellung und Charakterisierung von Polymerhölzern auf der Basis von niedrig-viskosen Epoxidharzen

inferredcites →https://doi.org/10.3390/ma3031888openalex-snapshot

Polyoxometalates in Oxidative Delignification of Chemical Pulps: Effect on Lignin

inferredcites →https://doi.org/10.4056/sigs.2104875openalex-snapshot

Complete genome sequence of “Enterobacter lignolyticus” SCF1

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Construction of Bacterial Consortium for Cornstalk Degradation in Soil

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Enzymatic and Microbial Bioconversion of Lignin to Renewable Chemicals

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Bacterial Enzymes and Multi-enzymatic Systems for Cleaning-up Dyes from the Environment

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Microbial-Assisted Systems for Lignin-Based Product Generation

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Ligninolytic Microbes and Their Role in Effluent Management of Pulp and Paper Industry

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Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)

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Characterization and use of a bacterial lignin peroxidase with an improved manganese-oxidative activity

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pH-dependent and whole-cell catalytic decolorization of dyes using recombinant dye-decolorizing peroxidase from Rhodococcus jostii

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Characterisation of Dyp-type peroxidases from Pseudomonas fluorescens Pf-5: Oxidation of Mn(II) and polymeric lignin by Dyp1B

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Basidiomycete DyPs: Genomic diversity, structural–functional aspects, reaction mechanism and environmental significance

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Understanding of Bacterial Lignin Extracellular Degradation Mechanisms by Pseudomonas putida KT2440 via Secretomic Analysis

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DyP-Type Peroxidases: Recent Advances and Perspectives

inferred← citeshttps://doi.org/10.3390/jof7050325openalex-snapshot

Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates

inferred← citeshttps://doi.org/10.3390/toxins13090602openalex-snapshot

Efficient Degradation of Zearalenone by Dye-Decolorizing Peroxidase from Streptomyces thermocarboxydus Combining Catalytic Properties of Manganese Peroxidase and Laccase

inferred← citeshttps://doi.org/10.3934/bioeng.2014.2.92openalex-snapshot

Lignin biodegradation and industrial implications

inferred← citeshttps://doi.org/10.6084/m9.figshare.21443757openalex-snapshot

Additional file 1 of Understanding of bacterial lignin extracellular degradation mechanisms by Pseudomonas putida KT2440 via secretomic analysis

inferred← citeshttps://doi.org/10.6084/m9.figshare.21443760openalex-snapshot

Additional file 2 of Understanding of bacterial lignin extracellular degradation mechanisms by Pseudomonas putida KT2440 via secretomic analysis

inferred← citeshttps://doi.org/10.6084/m9.figshare.21443763openalex-snapshot

Additional file 3 of Understanding of bacterial lignin extracellular degradation mechanisms by Pseudomonas putida KT2440 via secretomic analysis

inferred← citeshttps://doi.org/10.7324/jabb.2022.10s212openalex-snapshot

Process optimization for efficacious biodecolorization of crystal violet by Malaysian Rhodococcus pyridinivorans using monothetic analysis

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