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Archives of Biochemistry and Biophysics, ISSN 0003-9861, 05/2015, Volume 574, pp. 108 - 119
Four heme peroxidase superfamilies (peroxidase–catalase, peroxidase–cyclooxygenase, peroxidase–chlorite dismutase and peroxidase–peroxygenase superfamily)... 
Peroxidase–peroxygenase superfamily | Peroxidase–cyclooxygenase superfamily | Heme peroxidase | Peroxidase–catalase superfamily | Peroxidase–chlorite dismutase superfamily | Peroxidase-chlorite dismutase superfamily | Peroxidase-catalase superfamily | Peroxidase-cyclooxygenase superfamily | Peroxidase-peroxygenase superfamily | CATALASE-PEROXIDASE | PROTEIN | ASCORBATE-PEROXIDASE | ALPHA-DIOXYGENASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BACTERIAL PEROXIDASE | CHLORITE DISMUTASES | BIOPHYSICS | FUNGAL | CLASS-I | BINDING | Biological Evolution | Catalase - metabolism | Peroxidases - chemistry | Prostaglandin-Endoperoxide Synthases - metabolism | Heme | Models, Molecular | Peroxidases - metabolism | Protein Conformation | Peroxidase | Index Medicus | MnP, manganese peroxidase | HGT, horizontal gene transfer | WSC, cell-wall integrity & stress response component | PERCAL, calcium binding motif | LDS, linoleate diol synthase | ML, maximum likelihood method | MPO, myeloperoxidase | CcP, cytochrome c peroxidase | HRP, horseradish peroxidase | KatG, catalase–peroxidase | PDB, Protein Data Bank | APx, ascorbate peroxidase | TPO, thyroid peroxidase | EPO, eosinophil peroxidase | SCOP, structural classification of proteins | Pfam, protein families database | LspPOX, Lyngbya peroxidase | DyP, dye-decolorizing peroxidase | Cld, chlorite dismutase | LPO, lactoperoxidase
Journal Article
Journal of the Science of Food and Agriculture, ISSN 0022-5142, 08/2017, Volume 97, Issue 10, pp. 3249 - 3260
BACKGROUNDPeroxidase activity was increased during germination of green gram and such an increase may have benefits in many physiological processes. The... 
germination | phenol | temperature stability | peroxidase | green gram | chlorophenol | p-chlorophenol | FRUITS | SOYBEAN PEROXIDASE | FOOD SCIENCE & TECHNOLOGY | HORSERADISH-PEROXIDASE | ENZYME | POLYPHENOL OXIDASE | AGRICULTURE, MULTIDISCIPLINARY | HYDROGEN-PEROXIDE | CHEMISTRY, APPLIED | MUNG BEAN HYPOCOTYL | LEAF | Enzymes, Immobilized - metabolism | Vigna - chemistry | Plant Roots - genetics | Enzymes, Immobilized - isolation & purification | Peroxidase - chemistry | Phenol - metabolism | Plant Proteins - chemistry | Vigna - enzymology | Plant Proteins - metabolism | Chlorophenols - metabolism | Plant Roots - growth & development | Plant Proteins - isolation & purification | Enzymes, Immobilized - chemistry | Plant Roots - metabolism | Enzyme Stability | Vigna - growth & development | Vigna - genetics | Peroxidase - isolation & purification | Plant Proteins - genetics | Water Pollutants, Chemical - metabolism | Enzymes, Immobilized - genetics | Plant Roots - enzymology | Peroxidase - genetics | Kinetics | Hydrogen-Ion Concentration | Peroxidase - metabolism | Physiological aspects | Phenols | Cysteine | Peroxidase | Germination | p-Chlorophenol | Temperature | Hydrogen peroxide | Enzyme activity | Roots | Horseradish peroxidase | Optimization | Molecular weight | Enzymatic activity | Temperature effects | pH | Electrophoresis | Extraction | Oxidation | Physiology | Copper | Dithiothreitol | Enzymes | Stability | Purification | Gel electrophoresis | Wastewater | Phenolic compounds | Substrates | o-Dianisidine | Chlorophenol | Sodium | Homogeneity | Index Medicus
Journal Article
Biochimie, ISSN 0300-9084, 03/2012, Volume 94, Issue 3, pp. 673 - 683
All phytopathogenic fungi have two catalase–peroxidase paralogues located either intracellularly (KatG1) or extracellularly (KatG2). Here, for the first time a... 
Extracellular catalase–peroxidase | Oxidative stress | Phytopathogen | Reduction potential | Peroxidases–catalase superfamily | Resonance Raman spectroscopy | Extracellular catalase-peroxidase | Peroxidases-catalase superfamily | CELLS | PROTEIN | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESONANCE RAMAN-SPECTRA | HEME PEROXIDASES | ENZYME | RICE BLAST FUNGUS | SPECTROSCOPIC CHARACTERIZATION | CYTOCHROME-C PEROXIDASE | CYTOSOLIC ASCORBATE PEROXIDASE | Fungal Proteins - chemistry | Magnaporthe - enzymology | Oxidative Stress | Phylogeny | Catalase - classification | Peroxidases - classification | Catalase - metabolism | Peroxidases - chemistry | Magnaporthe - metabolism | Peroxidases - metabolism | Spectrum Analysis, Raman | Catalase - chemistry | Fungal Proteins - metabolism | Electrochemical reactions | Lignin | Hydrogen | Genes | Liquid chromatography | Cyanides | Raman spectroscopy | Cytochrome c | Histidine | Codon | Ionization | Hydroxylapatite | Heme | Electrochemistry | Peroxidase | Chemical properties | Mass spectrometry | Phenylalanine | Resveratrol | Cyanide | Spectroscopy | Data processing | Mass spectroscopy | pH effects | Host-pathogen interactions | rice blast | Catalase | Phytopathogenic fungi | Adducts | Structure-function relationships | Index Medicus | MnP, manganese peroxidase | HGT, horizontal gene transfer | 6c, six-coordinated | ESI, electrospray ionization | MagKatG2, catalase–peroxidase from Magnaporthe grisea | IPTG, isopropyl-β-thiogalactopyranoside | QS, quantum mixed-spin | CcP, cytochrome c peroxidase | HS, high-spin | HRP, horseradish peroxidase | LC, liquid chromatography | MCD, monochlorodimedone | KatG1, intracellular eukaryotic catalase–peroxidase | 5c, five-coordinated | BP1, barley peroxidase type 1 | KatG, catalase–peroxidase | Research Paper | E°′, reduction potential, referred to the standard hydrogen electrode, measured at pH 7.0 | RT-PCR, reverse-transcription PCR | SBP, soybean peroxidase | SHE, standard hydrogen electrode | MOPS, 4-morpholinepropane sulfonic acid | CAI, codon adaptation index | CAPS, 3-(cyclohexylamino)propane-1-sulfonic acid | l-DOPA, 3,4-dihydroxy-l-phenylalanine | APx, ascorbate peroxidase | ARP, Arthromyces ramosus peroxidase | ECD, electronic CD | CT, charge transfer | RR, resonance Raman | OTTLE, optically transparent thin-layer electrochemistry | MCAC, metal chelate affinity chromatography | LS, low-spin | CCD, charge-coupled device | NJ, neighbor-joining method | CIP, Coprinus cinereus peroxidase | LiP, lignin peroxidase | HA, hydroxyapatite | KatG2, extracellular eukaryotic catalase–peroxidase
Journal Article
Journal Article
Nature Nanotechnology, ISSN 1748-3387, 2007, Volume 2, Issue 9, pp. 577 - 583
Journal Article