Nature, ISSN 0028-0836, 04/2016, Volume 532, Issue 7599, pp. 293 - 293
The US Department of Agriculture (USDA) will not regulate a mushroom that has been genetically modified with the gene-editing tool CRISPR.Cas9, the agency has...
MULTIDISCIPLINARY SCIENCES | Crops, Agricultural - economics | Crops, Agricultural - enzymology | United States | Genetic Engineering - economics | CRISPR-Cas Systems - genetics | Patents as Topic | Genetic Engineering - legislation & jurisprudence | Agaricus - genetics | Gene Deletion | Catechol Oxidase - metabolism | Agaricus - enzymology | Catechol Oxidase - genetics | Crops, Agricultural - genetics | Food, Genetically Modified | United States Department of Agriculture - legislation & jurisprudence | Enzymes | Federal regulation | Genetic engineering | Genetically altered foods | Mushrooms | Biotechnology industry
MULTIDISCIPLINARY SCIENCES | Crops, Agricultural - economics | Crops, Agricultural - enzymology | United States | Genetic Engineering - economics | CRISPR-Cas Systems - genetics | Patents as Topic | Genetic Engineering - legislation & jurisprudence | Agaricus - genetics | Gene Deletion | Catechol Oxidase - metabolism | Agaricus - enzymology | Catechol Oxidase - genetics | Crops, Agricultural - genetics | Food, Genetically Modified | United States Department of Agriculture - legislation & jurisprudence | Enzymes | Federal regulation | Genetic engineering | Genetically altered foods | Mushrooms | Biotechnology industry
Journal Article
Journal of Agricultural and Food Chemistry, ISSN 0021-8561, 05/2003, Volume 51, Issue 10, pp. 2837 - 2853
Tyrosinase, also known as polyphenol oxidase, is a copper-containing enzyme, which is widely distributed in microorganisms, animals, and plants. Nowadays...
Immobilization | Activators | Mushroom tyrosinase | Inhibitors | Biochemical character | Clinical studies | inhibitors | immobilization | mushroom tyrosinase | FOOD SCIENCE & TECHNOLOGY | EDIBLE MUSHROOM | ASCORBIC-ACID DERIVATIVES | PRODRUG THERAPY MDEPT | biochemical character | CARBON-PASTE ELECTRODE | activators | AGARICUS-BISPORUS TYROSINASE | SODIUM DODECYL-SULFATE | POLYPHENOL OXIDASE | L-DOPA | AGRICULTURE, MULTIDISCIPLINARY | clinical studies | COPPER ACTIVE-SITE | SLOW-BINDING INHIBITOR | CHEMISTRY, APPLIED | Enzyme Inhibitors | Vitiligo - enzymology | Neoplasms - enzymology | Substrate Specificity | Enzymes, Immobilized | Monophenol Monooxygenase - antagonists & inhibitors | Monophenol Monooxygenase - metabolism | Antioxidants | Food Industry | Cosmetics | Plants - chemistry | Agaricales - enzymology | Monophenol Monooxygenase - chemistry
Immobilization | Activators | Mushroom tyrosinase | Inhibitors | Biochemical character | Clinical studies | inhibitors | immobilization | mushroom tyrosinase | FOOD SCIENCE & TECHNOLOGY | EDIBLE MUSHROOM | ASCORBIC-ACID DERIVATIVES | PRODRUG THERAPY MDEPT | biochemical character | CARBON-PASTE ELECTRODE | activators | AGARICUS-BISPORUS TYROSINASE | SODIUM DODECYL-SULFATE | POLYPHENOL OXIDASE | L-DOPA | AGRICULTURE, MULTIDISCIPLINARY | clinical studies | COPPER ACTIVE-SITE | SLOW-BINDING INHIBITOR | CHEMISTRY, APPLIED | Enzyme Inhibitors | Vitiligo - enzymology | Neoplasms - enzymology | Substrate Specificity | Enzymes, Immobilized | Monophenol Monooxygenase - antagonists & inhibitors | Monophenol Monooxygenase - metabolism | Antioxidants | Food Industry | Cosmetics | Plants - chemistry | Agaricales - enzymology | Monophenol Monooxygenase - chemistry
Journal Article
Phytochemistry, ISSN 0031-9422, 2006, Volume 67, Issue 21, pp. 2318 - 2331
PPO, constitutive or induced by jasmonate, in coded for by multiple genes. It oxidizes mono- or dihydroxy phenols to the corresponding quinones. The products...
Pathogens | Function of enzyme | Inhibitors | Induction | Multiplicity | Distribution | Genes coding | Herbivores | Structure | Polyphenol oxidase | genes coding | multiplicity | inhibitors | DIFFERENTIAL EXPRESSION | CATECHOL OXIDASE | HYBRID POPLAR | BIOCHEMISTRY & MOLECULAR BIOLOGY | POTENT TYROSINASE INHIBITORS | distribution | function of enzyme | SOLANUM-TUBEROSUM | structure | PLANT SCIENCES | induction | pathogens | herbivores | REPRODUCTIVE DEVELOPMENT | AGARICUS-BISPORUS | polyphenol oxidase | MOLECULAR-CLONING | SENSITIVE TETRAMERIC PROTEASE | PARTIAL-PURIFICATION | Catechol Oxidase - metabolism | Fungi - enzymology | Plants - enzymology | Oxidases | Physiological aspects
Pathogens | Function of enzyme | Inhibitors | Induction | Multiplicity | Distribution | Genes coding | Herbivores | Structure | Polyphenol oxidase | genes coding | multiplicity | inhibitors | DIFFERENTIAL EXPRESSION | CATECHOL OXIDASE | HYBRID POPLAR | BIOCHEMISTRY & MOLECULAR BIOLOGY | POTENT TYROSINASE INHIBITORS | distribution | function of enzyme | SOLANUM-TUBEROSUM | structure | PLANT SCIENCES | induction | pathogens | herbivores | REPRODUCTIVE DEVELOPMENT | AGARICUS-BISPORUS | polyphenol oxidase | MOLECULAR-CLONING | SENSITIVE TETRAMERIC PROTEASE | PARTIAL-PURIFICATION | Catechol Oxidase - metabolism | Fungi - enzymology | Plants - enzymology | Oxidases | Physiological aspects
Journal Article
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 2012, Volume 113, Issue 1, pp. 42 - 47
A novel serine protease, designated as cordysobin, was purified from dried fruiting bodies of the mushroom . The isolation procedure utilized ion exchange...
Fruiting bodies | Purification | HIV-1 reverse transcriptase | Alkaline serine protease | Mushroom | Cordyceps sobolifera | FRESH FRUITING BODIES | FOOD SCIENCE & TECHNOLOGY | EDIBLE MUSHROOM | BIOCHEMICAL-CHARACTERIZATION | PLEUROTUS-ERYNGII | HYPSIZIGUS-MARMOREUS | IN-VITRO | EXTRACELLULAR PROTEASE | SENESCENT SPOROPHORES | PROLYL ENDOPEPTIDASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | AGARICUS-BISPORUS | Anti-HIV Agents - pharmacology | Serine Proteases - pharmacology | Chromatography, Ion Exchange | Temperature | Molecular Weight | Oligopeptides | HIV-1 - drug effects | Electrophoresis, Polyacrylamide Gel | HIV Reverse Transcriptase - antagonists & inhibitors | Enzyme Stability | Coumarins | Fruiting Bodies, Fungal - enzymology | Cordyceps - enzymology | Mass Spectrometry | Serine Proteases - isolation & purification | Inhibitory Concentration 50 | Anti-HIV Agents - isolation & purification | Fungal Proteins - pharmacology | Chromatography, Gel | Fungal Proteins - isolation & purification | Hydrogen-Ion Concentration | DNA polymerases | Thrombin | HIV (Viruses) | Serine | Chromatography | Dried fruit | Antiviral activity
Fruiting bodies | Purification | HIV-1 reverse transcriptase | Alkaline serine protease | Mushroom | Cordyceps sobolifera | FRESH FRUITING BODIES | FOOD SCIENCE & TECHNOLOGY | EDIBLE MUSHROOM | BIOCHEMICAL-CHARACTERIZATION | PLEUROTUS-ERYNGII | HYPSIZIGUS-MARMOREUS | IN-VITRO | EXTRACELLULAR PROTEASE | SENESCENT SPOROPHORES | PROLYL ENDOPEPTIDASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | AGARICUS-BISPORUS | Anti-HIV Agents - pharmacology | Serine Proteases - pharmacology | Chromatography, Ion Exchange | Temperature | Molecular Weight | Oligopeptides | HIV-1 - drug effects | Electrophoresis, Polyacrylamide Gel | HIV Reverse Transcriptase - antagonists & inhibitors | Enzyme Stability | Coumarins | Fruiting Bodies, Fungal - enzymology | Cordyceps - enzymology | Mass Spectrometry | Serine Proteases - isolation & purification | Inhibitory Concentration 50 | Anti-HIV Agents - isolation & purification | Fungal Proteins - pharmacology | Chromatography, Gel | Fungal Proteins - isolation & purification | Hydrogen-Ion Concentration | DNA polymerases | Thrombin | HIV (Viruses) | Serine | Chromatography | Dried fruit | Antiviral activity
Journal Article
Journal of Microbiology, ISSN 1225-8873, 4/2017, Volume 55, Issue 4, pp. 280 - 288
The morphogenesis of macromycetes is a complex multilevel process resulting in a set of molecular-genetic, physiological-biochemical, and...
Life Sciences | lytic enzymes | cell wall ultrastructure | basidiomycete morphogenesis | Microbiology | phenol oxidases | gene expression | FRUITING BODY | GILL | ELECTRON-MICROSCOPY | MICROBIOLOGY | ORGANIZATION | FUNGAL CELL-WALL | PURIFICATION | AGARICUS-BISPORUS | LENTINULA-EDODES | Gene Expression Regulation, Fungal | Hyphae - growth & development | Grifola - ultrastructure | Hydrolases - biosynthesis | Hydrolases - genetics | Hyphae - ultrastructure | Reishi - enzymology | Reishi - ultrastructure | Reishi - growth & development | Grifola - growth & development | Morphogenesis | Grifola - enzymology | Microscopy | Shiitake Mushrooms - enzymology | Shiitake Mushrooms - growth & development | Transcription, Genetic | Hyphae - enzymology | Shiitake Mushrooms - ultrastructure | Oxidases | Plant physiology | Genes | Physiological aspects | Genetic aspects | Genetic transcription | Molecular biology
Life Sciences | lytic enzymes | cell wall ultrastructure | basidiomycete morphogenesis | Microbiology | phenol oxidases | gene expression | FRUITING BODY | GILL | ELECTRON-MICROSCOPY | MICROBIOLOGY | ORGANIZATION | FUNGAL CELL-WALL | PURIFICATION | AGARICUS-BISPORUS | LENTINULA-EDODES | Gene Expression Regulation, Fungal | Hyphae - growth & development | Grifola - ultrastructure | Hydrolases - biosynthesis | Hydrolases - genetics | Hyphae - ultrastructure | Reishi - enzymology | Reishi - ultrastructure | Reishi - growth & development | Grifola - growth & development | Morphogenesis | Grifola - enzymology | Microscopy | Shiitake Mushrooms - enzymology | Shiitake Mushrooms - growth & development | Transcription, Genetic | Hyphae - enzymology | Shiitake Mushrooms - ultrastructure | Oxidases | Plant physiology | Genes | Physiological aspects | Genetic aspects | Genetic transcription | Molecular biology
Journal Article
Nature Communications, ISSN 2041-1723, 2014, Volume 5, Issue 1, p. 5675
Centuries of artificial selection have dramatically improved the yield of human agriculture; however, strong directional selection also occurs in natural...
EVOLUTION | AGRICULTURE | ENZYMES | MULTIDISCIPLINARY SCIENCES | GROWING ANT | SEQUENCE | TRANSCRIPTION | SACCHAROMYCES-CEREVISIAE | DIFFERENTIAL EXPRESSION ANALYSIS | GENOME | ATTINE ANT | Gene Expression Regulation, Fungal | Agaricus - genetics | Agaricus - metabolism | Animals | Hyphae - metabolism | Transcriptome | Agaricus - enzymology | Amino Acids, Essential - metabolism | Hyphae - enzymology | Ants - microbiology | Evolution, Molecular | Symbiosis - genetics | Biological Sciences | Biologi | Naturvetenskap | Natural Sciences
EVOLUTION | AGRICULTURE | ENZYMES | MULTIDISCIPLINARY SCIENCES | GROWING ANT | SEQUENCE | TRANSCRIPTION | SACCHAROMYCES-CEREVISIAE | DIFFERENTIAL EXPRESSION ANALYSIS | GENOME | ATTINE ANT | Gene Expression Regulation, Fungal | Agaricus - genetics | Agaricus - metabolism | Animals | Hyphae - metabolism | Transcriptome | Agaricus - enzymology | Amino Acids, Essential - metabolism | Hyphae - enzymology | Ants - microbiology | Evolution, Molecular | Symbiosis - genetics | Biological Sciences | Biologi | Naturvetenskap | Natural Sciences
Journal Article
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 06/2011, Volume 111, Issue 6, pp. 641 - 645
A novel serine protease, with a molecular mass of 19 kDa and the N-terminal sequence of ARTPEAPAEV, was isolated from dried fruiting bodies of the mushroom ....
Fruiting bodies | Pholiota nameko | Protease | Mushroom | FRESH FRUITING BODIES | FOOD SCIENCE & TECHNOLOGY | EDIBLE MUSHROOM | LYOPHYLLUM-CINERASCENS | ALKALINE PROTEASE | ENZYMATIC-PROPERTIES | CULTIVATED MUSHROOM | EXTRACELLULAR PROTEASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | FIBRINOLYTIC ENZYME | AGARICUS-BISPORUS | FLAMMULINA-VELUTIPES | Serine Proteases - metabolism | Amino Acid Sequence | Chromatography, Ion Exchange | Temperature | Molecular Weight | Enzyme Stability | Molecular Sequence Data | Fruiting Bodies, Fungal - enzymology | Sequence Homology, Amino Acid | Pholiota - enzymology | Serine Proteases - isolation & purification | Chromatography, Gel | Fungal Proteins - isolation & purification | Agaricales - enzymology | Fungal Proteins - metabolism | Hydrogen-Ion Concentration | Chemical properties | Casein | Proteases | Serine | Dried fruit | Enzymes | Filtration | Purification | Metals | phenylmethylsulfonyl fluoride | pH effects | Chromatography | Fruit bodies | Basidiocarps | Temperature effects | Cations | Serine proteinase | Ion exchange
Fruiting bodies | Pholiota nameko | Protease | Mushroom | FRESH FRUITING BODIES | FOOD SCIENCE & TECHNOLOGY | EDIBLE MUSHROOM | LYOPHYLLUM-CINERASCENS | ALKALINE PROTEASE | ENZYMATIC-PROPERTIES | CULTIVATED MUSHROOM | EXTRACELLULAR PROTEASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | FIBRINOLYTIC ENZYME | AGARICUS-BISPORUS | FLAMMULINA-VELUTIPES | Serine Proteases - metabolism | Amino Acid Sequence | Chromatography, Ion Exchange | Temperature | Molecular Weight | Enzyme Stability | Molecular Sequence Data | Fruiting Bodies, Fungal - enzymology | Sequence Homology, Amino Acid | Pholiota - enzymology | Serine Proteases - isolation & purification | Chromatography, Gel | Fungal Proteins - isolation & purification | Agaricales - enzymology | Fungal Proteins - metabolism | Hydrogen-Ion Concentration | Chemical properties | Casein | Proteases | Serine | Dried fruit | Enzymes | Filtration | Purification | Metals | phenylmethylsulfonyl fluoride | pH effects | Chromatography | Fruit bodies | Basidiocarps | Temperature effects | Cations | Serine proteinase | Ion exchange
Journal Article
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 2008, Volume 105, Issue 1, pp. 69 - 72
The decolorization of industrial dyes was investigated using extracellular enzymes produced by 21 basidiomycetes, mainly edible mushrooms. Among the 27 dyes...
bioremediation | basidiomycete | dye decolorization | laccase | OXIDATION | EXTRACELLULAR LACCASE | FUNGI | FOOD SCIENCE & TECHNOLOGY | PHANEROCHAETE-CHRYSOSPORIUM | REMOVAL | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PURIFICATION | AGARICUS-BISPORUS | Biodegradation, Environmental | Fungal Proteins - chemistry | Sulfonic Acids - chemistry | Oxidoreductases - isolation & purification | Basidiomycota - enzymology | Coloring Agents - metabolism | Benzothiazoles - chemistry | Fungal Proteins - isolation & purification | Basidiomycota - isolation & purification | Oxidoreductases - chemistry | Index Medicus
bioremediation | basidiomycete | dye decolorization | laccase | OXIDATION | EXTRACELLULAR LACCASE | FUNGI | FOOD SCIENCE & TECHNOLOGY | PHANEROCHAETE-CHRYSOSPORIUM | REMOVAL | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PURIFICATION | AGARICUS-BISPORUS | Biodegradation, Environmental | Fungal Proteins - chemistry | Sulfonic Acids - chemistry | Oxidoreductases - isolation & purification | Basidiomycota - enzymology | Coloring Agents - metabolism | Benzothiazoles - chemistry | Fungal Proteins - isolation & purification | Basidiomycota - isolation & purification | Oxidoreductases - chemistry | Index Medicus
Journal Article
Applied Microbiology and Biotechnology, ISSN 0175-7598, 06/2017, Volume 101, Issue 12, pp. 5213 - 5222
Spent mushroom substrate (SMS) of Pleurotus ostreatus was supplemented with wheat bran and soybean flour in various proportions to obtain C/N ratios of 10, 20,...
Biomass | Glass tubes | Growth rate | Exopolysaccharides | Fruiting body | Solid state fermentation | MEDICINAL MUSHROOMS | SHIITAKE | EDODES | BIOCONVERSION | WHEAT-STRAW | SAJOR-CAJU | COMPOST | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENZYMES | OSTREATUS | AGARICUS-BISPORUS | Dietary Fiber - pharmacology | Pleurotus - enzymology | Lentinula - enzymology | Fruiting Bodies, Fungal - growth & development | Flour | Ganoderma - growth & development | Laccase - biosynthesis | Fermentation | Ganoderma - enzymology | Laccase - metabolism | Soybeans - chemistry | Fruiting Bodies, Fungal - drug effects | Ganoderma - drug effects | Pleurotus - drug effects | Complex Mixtures - pharmacology | Pleurotus - growth & development | Mycelium - growth & development | Mycelium - drug effects | Lentinula - drug effects | Lentinula - growth & development | Agaricales - chemistry | Oxidases | Physiological aspects | Mushrooms | Cultivation | Secretion | Recovery | Fruit bodies | Fungi | Solid state | Composting | Agronomy | Supplementation | Wheat | Colonization | Laccase
Biomass | Glass tubes | Growth rate | Exopolysaccharides | Fruiting body | Solid state fermentation | MEDICINAL MUSHROOMS | SHIITAKE | EDODES | BIOCONVERSION | WHEAT-STRAW | SAJOR-CAJU | COMPOST | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENZYMES | OSTREATUS | AGARICUS-BISPORUS | Dietary Fiber - pharmacology | Pleurotus - enzymology | Lentinula - enzymology | Fruiting Bodies, Fungal - growth & development | Flour | Ganoderma - growth & development | Laccase - biosynthesis | Fermentation | Ganoderma - enzymology | Laccase - metabolism | Soybeans - chemistry | Fruiting Bodies, Fungal - drug effects | Ganoderma - drug effects | Pleurotus - drug effects | Complex Mixtures - pharmacology | Pleurotus - growth & development | Mycelium - growth & development | Mycelium - drug effects | Lentinula - drug effects | Lentinula - growth & development | Agaricales - chemistry | Oxidases | Physiological aspects | Mushrooms | Cultivation | Secretion | Recovery | Fruit bodies | Fungi | Solid state | Composting | Agronomy | Supplementation | Wheat | Colonization | Laccase
Journal Article
Journal of Enzyme Inhibition and Medicinal Chemistry, ISSN 1475-6366, 01/2019, Volume 34, Issue 1, pp. 927 - 936
Skin ageing results from enhanced activation of intracellular enzymes such as collagenases, elastases and tyrosinase, stimulated by intrinsic ageing and...
photoageing | molecular docking | enzyme inhibition | matrix metalloproteinases | Caffeine | CHEMISTRY, MEDICINAL | PROTEIN | SMALL MOLECULES | BIOCHEMISTRY & MOLECULAR BIOLOGY | PARAMETERS | MELANIN | PROTEASES | POLYPHENOLS | PANCREATIC ELASTASE | STRUCTURAL BASIS | SKIN | UV-LIGHT | Enzyme Inhibitors - pharmacology | Monophenol Monooxygenase - antagonists & inhibitors | Pancreatic Elastase - metabolism | Structure-Activity Relationship | Pancreatic Elastase - antagonists & inhibitors | Enzyme Inhibitors - chemical synthesis | Clostridium histolyticum - enzymology | Molecular Dynamics Simulation | Monophenol Monooxygenase - metabolism | Dose-Response Relationship, Drug | Animals | Swine | Caffeine - chemistry | Computer Simulation | Enzyme Inhibitors - chemistry | Caffeine - pharmacology | Agaricus - enzymology | Ligands | Collagenases - metabolism | In Vitro Techniques | Pancreas - enzymology
photoageing | molecular docking | enzyme inhibition | matrix metalloproteinases | Caffeine | CHEMISTRY, MEDICINAL | PROTEIN | SMALL MOLECULES | BIOCHEMISTRY & MOLECULAR BIOLOGY | PARAMETERS | MELANIN | PROTEASES | POLYPHENOLS | PANCREATIC ELASTASE | STRUCTURAL BASIS | SKIN | UV-LIGHT | Enzyme Inhibitors - pharmacology | Monophenol Monooxygenase - antagonists & inhibitors | Pancreatic Elastase - metabolism | Structure-Activity Relationship | Pancreatic Elastase - antagonists & inhibitors | Enzyme Inhibitors - chemical synthesis | Clostridium histolyticum - enzymology | Molecular Dynamics Simulation | Monophenol Monooxygenase - metabolism | Dose-Response Relationship, Drug | Animals | Swine | Caffeine - chemistry | Computer Simulation | Enzyme Inhibitors - chemistry | Caffeine - pharmacology | Agaricus - enzymology | Ligands | Collagenases - metabolism | In Vitro Techniques | Pancreas - enzymology
Journal Article
Analytical and Bioanalytical Chemistry, ISSN 1618-2642, 1/2018, Volume 410, Issue 1, pp. 27 - 32
Up to now, knowledge of enzymes capable of degrading various contaminants of emerging concern (CEC) is limited, which is especially due to the lack of rapid...
Biochemistry, general | Food Science | Robotic nano-ESI | High-throughput screening | Laboratory Medicine | Oxidative enzymes | Emerging contaminants | Chemistry | Analytical Chemistry | Monitoring/Environmental Analysis | Characterization and Evaluation of Materials | Miniaturization | Mass spectrometry | CHEMISTRY, ANALYTICAL | MEDIATOR | BIOCHEMICAL RESEARCH METHODS | HORSERADISH-PEROXIDASE | MASS-SPECTROMETRY | REMOVAL | TRACE ORGANIC CONTAMINANTS | WASTE-WATER | ENZYMES | Pharmaceutical Preparations - isolation & purification | Miniaturization - methods | Environmental Monitoring - instrumentation | High-Throughput Screening Assays - instrumentation | Environmental Pollutants - metabolism | Equipment Design | Spectrometry, Mass, Electrospray Ionization - instrumentation | Monophenol Monooxygenase - metabolism | Time Factors | Agaricus - enzymology | Armoracia - enzymology | Environmental Restoration and Remediation | High-Throughput Screening Assays - methods | Biocatalysis | Environmental Monitoring - economics | Environmental Monitoring - methods | Environmental Pollutants - isolation & purification | Lab-On-A-Chip Devices | Trametes - enzymology | High-Throughput Screening Assays - economics | Laccase - metabolism | Pharmaceutical Preparations - metabolism | Spectrometry, Mass, Electrospray Ionization - economics | Spectrometry, Mass, Electrospray Ionization - methods | Miniaturization - instrumentation | Horseradish Peroxidase - metabolism | Technology application | Usage | Observations | Environmental monitoring | Methods | Robotics | Decomposition (Chemistry) | Drugs | Catalysts | Gabapentin | Pollution monitoring | Horseradish peroxidase | Diclofenac | Degradation | Sulfamethoxazole | Venlafaxine | Peroxidase | Monitoring | Laccase | Biodegradation | Enzymes | Metoprolol | Ions | Mass spectroscopy | Conversion | Carbamazepine | Screening | Mefenamic acid | Acetaminophen | Ionization | Contaminants | Environmental degradation | Tyrosinase | Benzotriazole
Biochemistry, general | Food Science | Robotic nano-ESI | High-throughput screening | Laboratory Medicine | Oxidative enzymes | Emerging contaminants | Chemistry | Analytical Chemistry | Monitoring/Environmental Analysis | Characterization and Evaluation of Materials | Miniaturization | Mass spectrometry | CHEMISTRY, ANALYTICAL | MEDIATOR | BIOCHEMICAL RESEARCH METHODS | HORSERADISH-PEROXIDASE | MASS-SPECTROMETRY | REMOVAL | TRACE ORGANIC CONTAMINANTS | WASTE-WATER | ENZYMES | Pharmaceutical Preparations - isolation & purification | Miniaturization - methods | Environmental Monitoring - instrumentation | High-Throughput Screening Assays - instrumentation | Environmental Pollutants - metabolism | Equipment Design | Spectrometry, Mass, Electrospray Ionization - instrumentation | Monophenol Monooxygenase - metabolism | Time Factors | Agaricus - enzymology | Armoracia - enzymology | Environmental Restoration and Remediation | High-Throughput Screening Assays - methods | Biocatalysis | Environmental Monitoring - economics | Environmental Monitoring - methods | Environmental Pollutants - isolation & purification | Lab-On-A-Chip Devices | Trametes - enzymology | High-Throughput Screening Assays - economics | Laccase - metabolism | Pharmaceutical Preparations - metabolism | Spectrometry, Mass, Electrospray Ionization - economics | Spectrometry, Mass, Electrospray Ionization - methods | Miniaturization - instrumentation | Horseradish Peroxidase - metabolism | Technology application | Usage | Observations | Environmental monitoring | Methods | Robotics | Decomposition (Chemistry) | Drugs | Catalysts | Gabapentin | Pollution monitoring | Horseradish peroxidase | Diclofenac | Degradation | Sulfamethoxazole | Venlafaxine | Peroxidase | Monitoring | Laccase | Biodegradation | Enzymes | Metoprolol | Ions | Mass spectroscopy | Conversion | Carbamazepine | Screening | Mefenamic acid | Acetaminophen | Ionization | Contaminants | Environmental degradation | Tyrosinase | Benzotriazole
Journal Article
Biochemistry, ISSN 0006-2960, 06/2011, Volume 50, Issue 24, pp. 5477 - 5486
Tyrosinase catalyzes the conversion of phenolic compounds into their quinone derivatives, which are precursors for the formation of melanin, a ubiquitous...
REFINEMENT | PLANT | ACTIVATION | PROTEIN | INHIBITION | MECHANISM | POLYPHENOL OXIDASE | SEQUENCE | DIFFRACTION DATA | MULTIPLE FORMS | ISOFORMS | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEMOCYANIN | Amino Acid Sequence | Protein Subunits | Catalytic Domain | DNA, Fungal - genetics | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Protein Folding | Monophenol Monooxygenase - metabolism | Sequence Homology, Amino Acid | Agaricus - genetics | Base Sequence | Copper - metabolism | Protein Structure, Quaternary | Protein Binding | Agaricus - enzymology | Monophenol Monooxygenase - genetics | Binding Sites | Monophenol Monooxygenase - chemistry | Tropolone - metabolism | Tyrosine | Calcium | Analysis | Crystals | Enzyme binding | Chemical properties | Structure | sequence | protein | plant | diffraction data | inhibition | polyphenol oxidase | refinement | multiple forms | mechanism | activation
REFINEMENT | PLANT | ACTIVATION | PROTEIN | INHIBITION | MECHANISM | POLYPHENOL OXIDASE | SEQUENCE | DIFFRACTION DATA | MULTIPLE FORMS | ISOFORMS | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEMOCYANIN | Amino Acid Sequence | Protein Subunits | Catalytic Domain | DNA, Fungal - genetics | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Protein Folding | Monophenol Monooxygenase - metabolism | Sequence Homology, Amino Acid | Agaricus - genetics | Base Sequence | Copper - metabolism | Protein Structure, Quaternary | Protein Binding | Agaricus - enzymology | Monophenol Monooxygenase - genetics | Binding Sites | Monophenol Monooxygenase - chemistry | Tropolone - metabolism | Tyrosine | Calcium | Analysis | Crystals | Enzyme binding | Chemical properties | Structure | sequence | protein | plant | diffraction data | inhibition | polyphenol oxidase | refinement | multiple forms | mechanism | activation
Journal Article
Planta, ISSN 0032-0935, 9/2015, Volume 242, Issue 3, pp. 519 - 537
Main conclusion Aurone synthase belongs to the novel group 2 polyphenol oxidases and the presented kinetic characterization suggests a differing aurone...
Life Sciences | Forestry | 4-Deoxyaurone | Agriculture | Ecology | Type-3 copper enzyme | Proteolytic activation | Allosteric activation | Plant Sciences | Aurone synthase | Polyphenol oxidase | SUICIDE INACTIVATION | FLAVONOID CHEMISTRY | ANTHOCHLOR PIGMENTS | COREOPSIS-LANCEOLATA L | KINETIC CHARACTERIZATION | PLANT SCIENCES | MUSHROOM TYROSINASE | FUNCTIONAL EXPRESSION | AGARICUS-BISPORUS | AUREUSIDIN SYNTHASE | FLOWER COLORATION | Plant Proteins - metabolism | Flowers - enzymology | Coreopsis - enzymology | Catechol Oxidase - metabolism | Benzofurans - metabolism | Oxidases | Physiological aspects | Polyphenols | Biological products | Peptides | Original
Life Sciences | Forestry | 4-Deoxyaurone | Agriculture | Ecology | Type-3 copper enzyme | Proteolytic activation | Allosteric activation | Plant Sciences | Aurone synthase | Polyphenol oxidase | SUICIDE INACTIVATION | FLAVONOID CHEMISTRY | ANTHOCHLOR PIGMENTS | COREOPSIS-LANCEOLATA L | KINETIC CHARACTERIZATION | PLANT SCIENCES | MUSHROOM TYROSINASE | FUNCTIONAL EXPRESSION | AGARICUS-BISPORUS | AUREUSIDIN SYNTHASE | FLOWER COLORATION | Plant Proteins - metabolism | Flowers - enzymology | Coreopsis - enzymology | Catechol Oxidase - metabolism | Benzofurans - metabolism | Oxidases | Physiological aspects | Polyphenols | Biological products | Peptides | Original
Journal Article
PLoS One, ISSN 1932-6203, 2015, Volume 10, Issue 8, p. e0134169
The fungus Agaricus bisporus is commercially grown for the production of edible mushrooms. This cultivation occurs on compost, but not all of this substrate is...
ENZYME-ACTIVITIES | H-1-NMR SPECTROSCOPY | OLIGOSACCHARIDES | MULTIDISCIPLINARY SCIENCES | WHEAT-FLOUR ARABINOXYLAN | MODE | PURIFICATION | ASPERGILLUS-AWAMORI | BUTTON MUSHROOM | Endo-1,4-beta Xylanases - metabolism | Mycelium - physiology | Xylans - metabolism | Mycelium - enzymology | Carbohydrate Metabolism | Agaricus - growth & development | Cellulases - metabolism | Mannans - metabolism | Xylosidases - metabolism | Mycelium - growth & development | Soil - chemistry | Agaricus - enzymology | Agaricus - physiology | Cellulose - metabolism | Physiological aspects | Polysaccharides | Genetic aspects | Agaricus | Research | Residues | Laboratories | Genomics | Cellulose | Xylan | Genomes | Fruit bodies | Substitutes | Degradation | Fungi | Xylanase | Xylosidase | Physiology | Arabinofuranosidase | Saccharides | Carbohydrates | Enzymes | Cultivation | Mushrooms | Fragments | Substrates | Biological diversity | Xylose | Studies | Basidiocarps | Composting | Composts | h-1-nmr spectroscopy | mode | button mushroom | purification | oligosaccharides | wheat-flour arabinoxylan | aspergillus-awamori | enzyme-activities
ENZYME-ACTIVITIES | H-1-NMR SPECTROSCOPY | OLIGOSACCHARIDES | MULTIDISCIPLINARY SCIENCES | WHEAT-FLOUR ARABINOXYLAN | MODE | PURIFICATION | ASPERGILLUS-AWAMORI | BUTTON MUSHROOM | Endo-1,4-beta Xylanases - metabolism | Mycelium - physiology | Xylans - metabolism | Mycelium - enzymology | Carbohydrate Metabolism | Agaricus - growth & development | Cellulases - metabolism | Mannans - metabolism | Xylosidases - metabolism | Mycelium - growth & development | Soil - chemistry | Agaricus - enzymology | Agaricus - physiology | Cellulose - metabolism | Physiological aspects | Polysaccharides | Genetic aspects | Agaricus | Research | Residues | Laboratories | Genomics | Cellulose | Xylan | Genomes | Fruit bodies | Substitutes | Degradation | Fungi | Xylanase | Xylosidase | Physiology | Arabinofuranosidase | Saccharides | Carbohydrates | Enzymes | Cultivation | Mushrooms | Fragments | Substrates | Biological diversity | Xylose | Studies | Basidiocarps | Composting | Composts | h-1-nmr spectroscopy | mode | button mushroom | purification | oligosaccharides | wheat-flour arabinoxylan | aspergillus-awamori | enzyme-activities
Journal Article