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lytic polysaccharide monooxygenase (115) 115
cellulose (114) 114
index medicus (111) 111
enzymes (110) 110
lytic polysaccharide monooxygenases (83) 83
biotechnology & applied microbiology (67) 67
biochemistry & molecular biology (66) 66
polysaccharides (66) 66
degradation (63) 63
biomass (58) 58
hydrolysis (53) 53
lignocellulose (45) 45
biotechnology (42) 42
cellobiose dehydrogenase (41) 41
mixed function oxygenases - metabolism (41) 41
monooxygenase (39) 39
fungi (38) 38
cellulase (37) 37
chitin (37) 37
analysis (33) 33
mixed function oxygenases - chemistry (32) 32
proteins (32) 32
research (31) 31
energy & fuels (30) 30
glycoside hydrolase family (30) 30
oxidation (30) 30
microbiology (28) 28
cellulose - metabolism (27) 27
monooxygenases (27) 27
oxidation-reduction (27) 27
cellulose degradation (26) 26
lpmo (26) 26
binding (25) 25
life sciences (25) 25
biomass energy (24) 24
cleavage (24) 24
neurospora-crassa (24) 24
polysaccharides - metabolism (24) 24
substrate specificity (24) 24
crystal-structure (23) 23
enzymatic-hydrolysis (23) 23
serratia-marcescens (22) 22
biomasse (21) 21
lignin (21) 21
biofuels (20) 20
copper (20) 20
functional-characterization (20) 20
biodegradation (19) 19
biophysics (19) 19
hydrogen peroxide (18) 18
oxidative cleavage (18) 18
mixed function oxygenases - genetics (17) 17
physiological aspects (17) 17
substrates (17) 17
usage (17) 17
aa9 (16) 16
carbohydrates (16) 16
catalysis (16) 16
discovery (16) 16
family (16) 16
fuel (16) 16
lignocellulosic biomass (16) 16
protein (16) 16
saccharification (16) 16
trichoderma-reesei (16) 16
bacteria (15) 15
binding protein cbp21 (15) 15
catalytic domain (15) 15
cellulases (15) 15
cellulose - chemistry (15) 15
fungal proteins - metabolism (15) 15
lignocelluloses (15) 15
models, molecular (15) 15
organic chemistry (15) 15
conversion (14) 14
lignin - metabolism (14) 14
oligosaccharides (14) 14
bacterial proteins - chemistry (13) 13
biochemical research methods (13) 13
chemistry, applied (13) 13
genomes (13) 13
oxidases (13) 13
xylan (13) 13
aa10 (12) 12
activation (12) 12
chemistry, multidisciplinary (12) 12
chemistry, organic (12) 12
chitin - chemistry (12) 12
chitinase (12) 12
crystallography (12) 12
enzym (12) 12
enzymology (12) 12
fungal proteins - genetics (12) 12
gene expression (12) 12
glycoside hydrolase (12) 12
oxidative-degradation (12) 12
pichia-pastoris (12) 12
polysaccharid (12) 12
amino acid sequence (11) 11
biofuel (11) 11
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1. Full Text Lytic Polysaccharide Monooxygenases in Biomass Conversion
by Hemsworth, Glyn R and Johnston, Esther M and Davies, Gideon J and Walton, Paul H
Trends in Biotechnology, ISSN 0167-7799, 2015, Volume 33, Issue 12, pp. 747 - 761
The derivation of second-generation biofuels from non-edible biomass is viewed as crucial for establishing a sustainable bio-based economy for the future. The... 
Internal Medicine | biomass conversion | starch | lytic polysaccharide monooxygenase | lignocellulose | chitin | Chitin | Lignocellulose | Biomass conversion | Starch | Lytic polysaccharide monooxygenase | SUBSTRATE-SPECIFICITY | CELLOBIOSE DEHYDROGENASE | STRUCTURAL BASIS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PODOSPORA-ANSERINA | OXIDATIVE CELLULOSE DEGRADATION | FUNGUS PHANEROCHAETE-CHRYSOSPORIUM | CARBOHYDRATE-ACTIVE ENZYMES | BINDING PROTEIN CBP21 | SERRATIA-MARCESCENS | NEUROSPORA-CRASSA | Biotechnology - methods | Biotechnology - trends | Biotransformation | Mixed Function Oxygenases - metabolism | Biomass | Biofuels | Polysaccharides - metabolism | Enzymes | Biomass energy | Polysaccharides | Deconstruction | Lignin | Microorganisms | Algae | Cellulose | Oxidation | Fermentation
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2. Full Text A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides
by Isaksen, Trine and Westereng, Bjørge and Aachmann, Finn L and Agger, Jane W and Kracher, Daniel and Kittl, Roman and Ludwig, Roland and Haltrich, Dietmar and Eijsink, Vincent G. H and Horn, Svein J
Journal of Biological Chemistry, ISSN 0021-9258, 01/2014, Volume 289, Issue 5, pp. 2632 - 2642
Background: Lytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that cleave polysaccharides. Results: We describe a novel LPMO and use... 
OXIDATION | AA10 | CBM33 | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | Mass Spectrometry (MS) | Biofuel | Metalloenzymes | CLEAVAGE | DEHYDROGENASE | NMR | NOMENCLATURE | Cellulase | ENZYMES | AA9 | PICHIA-PASTORIS | DEGRADATION | Lytic Polysaccharide Monooxygenase (LPMO) | GH61 | BINDING | Neurospora crassa - enzymology | Carbon - metabolism | Oxidation-Reduction | Mass Spectrometry | Mixed Function Oxygenases - metabolism | Neurospora crassa - metabolism | Oligosaccharides - metabolism | Biofuels - microbiology | Oxygen - metabolism | Cellulose - metabolism | Polysaccharides - metabolism | Enzymology
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3. Full Text Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency
by Eibinger, Manuel and Ganner, Thomas and Bubner, Patricia and Rošker, Stephanie and Kracher, Daniel and Haltrich, Dietmar and Ludwig, Rol and Plank, Harald and Nidetzky, Bernd
Journal of Biological Chemistry, ISSN 0021-9258, 12/2014, Volume 289, Issue 52, pp. 35929 - 35938
Lytic polysaccharide monooxygenase (LPMO) represents a unique principle of oxidative degradation of recalcitrant insoluble polysaccharides. Used in combination... 
LIGNOCELLULOSIC BIOMASS | ATOMIC-FORCE MICROSCOPY | CELLOBIOSE DEHYDROGENASE | STRUCTURAL-DYNAMICS | ENZYMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENZYMATIC-HYDROLYSIS | PICHIA-PASTORIS | IN-SITU-OBSERVATION | NEUROSPORA-CRASSA | NATIVE CELLULOSE | Fungal Proteins - chemistry | Hydrolysis | Neurospora crassa - enzymology | Cellulose - chemistry | Oxidation-Reduction | Cellulase | Surface Properties | Mixed Function Oxygenases - chemistry | Copper Monooxygenase | Atomic Force Microscopy (AFM) | Cellulose | GH61-AA9 | Biofuel | Synergy | Lytic Polysaccharide Monooxygenase (LPMO) | Enzymology | Oxidative Cellulose Surface Degradation
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4. Chitin-Active Lytic Polysaccharide Monooxygenases
by Courtade, G and Aachmann, FL
2019, Advances in Experimental Medicine and Biology, Volume 1142, 15
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the cleavage of 1,4-glycosidic bonds various plant cell wall... 
Crystalline polysaccharides | MEDICINE, RESEARCH & EXPERIMENTAL | DOMAIN | GLYCOSIDE HYDROLASE FAMILY | BIOCHEMISTRY & MOLECULAR BIOLOGY | Copper-dependent enzymes | FUNCTIONAL-CHARACTERIZATION | SERRATIA-MARCESCENS | Lytic polysaccharide monooxygenase (LPMO) | DISCOVERY | CELLOBIOSE DEHYDROGENASE | CARBOHYDRATE-BINDING MODULES | BIOLOGY | DEGRADATION | OXIDATIVE CLEAVAGE | CELLULOSE
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5. Full Text Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase
by Gaston Courtade and Reinhard Wimmer and Åsmund K. Røhr and Marita Preims and Alfons K. G. Felice and Maria Dimarogona and Gustav Vaaje-Kolstad and Morten Sørlie and Mats Sandgren and Roland Ludwig and Vincent G. H. Eijsink and Finn Lillelund Aachmann and Sveriges lantbruksuniversitet
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2016, Volume 113, Issue 21, pp. 5922 - 5927
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds using molecular oxygen and an... 
Cellobiose dehydrogenase | Xyloglucan | LPMO | Cellulose | Lytic polysaccharide monooxygenase | BACKBONE DYNAMICS | PROTEIN | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | xyloglucan | OXIDATIVE CELLULOSE DEGRADATION | CLEAVAGE | DISCOVERY | cellobiose dehydrogenase | cellulose | STRUCTURAL BASIS | ENZYMES | lytic polysaccharide monooxygenase | BINDING | NEUROSPORA-CRASSA | Fungal Proteins - chemistry | Neurospora crassa - enzymology | Copper - chemistry | Neurospora crassa - genetics | Nuclear Magnetic Resonance, Biomolecular | Substrate Specificity | Mixed Function Oxygenases - chemistry | Fungal Proteins - genetics | Mixed Function Oxygenases - genetics | Binding Sites | Carbohydrate Dehydrogenases - chemistry | Carbohydrate Dehydrogenases - genetics | Biological Sciences | Biofysik | Analytical Chemistry | Biokemi och molekylärbiologi | Structural Biology | Strukturbiologi | Biochemistry and Molecular Biology | Biophysics | Analytisk kemi
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6. Full Text Insecticidal fern protein Tma12 is possibly a lytic polysaccharide monooxygenase
by Yadav, SK and Archana and Singh, R and Singh, PK and Vasudev, PG
PLANTA, ISSN 0032-0935, 06/2019, Volume 249, Issue 6, pp. 1987 - 1996
Main conclusionAmino acid sequence and crystal structure analyses of Tma12, an insecticidal protein isolated from the fern Tectaria macrodonta, identify it as... 
DETERMINANTS | FUNCTIONAL-CHARACTERIZATION | VIRULENCE | CELLULOSE DEGRADATION | Tectaria macrodonta | PLANT SCIENCES | Carbohydrate-binding | STRUCTURAL BASIS | Lytic polysaccharide monooxygenase | CHITIN | PLANTS | Fern | Tma12 | OXIDATIVE CLEAVAGE | Crystal structure | INSIGHTS | Insecticides - pharmacology | Amino Acid Sequence | Hemiptera - drug effects | Gossypium - enzymology | Receptors, Cell Surface - metabolism | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Hydrogen Peroxide - metabolism | Polysaccharides - metabolism | Plant Proteins - genetics | Ferns - genetics | Gossypium - physiology | Sequence Alignment | Animals | Ferns - enzymology | Insecticides - metabolism | Plant Proteins - chemistry | Gossypium - genetics | Plants, Genetically Modified | Receptors, Cell Surface - chemistry | Plant Proteins - metabolism | Mixed Function Oxygenases - genetics | Ferns - chemistry | Receptors, Cell Surface - genetics | Enzymes | Plant genetics | Crystals | Amino acids | Virus diseases | Polysaccharides | Genetically modified crops | Analysis | Medicine, Botanic | Genetic engineering | Aleyrodidae | Medicine, Herbal | Molecular biology | Structure | Protein binding | Carbohydrates | Hydrogen peroxide | Streptomyces coelicolor | Viral diseases | Transgenic | Amino acid sequence | Exploration | Cotton | Monooxygenase | Proteins | Ferns | Microorganisms | Insecticide resistance | Acids | Structure-function relationships
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7. Full Text A fast and sensitive activity assay for lytic polysaccharide monooxygenase
by Breslmayr, Erik and Hanžek, Marija and Hanrahan, Aoife and Leitner, Christian and Kittl, Roman and Šantek, Božidar and Oostenbrink, Chris and Ludwig, Roland
Biotechnology for Biofuels, ISSN 1754-6834, 03/2018, Volume 11, Issue 1, pp. 79 - 13
Background: Lytic polysaccharide monooxygenases (LPMO) release a spectrum of cleavage products from their polymeric substrates cellulose, hemicellulose, or... 
2,6-Dimethoxyphenol | Hydrogen peroxide | Biomass degradation | Activity assay | Peroxidase activity | Lytic polysaccharide monooxygenase | FUNGI | SHOWS | ENERGY & FUELS | MANGANESE PEROXIDASE | CLEAVAGE | PRODUCTS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENZYMES | DEGRADATION | CELLULOSE | CELLO-OLIGOSACCHARIDES
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8. Full Text Recent insights into lytic polysaccharide monooxygenases (LPMOs)
by Tandrup, Tobias and Frandsen, Kristian E.H and Johansen, Katja S and Berrin, Jean-Guy and Leggio, Leila Lo
Biochemical Society Transactions, ISSN 0300-5127, 10/2018, Volume 46, Issue 6, pp. 1431 - 1447
Lytic polysaccharide monooxygenases (LPMOs) are copper enzymes discovered within the last 10 years. By degrading recalcitrant substrates oxidatively, these... 
ACTIVATION | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY | FUNCTIONAL-CHARACTERIZATION | LIGNOCELLULOSE | SERRATIA-MARCESCENS | OXIDATIVE CLEAVAGE | CELLULOSE | BINDING | NEUROSPORA-CRASSA | Chemical Sciences | Other
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9. Full Text A small lytic polysaccharide monooxygenase from Streptomyces griseus targeting α‐ and β‐chitin
by Nakagawa, Yuko S and Kudo, Madoka and Loose, Jennifer S. M and Ishikawa, Takahiro and Totani, Kazuhide and Eijsink, Vincent G. H and Vaaje‐Kolstad, Gustav
The FEBS Journal, ISSN 1742-464X, 03/2015, Volume 282, Issue 6, pp. 1065 - 1079
The lytic polysaccharide monooxygenases (LPMOs) have received considerable attention subsequent to their discovery because of their ability to boost the... 
AA10 | Streptomyces griseus | chitinase | lytic polysaccharide monooxygenases | chitin | Chitinase | Chitin | Streptomyces griseus | Lytic polysaccharide monooxygenases | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | Streptomycesgriseus | SERRATIA-MARCESCENS BJL200 | BINDING PROTEIN CBP21 | RECALCITRANT POLYSACCHARIDES | CELLULOSE DEGRADATION | PROCESSIVITY | CELLOBIOSE DEHYDROGENASE | SUBSTRATE | ENZYMES | PROVIDES INSIGHT | Protein Structure, Tertiary | Genome, Bacterial | Mutagenesis, Site-Directed | Bacterial Proteins - chemistry | Recombinant Proteins - chemistry | Substrate Specificity | Tryptophan - chemistry | Chitin - chemistry | Mixed Function Oxygenases - chemistry | Biomass | Phylogeny | Streptomyces griseus - enzymology | Brevibacillus - enzymology | Cellulose - chemistry | Cloning, Molecular | Oxygen - chemistry | Polysaccharides - chemistry | Protein Binding | Mutation | Binding Sites | Chitinases - chemistry
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10. Full Text The pyrroloquinolinequinone- dependent pyranose dehydrogenase from Coprinopsis cinerea drives lytic polysaccharide monooxygenase action
by Várnai, Anikó and Umezawa, Kiwamu and Yoshida, Makoto and Eijsink, Vincent G.H
Applied and Environmental Microbiology, ISSN 0099-2240, 06/2018, Volume 84, Issue 11
Carbohydrate-binding module | LPMO | Lytic polysaccharide monooxygenase | Electron transfer | AA9 | PQQ-dependent PDH | AA12
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11. Progress in lytic polysaccharide monooxygenase
by Sun, Xiaobao and Wan, Jiaxin and Cao, Jiawen and Si, Yuexiu and Wang, Qian
Shengwu Gongcheng Xuebao/Chinese Journal of Biotechnology, ISSN 1000-3061, 02/2018, Volume 34, Issue 2, pp. 177 - 187
Degradation | Lignocellulose | Lytic polysaccharide monooxygenase | Application | Glycoside hydrolase
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12. Full Text Targeting the reactive intermediate in polysaccharide monooxygenases
by Hedegård, Erik D and Ryde, Ulf and Lund University and Theoretical Chemistry and Teoretisk kemi and Lunds universitet
JBIC Journal of Biological Inorganic Chemistry, ISSN 0949-8257, 10/2017, Volume 22, Issue 7, pp. 1029 - 1037
Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism, making... 
Life Sciences | Biochemistry, general | Computational chemistry | Microbiology | Lytic polysaccharide monooxygenase | Reaction mechanism | Density functional theory | DIOXYGEN ACTIVATION | ENERGY | GLYCOSIDE HYDROLASE FAMILY | ACTIVE-SITE | THERMOCHEMISTRY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLEAVAGE | CELLULOSE DEGRADATION | CHEMISTRY, INORGANIC & NUCLEAR | COUPLED ELECTRON-TRANSFER | BASIS-SETS | INSIGHTS | Protons | Catalytic Domain | Models, Molecular | Crystallography, X-Ray | Lentinula - enzymology | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Polysaccharides - metabolism | Lentinula - metabolism | Thermodynamics | Lentinula - chemistry | Copper - chemistry | Copper - metabolism | Polysaccharides - chemistry | Hydroxides | Biomass energy | Analysis | Bonds | Cellulose | Density functionals | Metalloenzymes | Original Paper | Naturvetenskap | Kemi | Natural Sciences | Chemical Sciences
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13. Full Text Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability
by Kracher, Daniel and Andlar, Martina and Furtmüller, Paul G and Ludwig, Roland
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 5, pp. 1676 - 1687
Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-containing enzymes that oxidatively degrade insoluble plant polysaccharides and soluble... 
ACTIVATION | PROTEIN | polysaccharide | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROLYSIS | carbohydrate-binding protein | FUNCTIONAL-CHARACTERIZATION | INSIGHT | metalloenzyme | protein stability | CELLULOSE DEGRADATION | DISCOVERY | CELLOBIOSE DEHYDROGENASE | lytic polysaccharide monooxygenase | OXIDATIVE CLEAVAGE | plant cell wall | Active-site copper | NEUROSPORA-CRASSA | Enzymology
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14. Full Text Crystal structure and computational characterization of the lytic polysaccharide monooxygenase GH61D from the basidiomycota fungus Phanerochaete chrysosporium
by Wu, Miao and Beckham, Gregg T and Larsson, Anna M and Ishida, Takuya and Kim, Seonah and Payne, Christina M and Himmel, Michael E and Crowley, Michael F and Horn, Svein J and Westereng, Bjørge and Igarashi, Kiyohiko and Samejima, Masahiro and Ståhlberg, Jerry and Eijsink, Vincent G. H and Sandgren, Mats and Sveriges lantbruksuniversitet
Journal of Biological Chemistry, ISSN 0021-9258, 05/2013, Volume 288, Issue 18, pp. 12828 - 12839
Carbohydrate structures are modified and degraded in the biosphere by a myriad of mostly hydrolytic enzymes. Recently, lytic polysaccharide mono-oxygenases... 
LIGNOCELLULOSIC BIOMASS | GLYCOSIDE HYDROLASE FAMILY | CARBOHYDRATE-BINDING MODULE | CELLOBIOSE DEHYDROGENASE | ENZYMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | SEQUENCE | DEGRADATION | SERRATIA-MARCESCENS | CELLULOSE | Fungal Proteins - chemistry | Catalytic Domain | Cellobiose - chemistry | Copper - chemistry | Phanerochaete - enzymology | Copper - metabolism | Cellobiose - metabolism | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Fungal Proteins - metabolism | Carbohydrate-binding Protein | CBM33 | Lytic Polysaccharide Monooxygenase | Copper Monooxygenase | Molecular Dynamics | Glycoside Hydrolases | Structural Biology | Phanerochaete chrysosporium | Biofuel | Enzymology | GH61 | Biochemistry and Molecular Biology | Renewable Bioenergy Research | Förnyelsebar bioenergi | Biokemi och molekylärbiologi | Strukturbiologi
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15. Full Text The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation
by Courtade, Gaston and Forsberg, Zarah and Heggset, Ellinor B and Eijsink, Vincent G. H and Aachmann, Finn L and RISE - Research Institutes of Sweden and Bioekonomi and PFI
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 34, pp. 13006 - 13015
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of polysaccharides such as cellulose and chitin,... 
PROTEIN DYNAMICS | DOMAIN | CELLOBIOSE DEHYDROGENASE | NMR-SPECTROSCOPY | ENZYMES | SUBSTRATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMICAL-SHIFT | DEGRADATION | HYDROLYTIC EFFICIENCY | THERMOMONOSPORA-FUSCA | Catalytic Domain | Cellulose - chemistry | Oxidation-Reduction | Fungal Polysaccharides - metabolism | Models, Molecular | Streptomyces coelicolor - enzymology | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Protein Conformation | Mixed Function Oxygenases - chemistry | Fungal Polysaccharides - chemistry | Cellulose - metabolism | carbohydrate-active enzyme | Protein Structure and Folding | biotechnology | hydrolytic enzyme | cellulose | LPMO | carbohydrate-binding module | protein linker | copper monooxygenase | lytic polysaccharide monooxygenase | nanofibril | Naturvetenskap | Natural Sciences
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16. Full Text A rapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase
by Loose, Jennifer S.M and Forsberg, Zarah and Fraaije, Marco W and Eijsink, Vincent G.H and Vaaje-Kolstad, Gustav
FEBS Letters, ISSN 0014-5793, 09/2014, Volume 588, Issue 18, pp. 3435 - 3440
The discovery of the copper-dependent lytic polysaccharide monooxygenases (LPMOs) has revealed new territory for chemical and biochemical analysis. These... 
Colonization factor | AA10 | Vibrio cholerae | Lytic polysaccharide monooxygenase | AA9 | GbpA | AA11 | CHITOBIASE | MECHANISM | CLEAVAGE | CHITIN | DEGRADATION | PROVIDES INSIGHT | OXYGENASES | CELLULOSE | BINDING | NEUROSPORA-CRASSA | hydrophilic interaction chromatography | LPMO | ACN | COAA | auxiliary activities | chitooligosaccharide oxidase | degree of polymerization | chitooligosaccharide aldonic acid | acetonitrile | lytic polysaccharide monooxygenase | HILIC | ChitO | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | BIOPHYSICS | Reference Standards | Vibrio cholerae - enzymology | Enzyme Assays - standards | Oxidation-Reduction | Bacterial Proteins - chemistry | Chitin - chemistry | Fimbriae Proteins - chemistry | Mixed Function Oxygenases - chemistry | Oxidases | Polysaccharides | Cholera toxin
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