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biochemistry & molecular biology (24) 24
index medicus (20) 20
covalently attached fad (19) 19
covalently bound flavin (14) 14
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berberine bridge enzyme (9) 9
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amino acid sequence (8) 8
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-tetrahydroprotoberberine oxidase (2) 2
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FEBS JOURNAL, ISSN 1742-464X, 05/2018, Volume 285, Issue 10, pp. 1923 - 1943
The berberine bridge enzyme from the California poppy Eschscholziacalifornica (EcBBE) catalyzes the oxidative cyclization of (S)-reticuline to (S)-scoulerine,... 
MECHANISM | plant biochemistry | CRYSTAL-STRUCTURE | MOSS | BIOCHEMISTRY & MOLECULAR BIOLOGY | enzyme catalysis | MODEL | protein structure | COVALENTLY ATTACHED FAD | DEVELOPMENTAL PROGRESSION | PATENS | PLANTS | enzyme mechanism | EXPRESSION | flavin adenine dinucleotide | RNA PROTEIN TRANSFERASE
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2011, Volume 286, Issue 26, pp. 23533 - 23543
Journal Article
Biochemistry, ISSN 0006-2960, 12/2017, Volume 56, Issue 51, pp. 6677 - 6690
Journal Article
ChemCatChem, ISSN 1867-3880, 11/2018, Volume 10, Issue 21, pp. 4783 - 4804
Journal Article
Advanced Synthesis & Catalysis, ISSN 1615-4150, 09/2011, Volume 353, Issue 13, pp. 2377 - 2383
Berberine bridge enzyme (BBE) catalyses the oxidative formation of an intramolecular CC bond using (S)‐reticuline as the natural substrate to form... 
oxidation | enzyme catalysis | biotransformations | CC bond formation | alkaloids | C-C bond formation | COVALENTLY ATTACHED FAD | STABILITY | CHEMISTRY, ORGANIC | CHEMISTRY, APPLIED | DEHYDROGENASE
Journal Article
Journal Article
The FEBS Journal, ISSN 1742-464X, 08/2015, Volume 282, Issue 16, pp. 3060 - 3074
The ability of flavoenzymes to reduce dioxygen varies greatly, and is controlled by the protein environment, which may cause either a rapid reaction (oxidases)... 
oxidase | enzyme design | oxyanion hole | dehydrogenase | oxygen reactivity | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | FLAVOPROTEIN OXIDASES | REACTIVITY | 3-DIMENSIONAL STRUCTURE | COVALENTLY ATTACHED FAD | OXIDATIVE HALF-REACTION | OXYGEN ACTIVATION SITE | AMINO-ACID OXIDASE | INTERMEDIATE | BINDING | Oxidoreductases, N-Demethylating - genetics | Allosteric Regulation | Molecular Sequence Data | Crystallography, X-Ray | Poaceae - genetics | Pollen - immunology | Oxygen - metabolism | Alcohol Oxidoreductases - genetics | Flavin-Adenine Dinucleotide - metabolism | Poaceae - enzymology | Oxygenases - metabolism | Plant Proteins - chemistry | Pollen - genetics | Allergens - chemistry | Protein Engineering | Plant Proteins - metabolism | Oxidoreductases, N-Demethylating - metabolism | Amino Acid Sequence | Poaceae - immunology | Mutagenesis, Site-Directed | Oxidation-Reduction | Catalytic Domain - genetics | Models, Molecular | Alcohol Oxidoreductases - metabolism | Allergens - genetics | Oxygenases - chemistry | Allergens - metabolism | Amino Acid Motifs | Oxidoreductases, N-Demethylating - chemistry | Sequence Homology, Amino Acid | Plant Proteins - genetics | Alcohol Oxidoreductases - chemistry | Pollen - enzymology | Kinetics | Oxygenases - genetics | Amino Acid Substitution | Flavins - metabolism | Oxidases | Glucose | Analysis | Dextrose | Bioengineering | Enzymes | Amino acids | Biophysics
Journal Article