1.21.3.3: reticuline oxidase
This is an abbreviated version!
For detailed information about reticuline oxidase, go to the full flat file.
Word Map on EC 1.21.3.3
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1.21.3.3
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poppy
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sanguinarine
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s-reticuline
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s-scoulerine
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papaver
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benzylisoquinoline
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somniferum
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opium
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benzophenanthridine
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codeinone
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cyp80b1
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eschscholtzia
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papaveraceae
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vanillyl
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flavinylated
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3\'-hydroxylase
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s-norcoclaurine
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synthesis
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medicine
- 1.21.3.3
- poppy
- sanguinarine
-
s-reticuline
-
s-scoulerine
- papaver
-
benzylisoquinoline
- somniferum
-
opium
-
benzophenanthridine
- codeinone
- cyp80b1
-
eschscholtzia
- papaveraceae
-
vanillyl
-
flavinylated
-
3\'-hydroxylase
-
s-norcoclaurine
- synthesis
- medicine
Reaction
Synonyms
(S)-reticuline oxidase, BBE, BBE-like 13, BBE-like 15, BBE-like 28, BBE1, BBL, berberine bridge enzyme, berberine bridge enzyme-like, berberine bridge enzyme-like 28, berberine bridge-forming enzyme, berberine-bridge-forming enzyme, EC 1.5.3.9, flavin-dependent oxidase, monolignol oxidoreductase, reticuline oxidase, tetrahydroprotoberberine synthase
ECTree
1.21.3.3 reticuline oxidaseAdvanced search results
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results (Engineering
Engineering on EC 1.21.3.3 - reticuline oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C166A
E417Q
H104A
mutant, lacking one of the covalent linkages to the cofactor FAD
H174A
mutation leads to substantial changes in all kinetic parameters and a decrease in midpoint potential. The crystal structure of the variant shows significant structural rearrangements compared to wild-type enzyme
H459A
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mutant, based on structural information, His459 do not directly interact with the substrate, bicovalent flavin linkage is not affected by the mutation
Y106F
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mutant, based on structural information, Tyr106 do not directly interact with the substrate, bicovalent flavin linkage is not affected by the mutation
additional information
C166A
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site-directed mutagenesis, the mutant protein still has residual activity, but reduced to about 6% of the turnover rate observed for wild-type berberine bridge enzyme, the reductive half-reaction is greatly influenced by the lack of the 6-S-cysteinyl linkage, resulting in a 370fold decrease in the rate of flavin reduction
C166A
mutant, lacking one of the covalent linkages to the cofactor FAD
E417Q
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mutant, based on structural information, Glu417 essential amino acid for substrate oxidation, bicovalent flavin linkage is not affected by the mutation
E417Q
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solvent isotope effects on kred are equal to 1 for both wild-type and the E417Q mutant, indicating that solvent exchangeable protons are not in flight during or before flavin reduction, thus eliminating a fully concerted mechanism
additional information
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knockdown of berberine bridge enzyme by RNAi via Agrobacterium tumefaciens transfection leads to accumulation of (S)-reticuline and activates a silent pathway in cultured California poppy cells, they also produced a methylated derivative of reticuline, laudanine, which can scarcely be detected in control cells, analysis of reticuline metabolites, overview
additional information
recombinant coexpression of seven enzymes, including the three membrane-bound enzymes: the flavin-dependent oxidase berberine bridge enzyme, the cytochrome P450 canadine synthase, and a cytochrome P450 reductase, in Saccharomyces cerevisiae results in protoberberine alkaloid production from a simple benzylisoquinoline alkaloid precursor rac-norlaudanosoline. Improvement of flux through the pathway, by methods including enzyme variant screening, genetic copy number variation, and culture optimization, leading to an over 70fold increase in canadine titer up to 1.8 mg/l
