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Information on EC 1.21.3.3 - reticuline oxidase and Organism(s) Eschscholzia californica and UniProt Accession P30986
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1.21.3.3 reticuline oxidaseIUBMB Comments
Contains FAD. The enzyme from the plant Eschscholtzia californica binds the cofactor covalently . Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge ('berberine bridge') of (S)-tetrahydroprotoberberines. The product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants.
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Word Map
- 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
The taxonomic range for the selected organisms is: Eschscholzia californica
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
berberine bridge enzyme, berberine bridge enzyme-like, flavin-dependent oxidase, reticuline oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BBE
berberine bridge enzyme
berberine-bridge-forming enzyme
-
-
-
-
tetrahydroprotoberberine synthase
-
-
-
-
BBE
-
-
-
-
berberine bridge enzyme
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming)
Contains FAD. The enzyme from the plant Eschscholtzia californica binds the cofactor covalently [3]. Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge ('berberine bridge') of (S)-tetrahydroprotoberberines. The product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants.
CAS REGISTRY NUMBER
COMMENTARY
152232-28-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(2-fluoro-3-hydroxybenzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol + O2
(13aS)-12-fluoro-3-methoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-2,11-diol + H2O
-
49% conversion, more than 99% of product (13aS)-12-fluoro-3-methoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-2,11-diol
-
?
1-(2-fluoro-3-hydroxybenzyl)-7-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-6-ol + O2
(13aS)-12-fluoro-2-methoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-3,11-diol + H2O
-
49% conversion, more than 99% of product (13aS)-12-fluoro-2-methoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-3,11-diol
-
?
1-(3-hydroxy-4-methoxybenzyl)-7-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-6-ol + O2
(13aS)-2,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-3,9-diol + isocoreximine + H2O2
-
53% conversion, ratio (13aS)-2,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-3,9-diol to isocoreximine is 98:2
-
?
1-(3-hydroxybenzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol + O2
(13aS)-3-methoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-2,9-diol + (1R)-1-(3-hydroxybenzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol + H2O2
-
reaction leads to the (S)-enantiomer of the product and enantiomerically pure (R)-substrate. 22% yield of (13aS)-3-methoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinoline-2,9-diol in more than 97% enantiomeric excess, 549% yield of + (1R)-1-(3-hydroxybenzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-olin more than 97% enantiomeric excess
-
?
3-[(2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl)methyl]phenol + O2
(13aS)-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinolin-9-ol + 3-[[(1R)-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl]phenol + H2O2
-
reaction leads to the (S)-enantiomer of the product and enantiomerically pure (R)-substrate. 46% yield of (13aS)-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinolin-9-ol in more than 97% enantiomeric excess, 49% yield of + 3-[[(1R)-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl]phenol in more than 97% enantiomeric excess
-
?
3-[(6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl)methyl]-2-fluorophenol + O2
(13aS)-12-fluoro-2,3-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinolin-11-ol + H2O
-
48% conversion, more than 99% of product (13aS)-12-fluoro-2,3-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinolin-11-ol
-
?
3-[(6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl)methyl]phenol + O2
(13aS)-2,3-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinolin-9-ol + 3-[[(1R)-6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl]phenol + H2O2
-
reaction leads to the (S)-enantiomer of the product and enantiomerically pure (R)-substrate. 42% yield of (13aS)-2,3-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquinolino[3,2-a]isoquinolin-9-ol in more than 97% enantiomeric excess, 50% yield of + 3-[[(1R)-6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl]phenol in more than 97% enantiomeric excess
-
?
reticuline + O2
(S)-scoulerine + (S)-coreximine + H2O2
-
50% conversion, ratio (S)-scoulerine to (S)-coreximine is >99 to <1
-
?
(R,S)-laudanosoline + O2
? + H2O2
-
specific for the (S)-enantiomer
-
-
?
(S)-coreximine + O2
(13aS)-2,11-dihydroxy-3,10-dimethoxy-5,8,13,13a-tetrahydroisoquinolino[3,2-a]isoquinolin-7-ium + H2O2
-
-
-
-
?
1-[(4-chlorophenyl)methyl]-2-ethyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + O2
(1S)-1-[(4-chlorophenyl)methyl]-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + (1R)-1-[(4-chlorophenyl)methyl]-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + H2O2
-
-
-
-
?
2-ethyl-6,7-dimethoxy-1-[(3-methoxyphenyl)methyl]-1,2,3,4-tetrahydroisoquinoline + O2
(1S)-6,7-dimethoxy-1-[(3-methoxyphenyl)methyl]-1,2,3,4-tetrahydroisoquinoline + (1R)-6,7-dimethoxy-1-[(3-methoxyphenyl)methyl]-1,2,3,4-tetrahydroisoquinoline + H2O2
-
-
-
-
?
2-ethyl-6,7-dimethoxy-1-[(4-methoxyphenyl)methyl]-1,2,3,4-tetrahydroisoquinoline + O2
(1S)-6,7-dimethoxy-1-[(4-methoxyphenyl)methyl]-1,2,3,4-tetrahydroisoquinoline + (1R)-2-ethyl-6,7-dimethoxy-1-[(4-methoxyphenyl)methyl]-1,2,3,4-tetrahydroisoquinoline + H2O2
-
-
-
-
?
3-[(2-ethyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinolin-1-yl)methyl]phenol + O2
3-[[(1S)-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl]phenol + 3-[[(1R)-2-ethyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl]phenol + H2O2
-
-
-
-
?
6,7-dimethoxy-2-methyl-1,2,3,4-tetrahydroisoquinoline + H2O2
? + O2
-
-
-
-
?
6-ethyl-5-[(4-methoxyphenyl)methyl]-5,6,7,8-tetrahydro-2H-[1,3]dioxolo[4,5-g]isoquinoline + O2
(5S)-5-[(4-methoxyphenyl)methyl]-5,6,7,8-tetrahydro-2H-[1,3]dioxolo[4,5-g]isoquinoline + (5R)-5-[(4-methoxyphenyl)methyl]-5,6,7,8-tetrahydro-2H-[1,3]dioxolo[4,5-g]isoquinoline + H2O2
-
-
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
highest activity
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
(S)-scoulerine is further oxidized to dehydroscoulerine in a second oxidation step
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
-
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
first step of benzophenanthridine alkaloid biosynthesis
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
first step of isoquinoline and benzophenanthridine alkaloid biosynthesis, involved in sanguinarine pathway
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
the enzyme is involved in the biosynthetic pathway for benzophenanthridine alkaloids in California poppy, Eschscholzia californica, cells, related alkaloids, overview
-
-
?
additional information
?
-
enzyme employs an enantioselective oxidative C-C bond formation
-
-
?
additional information
?
-
-
C-H bond cleavage is rate-limiting during flavin reduction. Solvent isotope effects on kred indicate that solvent exchangeable protons are not in flight during or before flavin reduction, thus eliminating a fully concerted mechanism. Deprotonation is not occurring before or during C-H bond cleavage, and a hydroxyl group must be present at C3 for cyclization. This could be due to the methoxy group being less electron-donating than a hydroxyl substituent or to disruption of the interaction between the glutamate and the substrate, causing altered binding. A concerted attack of a methyl amine by the C2-atom and hydride transfer is less likely than attack on a methylene iminium ion intermediate by the C2-atom, indicating that a stepwise mechanism is the likely mechanism
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
-
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
first step of benzophenanthridine alkaloid biosynthesis
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
first step of isoquinoline and benzophenanthridine alkaloid biosynthesis, involved in sanguinarine pathway
-
-
?
(S)-reticuline + O2
(S)-scoulerine + H2O2
-
the enzyme is involved in the biosynthetic pathway for benzophenanthridine alkaloids in California poppy, Eschscholzia californica, cells, related alkaloids, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
covalently attached to enzyme at 8alpha position to H104 and also at 6 position to thiol group of C166. anaerobic photoirradiation leads to cleavage of the linkage to C166 yielding 6-mercaptoflavin and a peptide with C replaced by A due to breakage of the C-S bond
FAD
-
residues His104 and Cys166, which are involved in the bi-covalent attachment of FAD to berberine bridge enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetic analysis, and redox potentials for both wild type and C166A mutant enzyme are +132 mV and +53 mV, respectively, rapid reaction stopped-flow experiments, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RETO_ESCCA
538
0
59958
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
three potential N-glycosylation sites, one at the N-terminus, N38, and two at the C-terminus, Asn-423 and Asn-471
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the H174A variant shows significant structural rearrangements compared to wild-type enzyme. Residue H174 is part of a hydrogen bonding network that stabilizes the negative charge at the N1/C2=O locus via interaction with the hydroxyl group at C2 of the ribityl side chain of the flavin cofactor
the crystal structure of Berberine bridge enzyme in complex with dehydroscoulerine is determined to 1.63 A resolution
the crystal structures of the mutants H104A, C166A, C166A in complex with (S)-reticuline and of the wild-type enzyme in complex with (S)-scoulerine are determined
the crystal structures of berberine bridge enzyme in two different crystal forms, monoclinic and tetragonal, and in complex with (S)-reticuline are determined
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C166A
mutant, lacking one of the covalent linkages to the cofactor FAD
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
C166A
-
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
E417Q
H459A
-
mutant, based on structural information, His459 do not directly interact with the substrate, bicovalent flavin linkage is not affected by the mutation
Y106F
-
mutant, based on structural information, Tyr106 do not directly interact with the substrate, bicovalent flavin linkage is not affected by the mutation
additional information
-
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
E417Q
-
mutant, based on structural information, Glu417 essential amino acid for substrate oxidation, bicovalent flavin linkage is not affected by the mutation
E417Q
-
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
toluene
reaction can be performed in 70% v/v toluene, allowing a substrate concentration of at least 20 g/l
additional information
enzyme tolerates a variety of organic solvents
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the secreted enzymes are purified by gel filtration and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for co-overexpression with disulfide isomerase in Pichia pastoris cells, for cloning of wild-type BBE, the mutant H104A and mutant H104A-C166A the vector pPICZalpha is used
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
substrate tuning by introducing a fluoro moiety at one potential reactive carbon center switches the reaction to the formation of exclusively one regioisomer with perfect enantioselectivity. The formation of 11-hydroxy-functionalized tetrahydroprotoberberines instead of the commonly formed 9-hydroxy-functionalized products from 1,2,3,4-tetrahydroisoquinolines can be successfully promoted
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hauschild, K.; Pauli, H.H.; Kutchan, T.M.
Isolation and analysis of a gene bbe1 encoding the berberine bridge enzyme from the California poppy Eschscholzia californica
Plant Mol. Biol.
36
473-478
1998
Eschscholzia californica
Kutchan, T.M.; Dittrich, H.
Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants
J. Biol. Chem.
270
24475-24481
1995
Eschscholzia californica
Kutchan, T.M.; Bock, A.; Dittrich, H.
Heterologous expression of the plant proteins strictosidine synthase and berberine bridge enzyme in insect cell culture
Phytochemistry
35
353-360
1994
Eschscholzia californica
Weid, M.; Ziegler, J.; Kutchan, T.M.
The roles of latex and the vascular bundle in morphine biosynthesis in the opium poppy, Papaver somniferum
Proc. Natl. Acad. Sci. USA
101
13957-13962
2004
Eschscholzia californica, Papaver somniferum
Park, S.U.; Yu, M.; Facchini, P.J.
Modulation of berberine bridge enzyme levels in transgenic root cultures of California poppy alters the accumulation of benzophenanthridine alkaloids
Plant Mol. Biol.
51
153-164
2003
Eschscholzia californica, Papaver somniferum
Winkler, A.; Hartner, F.; Kutchan, T.M.; Glieder, A.; Macheroux, P.
Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor
J. Biol. Chem.
281
21276-21285
2006
Eschscholzia californica
Winkler, A.; Kutchan, T.M.; Macheroux, P.
6-S-cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity
J. Biol. Chem.
282
24437-24443
2007
Eschscholzia californica
Fujii, N.; Inui, T.; Iwasa, K.; Morishige, T.; Sato, F.
Knockdown of berberine bridge enzyme by RNAi accumulates (S)-reticuline and activates a silent pathway in cultured California poppy cells
Transgenic Res.
16
363-375
2007
Eschscholzia californica
Winkler, A.; Motz, K.; Riedl, S.; Puhl, M.; Macheroux, P.; Gruber, K.
Structural and mechanistic studies reveal the functional role of bicovalent flavinylation in berberine bridge enzyme
J. Biol. Chem.
284
19993-20001
2009
Eschscholzia californica (P30986)
Winkler, A.; Lyskowski, A.; Riedl, S.; Puhl, M.; Kutchan, T.M.; Macheroux, P.; Gruber, K.
A concerted mechanism for berberine bridge enzyme
Nat. Chem. Biol.
4
739-741
2008
Eschscholzia californica
Winkler, A.; Puhl, M.; Weber, H.; Kutchan, T.M.; Gruber, K.; Macheroux, P.
Berberine bridge enzyme catalyzes the six electron oxidation of (S)-reticuline to dehydroscoulerine
Phytochemistry
70
1092-1097
2009
Eschscholzia californica (P30986)
Resch, V.; Schrittwieser, J.; Wallner, S.; MacHeroux, P.; Kroutil, W.
Biocatalytic oxidative C-C bond formation catalysed by the berberine bridge enzyme: Optimal reaction conditions
Adv. Synth. Catal.
353
2377-2383
2011
Eschscholzia californica (P30986)
-
Wallner, S.; Winkler, A.; Riedl, S.; Dully, C.; Horvath, S.; Gruber, K.; Macheroux, P.
Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme
Biochemistry
51
6139-6147
2012
Eschscholzia californica (P30986)
Gaweska, H.M.; Roberts, K.M.; Fitzpatrick, P.F.
Isotope effects suggest a stepwise mechanism for berberine bridge enzyme
Biochemistry
51
7342-7347
2012
Eschscholzia californica
Resch, V.; Lechner, H.; Schrittwieser, J.H.; Wallner, S.; Gruber, K.; Macheroux, P.; Kroutil, W.
Inverting the regioselectivity of the berberine bridge enzyme by employing customized fluorine-containing substrates
Chemistry
18
13173-13179
2012
Eschscholzia californica (P30986)
Schrittwieser, J.H.; Resch, V.; Wallner, S.; Lienhart, W.D.; Sattler, J.H.; Resch, J.; Macheroux, P.; Kroutil, W.
Biocatalytic organic synthesis of optically pure (S)-scoulerine and berbine and benzylisoquinoline alkaloids
J. Org. Chem.
76
6703-6714
2011
Eschscholzia californica (P30986)
Gandomkar, S.; Fischereder, E.M.; Schrittwieser, J.H.; Wallner, S.; Habibi, Z.; Macheroux, P.; Kroutil, W.
Enantioselective oxidative aerobic dealkylation of N-ethyl benzylisoquinolines by employing the berberine bridge enzyme
Angew. Chem. Int. Ed. Engl.
54
15051-15054
2015
Eschscholzia californica
Daniel, B.; Konrad, B.; Toplak, M.; Lahham, M.; Messenlehner, J.; Winkler, A.; Macheroux, P.
The family of berberine bridge enzyme-like enzymes A treasure-trove of oxidative reactions
Arch. Biochem. Biophys.
632
88-103
2017
Eschscholzia californica (P30986), Eschscholzia californica
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