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Information on EC 1.14.19.64 - (S)-stylopine synthase
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1.14.19.64 (S)-stylopine synthaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline.
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Word Map
- 1.14.19.64
- californica
-
eschscholzia
- sanguinarine
- coptis
- berberine
-
benzophenanthridine
- japonica
-
s-tetrahydrocolumbamine
-
s-scoulerine
- mexicana
- isoquinoline
- cyp80b1
-
argemone
- poppy
-
benzylisoquinoline
- majus
-
chelidonium
-
6-hydroxylase
- protopine
- papaveraceae
- pharmacology
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
stylopine synthase, cyp719a2, cyp719a3, methylenedioxy bridge-forming enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)
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-
-
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CYP719A2
EC 1.1.3.32
-
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formerly
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EC 1.14.21.1
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formerly
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stylopine synthase
synthase, (S)-stylopine
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2 = (S)-stylopine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
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reduction
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-
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(S)-cheilanthifoline,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)
A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline.
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CAS REGISTRY NUMBER
COMMENTARY
138791-29-4
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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
(R,S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(R,S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
-
?
(R,S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
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both CYP719A2 and CYP719A3 have stylopine synthase activity to catalyze methylenedioxy bridge-formation from cheilanthifoline to stylopine, but not cheilanthifoline synthase activity to convert scoulerine to cheilanthifoline, overview
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-
?
(R,S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-nandinine + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
-
r
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
(S)-coreximine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
kcat (S)-coreximine: 1% compared to kcat (S)-cheilanthifoline: 100%
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-
?
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-nandinine + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
-
?
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
?
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CYP719A3
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-
?
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
nandinine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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-
-
?
(S)-tetrahydrocolumbamine + [reduced NADPH-hemoprotein reductase] + O2
(S)-tetrahydroberberine + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
-
?
(S)-tetrahydrocolumbamine + [reduced NADPH-hemoprotein reductase] + O2
?
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CYP719A3
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-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
the enzyme is involved in biosynthesis of stylopine
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-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
high substrate specificity. The only alternative substrate identified is scoulerine, which is converted by stylopine synthase to yield minor amounts of nandinine
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-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
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NADPH is essential for activity, NADH displays only 0.5% turnover of that of NADPH
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?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
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enzyme is induced 20 h after challenging the cell suspension culture with elicitor
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?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
stylopine biosynthesis involves the sequential formation of two methylenedioxy bridges, (S)-stylopine is an important intermediate in the biosynthesis of benzophenanthridine alkaloids, such as sanguinarine
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-
?
additional information
?
-
-
the methylenedioxy bridge-forming enzyme is involved in stylopine biosynthesis in Eschscholzia californica, biosynthetic pathway for a variety of isoquinoline alkaloids, overview
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?
additional information
?
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CYP719A2 has high substrate affinity only toward (R,S)-cheilanthifoline, whereas CYP719A3 has high affinity toward the three similar substrates (R,S)-cheilanthifoline, (S)-scoulerine, and (S)-tetrahydrocolumbamine, both show no activity with columbamine, (R,S)-reticuline, (R,S)-norreticuline, (S)-N-methylcoclaurine, (S)-coclaurine, (R,S)-6-O-methylnorlaudanosoline, and magnoflorine, overview
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-
?
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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
(R,S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(R,S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
the enzyme is involved in biosynthesis of stylopine
-
-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
(S)-tetrahydrocolumbamine + [reduced NADPH-hemoprotein reductase] + O2
(S)-tetrahydroberberine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
-
the methylenedioxy bridge-forming enzyme is involved in stylopine biosynthesis in Eschscholzia californica, biosynthetic pathway for a variety of isoquinoline alkaloids, overview
-
-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme is induced 20 h after challenging the cell suspension culture with elicitor
-
?
(S)-cheilanthifoline + [reduced NADPH-hemoprotein reductase] + O2
(S)-stylopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
stylopine biosynthesis involves the sequential formation of two methylenedioxy bridges, (S)-stylopine is an important intermediate in the biosynthesis of benzophenanthridine alkaloids, such as sanguinarine
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome P450
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the enzyme is a cytochrome P450 dependent monooxygenase
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FAD
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0.004 mM, together with the optimal concentration of NADPH, 0.2 mM, enhances activity by 50%
FMN
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0.004 mM, together with the optimal concentration of NADPH, 0.2 mM, enhances activity by 50%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kcat (S)-coreximine: 1% compared to kcat (S)-cheilanthifoline: 100%
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additional information
additional information
-
kcat (S)-coreximine: 1% compared to kcat (S)-cheilanthifoline: 100%
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000045
-
CYP719A3 variant, (S)-scoulerine as substrate, microsomal protein used for determination
additional information
additional information
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0.43 pmol/min/pmol P450 for the CYP719A2 variant, (R,S)-scoulerine as substrate
additional information
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CYP719A2 variant uses only (R,S)-cheilanthifoline as substrate to produce stylopine when incubating with a mixture of 0.4 microM (R,S)-cheilanthifoline and 0.4 microM S-scoulerine as substrates
additional information
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CYP719A3 and CYP719A2 do not react with columbamine, (R,S)-reticuline, (R,S)-norreticuline, (S)-N-methylcoclaurine, (S)-coclaurine, (R,S)-6-O-methylnorlaudanosoline and magnoflorine to make corresponding products with a methylenedioxy bridge
additional information
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CYP719A3 but not CYP719A2 variant converts (S)-tetrahydrocolumbamine to (S)-tetrahydroberberine
additional information
-
CYP719A3 converts a mixture of 0.4 microM (R,S)-cheilanthifoline and 0.4 microM S-scoulerine as substrates to stylopine and nandinine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
half optimal activity at pH 6.5 and pH 9 using S-cheilanthifoline as a substrate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two full-length P450 cDNAs, CYP719A2 and CYP7193A, isolated
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
tissue expression patterns of CYP719A2 and CYP719A3, overview
brenda
expression is very similar in both roots and leaves, although the alkaloid accumulation patterns in these organs are quite different
brenda
expression is very similar in both roots and leaves, although the alkaloid accumulation patterns in these organs are quite different
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
CYP719A13 can be involved in both sanguinarine and berberine formation in Argemone mexicana
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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). C719D_ARGME
504
1
57452
Swiss-Prot
other Location (Reliability: 4)
C7192_ESCCA
495
1
56420
Swiss-Prot
other Location (Reliability: 5)
C7193_ESCCA
495
1
56806
Swiss-Prot
Secretory Pathway (Reliability: 2)
A0A240FWB4_CHEMJ
489
0
55641
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of cheilanthifoline synthase (CYP719A5), and stylopine synthase (CYP719A2) in Pichia pastoris. Biosynthetic enzyme expression is examined in a consolidated system with all genes expressed in one cell and a coculture system with three cell lines that each express a single gene were examined. Although both systems efficiently converted reticuline to stylopine, the consolidated system is more rapid and efficient than the co-culture system. However, substrate-feeding experiments reveal a decrease in the conversion efficiency in the consolidated system during successive cultures, whereas the conversion efficiency in the co-culture system remains constant. Thus, the final amount of stylopine produced from reticuline after successive feedings in the co-culture system is more than 150 nmoles from 750 nmoles of (R,S)-reticuline (375 nmoles of (S)-reticuline)
CYP719A2 and CYP719A3, DNA and amino acid sequence determination and analysis, expression patterns, expression in Saccharomyces cerevisiae microsomes
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two full-length P450 cDNAs, CYP719A2 and CYP7193A, expression in Saccharomyces cerevisiae
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
a microbial system is established for producing a protoberberine-type alkaloid (stylopine) in Pichia cells
synthesis
a microbial system is established for producing a protoberberine-type alkaloid (stylopine) in Pichia cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, W.; Zenk, M.H.
Two methylenedioxy bridge forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis
Phytochemistry
30
2953-2961
1991
Eschscholzia californica
-
brenda
Ikezawa, N.; Iwasa, K.; Sato, F.
Molecular cloning and characterization of methylenedioxy bridge-forming enzymes involved in stylopine biosynthesis in Eschscholzia californica
FEBS J.
274
1019-1035
2007
Eschscholzia californica
brenda
Diaz Chavez, M.L.; Rolf, M.; Gesell, A.; Kutchan, T.M.
Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana
Arch. Biochem. Biophys.
507
186-193
2011
Argemone mexicana (B1NF19), Argemone mexicana
brenda
Takemura, T.; Ikezawa, N.; Iwasa, K.; Sato, F.
Molecular cloning and characterization of a cytochrome P450 in sanguinarine biosynthesis from Eschscholzia californica cells
Phytochemistry
91
100-108
2013
Eschscholzia californica
brenda
Yahyazadeh, M.; Ratmoyo, P.; Bittner, F.; Sato, F.; Selmar, D.
Cloning and characterization of Cheilanthifoline and stylopine synthase genes from Chelidonium majus
Plant Cell Physiol.
58
1421-1430
2017
Chelidonium majus (A0A240FWB4)
-
brenda
Hori, K.; Okano, S.; Sato, F.
Efficient microbial production of stylopine using a Pichia pastoris expression system
Sci. Rep.
6
22201
2016
Eschscholzia californica (Q50LH3)
brenda
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