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EC Tree
IUBMB Comments A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline by the oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine. cf. EC 1.14.19.73, (S)-nandinine synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-nandinine.
The enzyme appears in viruses and cellular organisms
Synonyms
cheilanthifoline synthase, cyp719a14, cyp719a5, (s)-cheilanthifoline synthase,
more
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(S)-scoulerine oxidase (methylenedioxy-bridge-forming)
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cheilanthifoline synthase
EC 1.1.3.33
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formerly
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EC 1.14.21.2
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formerly
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S-cheilanthifoline synthase
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synthase, (S)-cheilanthifoline
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cheilanthifoline synthase
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cheilanthifoline synthase
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CYP719A5
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2 = (S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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oxidation
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reduction
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(S)-scoulerine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase [(S)-cheilanthifoline-forming]
A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline by the oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine. cf. EC 1.14.19.73, (S)-nandinine synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-nandinine.
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(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)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
(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
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
high substrate specificity
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
the enzyme is involved in biosynthesis of stylopine
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [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)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
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enzyme is induced 20 h after challenging the cell suspension cultur with elicitor
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
the enzyme is involved in biosynthesis of stylopine
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
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(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
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enzyme is induced 20 h after challenging the cell suspension cultur with elicitor
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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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0.0009 - 8.1
(S)-scoulerine
0.0009
(S)-scoulerine
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1.9
(S)-scoulerine
pH 8.0, 30°C, kcat: 100%
8.1
(S)-scoulerine
pH 8.0, 30°C, kcat: 29%
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additional information
additional information
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additional information
additional information
kcat (S)-coreximine: 1% compared to kcat (S)-cheilanthifoline: 100%
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additional information
additional information
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kcat (S)-coreximine: 1% compared to kcat (S)-cheilanthifoline: 100%
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additional information
additional information
kcat (S)-scoulerine: 100%, pH8, 30°C
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additional information
additional information
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kcat (S)-scoulerine: 100%, pH8, 30°C
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additional information
additional information
kcat (S)-scoulerine: 29%, kcat (S)-cheilanthifoline: 100%
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additional information
additional information
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kcat (S)-scoulerine: 29%, kcat (S)-cheilanthifoline: 100%
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8
assay at
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assay at, optimal pH using S-cheilanthifoline as a substrate
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7 - 9
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about 50% of maximal activity at pH 7 and pH 9
6 - 10
half optimal activity at pH 6.5 and 8.5
6 - 10
half optimal activity at pH 6.5 and pH 9 using S-cheilanthifoline as a substrate
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30
assay at
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UniProt
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UniProt
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SwissProt
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expression is very similar in both roots and leaves, although the alkaloid accumulation patterns in these organs are quite different
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highly expressed
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expression is very similar in both roots and leaves, although the alkaloid accumulation patterns in these organs are quite different
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metabolism
the enzyme is involved in biosynthesis of stylopine
physiological function
CYP719A13 can be involved in both sanguinarine and berberine formation in Argemone mexicana
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C719E_ARGME
494
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55780
Swiss-Prot
Secretory Pathway (Reliability: 2 )
C7195_ESCCA
490
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55179
Swiss-Prot
Secretory Pathway (Reliability: 2 )
A0A240FWB3_CHEMJ
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55065
TrEMBL
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C719D_ARGME
504
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57452
Swiss-Prot
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57450
calculated from cDNA
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-20°C, 15% loss of activity after 4 months
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yeast microsomal fractions are prepared
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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)
expressed in Spodoptera frugiperda Sf9 cells
heterologously expressed in Saccharcomyces cerevisiae
into the pT7Blue T-vector for sequencing, and subcloned into a yeast expression vector
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methyl jasmonate induces the expression of CYP719A genes in seedlings
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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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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
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Ikezawa, N.; Iwasa, K.; Sato, F.
CYP719A subfamily of cytochrome P450 oxygenases and isoquinoline alkaloid biosynthesis in Eschscholzia californica
Plant Cell Rep.
28
123-133
2009
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
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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
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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 (A0A240FWB3)
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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 (B5UAQ8)
brenda
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