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Information on EC 2.1.1.117 - (S)-scoulerine 9-O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.117
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.117 (S)-scoulerine 9-O-methyltransferase
IUBMB Comments
The product of this reaction is a precursor for protoberberine alkaloids in plants
The enzyme appears in viruses and cellular organisms
- 2.1.1.117
-
benzylisoquinoline
- coptis
-
s-scoulerine
- japonica
- poppy
- californica
-
eschscholzia
-
s-tetrahydrocolumbamine
-
n-methylated
-
regio-specific
- papaveraceae
- n-methyltransferase
- norreticuline
-
methylenedioxy
- isoquinoline
-
benzophenanthridine
-
opium
-
virus-induced
- sanguinarine
-
7-o-methylated
- allocryptopine
- noscapine
- medicine
- analysis
Reaction Schemes
showSynonyms
somt1, scoulerine-9-o-methyltransferase, scoulerine 9-o-methyltransferase, scoulerine 9-omt, (s)-scoulerine 9-o-methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-Adenosyl-L-methionine:(S)-scoularine 9-O-methyltransferase
-
-
-
-
Methyltransferase, (S)-scoularine 9-
-
-
-
-
Methyltransferase, (S)-scoularine 9- (Coptis japonica clone pCJSMT)
-
-
-
-
scoulerine 9-O-methyltransferase
scoulerine/reticuline O-methyltransferase
-
SMT
SOMT
SMT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + (S)-scoulerine = S-adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
berberine biosynthesis, chelerythrine biosynthesis, noscapine biosynthesis, palmatine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase
The product of this reaction is a precursor for protoberberine alkaloids in plants
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CAS REGISTRY NUMBER
COMMENTARY
164205-21-4
methyltransferase, (S)-scoularine 9- (Coptis japonica clone pCJSMT)
96380-65-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + (S)-tetrahydropalmatrubine
S-adenosyl-L-homocysteine + (S)-tetrahydropalmatine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + (2,3,9,10)-tetrahydroxyberbine
S-adenosyl-L-homocysteine + (2,3,10)-trihydroxy-9-methoxy-berbine
S-adenosyl-L-methionine + (2,3,9,10)-tetrahydroxyberbine
S-adenosyl-L-homocysteine + (S)-scoulerine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (R,S)-2,3,9,10-tetrahydroxytetrahydroprotoberberine
?
-
Substrates: methylated at 50% of the rate of (S)-scoulerine
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-3,9-dihydroxy-2,10-dimethoxytetrahydroprotoberberine
?
-
Substrates: methylated at 4% of the rate of (S)-scoulerine
Products: -
Products: -
?
S-adenosyl-L-methionine + (S)-norreticuline
S-adenosyl-L-homocysteine + norcodamine + norlaudanine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + (S)-reticuline
S-adenosyl-L-homocysteine + codamine + laudanine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
S-adenosyl-L-methionine + (S)-scoulerine
S-adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine + 2-O-methylscoulerine + tetrahydropalmatine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + (S)-tetrahydrocolumbamine
S-adenosyl-L-homocysteine + (S)-tetrahydropalmatine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + 6-O-methylnorlaudanosoline
?
-
Substrates: 8% of the activity relative to (S)-scoulerine
Products: -
Products: -
?
S-adenosyl-L-methionine + norlaudanine
S-adenosyl-L-homocysteine + tetrahydropapaverine
Substrates: the engineered scoulerine 9-O-methyltransferase is capable of O-methylating 1-benzylisoquinoline alkaloids at the 3' position
Products: -
Products: -
?
S-Adenosyl-L-methionine + norlaudanosoline
?
-
Substrates: 2% of the activity relative to (S)-scoulerine
Products: -
Products: -
?
S-Adenosyl-L-methionine + norreticuline
?
-
Substrates: 9% of the activity relative to (S)-scoulerine
Products: -
Products: -
?
S-adenosyl-L-methionine + norreticuline
S-adenosyl-L-homocysteine + norcodamine
Substrates: the engineered scoulerine 9-O-methyltransferase is capable of O-methylating 1-benzylisoquinoline alkaloids at the 3' position
Products: -
Products: -
?
S-adenosyl-L-methionine + (2,3,9,10)-tetrahydroxyberbine
S-adenosyl-L-homocysteine + (2,3,10)-trihydroxy-9-methoxy-berbine
Substrates: PsSOMT exhibits high regiospecificity as the 9-O-methyltransferase targeting 2,3,9,10-tetrahydroxyberbine
Products: -
Products: -
?
S-adenosyl-L-methionine + (2,3,9,10)-tetrahydroxyberbine
S-adenosyl-L-homocysteine + (2,3,10)-trihydroxy-9-methoxy-berbine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
?
-
Substrates: central role in orotoberberine biosynthesis
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
?
-
Substrates: the enzyme is responsible for a late step in the biosynthesis of berberine
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
ir
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is a scoulerine-9-O-methyltransferase for the biosynthesis of chelerythrine in California poppy, it produces 7-O-methylated, 3'-O-methylated and dual O-methylated products from reticuline and norreticuline, and 9-O-methylated tetrahydrocolumbamine, 2-O-methylscoulerine and tetrahydropalmatine from scoulerine
Products: -
Products: -
?
additional information
?
-
Substrates: product identification by NMR spectroscopy
Products: -
Products: -
-
additional information
?
-
Substrates: enzyme catalyzes O-methylation at C-9 and C-2, and O-methylation events occur first at C-9 and then at C-2
Products: -
Products: -
?
additional information
?
-
Substrates: SiSOMT is able to sequentially provide 9-O- and 2-O-methylated 2,3,9,10-tetrahydroxyberbine. Product identification by NMR spectroscopy
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
S-Adenosyl-L-methionine + (S)-scoulerine
?
-
Substrates: central role in orotoberberine biosynthesis
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
?
-
Substrates: the enzyme is responsible for a late step in the biosynthesis of berberine
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
ir
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
-
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
?
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
divalent cations are not required
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibitory: Mg2+, Mn2+, Fe2+
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0382
(S)-norreticuline
product norlaudanine, pH 8.4, 35°C
0.04409
(2,3,9,10)-tetrahydroxyberbine
pH 7.5, 37°C, recombinant detagged enzyme
-
0.05377
(2,3,9,10)-tetrahydroxyberbine
pH 7.5, 37°C, recombinant detagged enzyme
-
0.187
(S)-reticuline
product codamine, pH 8.4, 35°C
0.393
(S)-reticuline
product laudanine, pH 8.4, 35°C
0.0219
(S)-scoulerine
product 2-O-methylscoulerine, pH 8.4, 35°C
0.0245
(S)-scoulerine
product (S)-tetrahydrocolumbamine, pH 8.4, 35°C
0.0093
S-adenosyl-L-methionine
cosubstrate (S)-scoulerine, product (S)-tetrahydrocolumbamine, pH 8.4, 35°C
0.0145
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product codamine, pH 8.4, 35°C
0.0157
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product norlaudanine, pH 8.4, 35°C
0.0288
S-adenosyl-L-methionine
cosubstrate (S)-scoulerine, product 2-O-methylscoulerine, pH 8.4, 35°C
0.119
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product laudanine, pH 8.4, 35°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
(S)-norreticuline
product norlaudanine, pH 8.4, 35°C
0.52
(2,3,9,10)-tetrahydroxyberbine
pH 7.5, 37°C, recombinant detagged enzyme
-
1.68
(2,3,9,10)-tetrahydroxyberbine
pH 7.5, 37°C, recombinant detagged enzyme
-
0.05
(S)-reticuline
product codamine, pH 8.4, 35°C
0.24
(S)-reticuline
product laudanine, pH 8.4, 35°C
0.01
(S)-scoulerine
product 2-O-methylscoulerine, pH 8.4, 35°C
0.02
(S)-scoulerine
product (S)-tetrahydrocolumbamine, pH 8.4, 35°C
0.01
S-adenosyl-L-methionine
cosubstrate (S)-scoulerine, product (S)-tetrahydrocolumbamine, pH 8.4, 35°C
0.01
S-adenosyl-L-methionine
cosubstrate (S)-scoulerine, product 2-O-methylscoulerine, pH 8.4, 35°C
0.01
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product norlaudanine, pH 8.4, 35°C
0.08
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product codamine, pH 8.4, 35°C
0.12
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product laudanine, pH 8.4, 35°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
(S)-norreticuline
product norlaudanine, pH 8.4, 35°C
9.671
(2,3,9,10)-tetrahydroxyberbine
pH 7.5, 37°C, recombinant detagged enzyme
-
38.1
(2,3,9,10)-tetrahydroxyberbine
pH 7.5, 37°C, recombinant detagged enzyme
-
0.27
(S)-reticuline
product codamine, pH 8.4, 35°C
0.61
(S)-reticuline
product laudanine, pH 8.4, 35°C
0.46
(S)-scoulerine
product 2-O-methylscoulerine, pH 8.4, 35°C
0.82
(S)-scoulerine
product (S)-tetrahydrocolumbamine, pH 8.4, 35°C
0.35
S-adenosyl-L-methionine
cosubstrate (S)-scoulerine, product 2-O-methylscoulerine, pH 8.4, 35°C
0.64
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product norlaudanine, pH 8.4, 35°C
1
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product laudanine, pH 8.4, 35°C
1.07
S-adenosyl-L-methionine
cosubstrate (S)-scoulerine, product (S)-tetrahydrocolumbamine, pH 8.4, 35°C
5.5
S-adenosyl-L-methionine
cosubstrate (S)-reticuline, product codamine, pH 8.4, 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
transient RNA silencing of scoulerine 9-O-methyltransferase expression by double stranded RNA in Coptis japonica protoplasts
Uniprot
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
differential expression of genes encoding enzymes of the BIA biosynthesis pathway, including scoulerine 9-O-methyltransferase, between tubers and leaves, overview
brenda
-
activity of high berberine-producing cells is higher than that of non-selected cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
phylogenetic analysis shows that all the OMT candidates cluster into 4 major clades: 6-OMT, 4-OMT, CoOMT, and SOMT. R7OMT is separated from all the presenting clades, which reveals the lack of homologous enzymes in Corydalis yanhusuo
malfunction
engineering of a variant of TfS9OMT with seven amino acid mutations results in a 35fold increase in THP titers compared to the wild-type TfS9OMT isoform, method, overview
metabolism
physiological function
additional information
metabolism
-
the gene expressions of berberine bridge enzymes (BBEs) like TsBBE2 have peak expression in low nitrogen treatments but are absent in higher nitrogen treatments. Similar trends are observed for other enzymes such as (S)-scoulerine 9-O-methyltransferase (TsCMT3), tetrahydroberberine oxidase (TsSTOX), and columbamine O-methyltransferase (TsCoCOMT2-4) in response to nitrogen levels. Comparison of (S)-scoulerine 9-O-methyltransferase with other enzymes in a transcriptomics and metabolomics analysis of secondary plant metabolism in response to N fertilizer, overview. Key enzymes in 1-benzylisoquinoline alkaloids (BIAs) biosynthesis pathways, such as (S)-norcoclaurine, coclaurine, N-methylcoclaurine, methylcoclaurine, reticuline, scoulerine, tetrahydrocolumbamine, N-methyltetrahydropalmatine, and columbamine, exhibit significant enrichment in 90 g N/pot. These enzymes show a decreasing trend at lower and higher N fertilizer levels, suggesting a predominantly negative response to extreme N conditions
metabolism
-
analysis of the benzylisoquinoline alkaloids (BIAs) biosynthetic pathway in Corydalis yanhusuo by metabolomics and transcriptomics. The BIA are the main bioactive ingredients in the plant, variation in metabolites in the tuber and leaf groups, including increased levels of scoulerine, tetrahydroberberine, tetrahydrocolumbamine, columbamine, tetrahydropalmatine, sanguinarine, corydaline, protopine, tetrahydrocoptisine, noroxyhydrastinine, dehydrocorydaline, oxoglaucine, 8-oxycoptisine, palmatine, coptisine, berberine, jatrorrhizine, epiberberine, and glaucine, overview. Scoulerine 9-O-methyltransferase (SOMT) catalyzes the penultimate step for tetrahydropalmatine synthesis
physiological function
the methyltransferase SOMT (SiSOMT), derived from Stephania intermedia, catalyzes the synthesis of several tetrahydroprotoberberine (THPB) compounds, selective methylation catalyzed by SOMT, overview
physiological function
the methyltransferase SOMT (SiSOMT), derived from Papaver somniferum, catalyzes the synthesis of several tetrahydroprotoberberine (THPB) compounds, selective methylation catalyzed by SOMT, overview
additional information
the active site of SiSOMT is formed by three amino acids, with Lys250 interacting with C-9, while His219 and Leu217 interact with the C-2 of substrate (2,3,9,10)-tetrahydroxyberbine. His219 and Leu217 may contribute to SiSOMT's capacity for two successive methylations
additional information
in PsSOMT, Lys292 and Ser211 interact with the C-9 of substrate (2,3,9,10)-tetrahydroxyberbine
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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). OMT3B_PAPSO
339
0
37691
Swiss-Prot
Secretory Pathway (Reliability: 5)
SOMT2_PAPSO
356
0
39087
Swiss-Prot
Mitochondrion (Reliability: 1)
A0A224ALZ8_ESCCA
362
0
39765
TrEMBL
-
Q5C9L2_THLFG
355
0
38591
TrEMBL
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
all the OMTs from other plant species contain two domains: the C-terminal methyltransferase domain is typical of SAM-dependent O-methyltransferases, and the N-terminal domain is a dimerization domain that is found in a variety of plant OMTs. The dimerization domain not only stabilizes the homodimer through hydrophobic interactions but also provides an extra water-mediated hydrogen bond with the substrate to improve specificity
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a selective methylation strategy is developed for the biocatalysis of seven high-value-added THPB compounds using 4'-O-methyltransferase (Cj4'OMT), norcoclaurine 6-O-methyltransferase (Cj6OMT), and (S)-scoulerine 9-O-methyltransferase (Stephania intermedia SiSOMT or PsSOMT) in engineered Escherichia coli. The methyltransferases Cj4'OMT, Cj6OMT, PsSOMT, and SiSOMT are expressed heterologously in Escherichia coli strain BL21(DE3)
additional information
a selective methylation strategy is developed for the biocatalysis of seven high-value-added THPB compounds using 4'-O-methyltransferase (Cj4'OMT), norcoclaurine 6-O-methyltransferase (Cj6OMT), and (S)-scoulerine 9-O-methyltransferase (SiSOMT or Papaver somniferum PsSOMT) in engineered Escherichia coli. The methyltransferases Cj4'OMT, Cj6OMT, PsSOMT, and SiSOMT are expressed heterologously in Escherichia coli strain BL21(DE3)
additional information
development of an engineered Saccharomyces cerevisiae strain for de novo biosynthesis of tetrahydropapaverine (THP). Production of THP is achieved through heterologous expression of two enzyme variants with activity on nonnative substrates. Engineering of variants of N-methylcoclaurine hydroxylase and of scoulerine 9-O-methyltransferase (TfS9OMTDS) with activity on coclaurine and capable of O-methylating 1-benzylisoquinoline alkaloids at the 3' position, respectively, enabling de novo norreticuline and THP biosynthesis. TfS9OMTDS 3' OMT activity for THP production is low on the nonnative substrates in the reconstructed THP pathway, additional optimization of engineered TfS9OMT 3' OMT activity with additional NNK mutagenesis. Flux through the heterologous pathway is improved by knocking out yeast multidrug resistance transporters and optimization of media conditions. The strain engineering increases the concentration of biosynthesized THP by 600fold to 0.121 mg/l. Method optimization, overview. Papaver somniferum norreticuline 7-O-methyltransferase (PsN7OMT) and Thalictrum flavum scoulerine 9-O-methyltransferase (TfS9OMT), are added to the strain (with SNQ2 and PDR5 knocked out) to O-methylate norreticuline at the 7 and 3' positions, respectively, resulting in de novo yeast biosynthesis of THP
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by amylose affinity chromatography
recombinant MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by amylose affinity chromatography
recombinant MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by amylose affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
canadine-producing Saccharomyces cerevisiae strain harbors expression cassettes for seven heterologous enzymes: Papaper somniferum norcoclaurine 6-O-methyltransferase (Ps6OMT), Papaver somniferum 3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase 2 (Ps4'OMT), Papapver somniferum coclaurine N-methyltransferase (PsCNMT), Papaver somniferum berberine bridge enzyme (PsBBE), Thalictrum flavum scoulerine 9-O-methyltransferase (TfS9OMT), Thalictrum flavum canadine synthase (TfCAS), and Arabidopsis thaliana cytochrome P450 reductase 1 (CPR). The expression cassettes for the methyltransferases Ps6OMT, PsCNMT, and Ps4'OMT and the cytochrome P450 reductase CPR were chromosomally integrated, TfS9OMT and TfCAS are expressed from a high-copy plasmid, and PsBBE is expressed from a second high-copy plasmid
expression in Escherichia coli
functional recombinant expression of the engineered Thalictrum flavum S9OMT enzyme in Saccharomyces cerevisiae strain CSY1174 from a high-copy plasmid
gene SOMT, recombinant expression of MBP-tagged enzyme in Escherichia coli strain BL21(DE3)
gene SOMT3, recombinant expression of MBP-tagged enzyme in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the (S)-scoulerine 9-O-methyltransferase (SMT) gene TsB11G003840 (TsCMT3) shows high expression in medium N fertilizer treatments and is not expressed in higher nitrogen medium, expression analysis of the enzyme, comparison with other enzymes in a transcriptomics and metabolomics analysis of secondary plant metabolism in response to N fertilizer, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
transient RNA silencing of scoulerine 9-O-methyltransferase expression by double stranded RNA in Coptis japonica protoplasts. Utility of gene silencing based on in vitro synthesized dsRNA to study function and behavior of endogenous enzymes
medicine
a Saccharomyces cerevisiae strain is engineered to express seven heterologous enzymes (Papaper somniferum norcoclaurine 6-O-methyltransferase (Ps6OMT), Papaver somniferum 3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase 2 (Ps4'OMT), Papapver somniferum coclaurine N-methyltransferase (PsCNMT), Papaver somniferum berberine bridge enzyme (PsBBE), Thalictrum flavum scoulerine 9-O-methyltransferase (TfS9OMT), Thalictrum flavum canadine synthase (TfCAS), and Arabidopsis thaliana cytochrome P450 reductase 1 (CPR)), resulting in protoberberine alkaloid production from a simple benzylisoquinoline alkaloid precursor. A number of strategies are implemented to improve flux through the pathway, including enzyme variant screening, genetic copy number variation, and culture optimization. This leads to an over 70-fold increase in canadine titer up to 1.8 mg/l. Increased canadine titers enable extension of the pathway to produce berberine, a major constituent of several traditional medicines in a microbial host. This strain is viable at pilot scale
synthesis
synthesis
the enzyme is utilized in an approach for selective methylation to produce high-value-added tetrahydroprotoberberine alkaloids in pharmaceutical use
synthesis
the enzyme is utilized in an approach for selective methylation to produce high-value-added tetrahydroprotoberberine alkaloids in pharmaceutical use
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujiwara, H.; Takeshita, N.; Terano, Y.; Fitchen, J.H.; Tsujita, T.; Katagiri, Y.; Sato, F.; Yamada, Y.
Expression of (S)-scoulerine 9-O-methyltransferase in Coptis japonica plants
Phytochemistry
34
949-954
1993
Coptis japonica
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brenda
Sato, F.; Takeshita, N.; Fitchen, J.H.; Fujiwara, H.; Yamada, Y.
S-Adenosyl-L-methionine:scoulerine-9-O-methyltransferase from cultured Coptis japonica cells
Phytochemistry
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1993
Coptis japonica
-
brenda
Takeshita, N.; Fujiwara, H.; Mimura, H.; Fitchen, J.H.; Yamada, Y.; Sato, F.
Molecular cloning and characterization of S-adenosyl-L-methionine:scoulerine 9-O-methyltransferase from cultured cells of Coptis japonica
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36
29-36
1995
Coptis japonica
brenda
Galneder, E.; Rueffer, M.; Wanner, G.; Tabata, M.; Zenk, M.H.
Alternative final steps in berberine biosynthesis in Coptis japonica cell cultures
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7
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Berberis stolonifera, Coptis japonica
brenda
Muemmler, S.; Rueffer, M.; Nagakura, N.; Zenk, M.H.
S-Adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase, a highly stereo- and regio-specific enzyme in tetrahydroprotoberberine biosynthesis
Plant Cell Rep.
4
36-39
1985
Berberis wilsoniae
brenda
Dubouzet, J.G.; Morishige, T.; Fujii, N.; An, C.I.; Fukusaki, E.; Ifuku, K.; Sato, F.
Transient RNA silencing of scoulerine 9-O-methyltransferase expression by double stranded RNA in Coptis japonica protoplasts
Biosci. Biotechnol. Biochem.
69
63-70
2005
Coptis japonica (Q39522), Coptis japonica
brenda
Takemura, T.; Ikezawa, N.; Iwasa, K.; Sato, F.
Metabolic diversification of benzylisoquinoline alkaloid biosynthesis through the introduction of a branch pathway in Eschscholzia californica
Plant Cell Physiol.
51
949-959
2010
Coptis japonica
brenda
Dang, T.T.; Facchini, P.J.
Cloning and characterization of canadine synthase involved in noscapine biosynthesis in opium poppy
FEBS Lett.
588
198-204
2014
Papaver somniferum
brenda
Zhu, Q.; Zhou, J.; Zhang, G.; Liao, H.
Homology modeling and molecular docking studies of (S)-scoulerine 9-O-methyltransferase from Coptis chinensis
Chin. J. Chem.
30
2533-2538
2012
Coptis chinensis (E0W6R9)
-
brenda
Galanie, S.; Smolke, C.
Optimization of yeast-based production of medicinal protoberberine alkaloids
Microb. Cell Fact.
14
144
2015
Thalictrum flavum subsp. glaucum (Q5C9L2)
brenda
Zhao, W.; Shen, C.; Zhu, J.; Ou, C.; Liu, M.; Dai, W.; Liu, X.; Liu, J.
Identification and characterization of methyltransferases involved in benzylisoquinoline alkaloids biosynthesis from Stephania intermedia
Biotechnol. Lett.
42
461-469
2019
Stephania intermedia (A0A5P9PAM0)
brenda
He, S.; Liang, Y.; Cong, K.; Chen, G.; Zhao, X.; Zhao, Q.; Zhang, J.; Wang, X.; Dong, Y.; Yang, J.; Zhang, G.; Qian, Z.; Fan, W.; Yang, S.
Identification and characterization of genes involved in benzylisoquinoline alkaloid biosynthesis in coptis species
Front. Plant Sci.
9
731
2018
Coptis teeta (A0A2Z5FRS0), Coptis teeta
brenda
Purwanto, R.; Hori, K.; Yamada, Y.; Sato, F.
Unraveling additional O-methylation steps in benzylisoquinoline alkaloid biosynthesis in California poppy (Eschscholzia californica)
Plant Cell Physiol.
58
1528-1540
2017
Eschscholzia californica subsp. californica (A0A224ALZ8)
brenda
Xu, D.; Lin, H.; Tang, Y.; Huang, L.; Xu, J.; Nian, S.; Zhao, Y.
Integration of full-length transcriptomics and targeted metabolomics to identify benzylisoquinoline alkaloid biosynthetic genes in Corydalis yanhusuo
Hortic. Res.
8
16
2021
Corydalis yanhusuo
brenda
Alami, M.M.; Shu, S.; Liu, S.; Alami, M.J.; Feng, S.; Mei, Z.; Yang, G.; Wang, X.
Impact of nitrogen rates on biosynthesis pathways a comparative study of diterpene synthases in clerodane diterpenoids and enzymes in benzylisoquinoline alkaloids
Int. J. Biol. Macromol.
280
135985
2024
Paratinospora sagittata
brenda
Zhao, W.; Liu, M.; Liu, K.; Liu, H.; Liu, X.; Liu, J.
An enzymatic strategy for the selective methylation of high-value-added tetrahydroprotoberberine alkaloids
Int. J. Mol. Sci.
24
15214
2023
Papaver somniferum (I3PLQ7), Stephania intermedia (A0A5P9PAM0)
brenda
Jamil, O.K.; Cravens, A.; Payne, J.T.; Kim, C.Y.; Smolke, C.D.
Biosynthesis of tetrahydropapaverine and semisynthesis of papaverine in yeast
Proc. Natl. Acad. Sci. USA
119
e2205848119
2022
Thalictrum flavum subsp. glaucum (Q5C9L2)
brenda
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