Information on EC 2.1.1.128 - (RS)-norcoclaurine 6-O-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.128
-
RECOMMENDED NAME
GeneOntology No.
(RS)-norcoclaurine 6-O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + (RS)-norcoclaurine = S-adenosyl-L-homocysteine + (RS)-coclaurine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(S)-reticuline biosynthesis I
-
-
Biosynthesis of secondary metabolites
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-
Isoquinoline alkaloid biosynthesis
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-
Metabolic pathways
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-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(RS)-norcoclaurine 6-O-methyltransferase
The enzyme will also catalyse the 6-O-methylation of (RS)-norlaudanosoline to form 6-O-methyl-norlaudanosoline, but this alkaloid has not been found to occur in plants.
CAS REGISTRY NUMBER
COMMENTARY hide
167398-06-3
-
89700-33-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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suppression of norcoclaurine 6-O-methyltransferase transcript levels significantly suppresses total alkaloid accumulation in opium poppy (73% compared to the controls). However, the relative abundance of morphine increased to 55% of the total alkaloid content. Suppression of the enzyme does not significantly affect (S)-3'-hydroxy-N-methylcoclaurine 1 or (S)-3'-hydroxy-N-methylcoclaurine 2 transcript levels
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + (S)-reticuline
S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine
show the reaction diagram
-
-
-
?
S-Adenosyl-L-methionine + (R)-norlaudanosoline
S-Adenosyl-L-homocysteine + 6-O-methylnorlaudanosoline + 7-O-methylnorlaudanosoline
show the reaction diagram
S-Adenosyl-L-methionine + (R,S)-2,3-dihydroxy-9,10-dimethoxytetrahydroprotoberberine
S-Adenosyl-L-homocysteine + ?
show the reaction diagram
-
5% of the activity with (S)-norlaudanosoline
-
-
-
S-Adenosyl-L-methionine + (R,S)-4'-O-methylnorlaudanosoline
S-Adenosyl-L-homocysteine + norprotosinomenine
show the reaction diagram
-
34% of the activity with (S)-norlaudanosoline
-
-
S-Adenosyl-L-methionine + (R,S)-5'-O-methylnorlaudanosoline
S-Adenosyl-L-homocysteine + 6-O-methyllaudanosoline
show the reaction diagram
-
81% of the activity with (S)-norlaudanosoline
-
-
S-adenosyl-L-methionine + (RS)-norcoclaurine
S-adenosyl-L-homocysteine + (RS)-coclaurine
show the reaction diagram
S-adenosyl-L-methionine + (S)-norcoclaurine
S-adenosyl-L-homocysteine + (S)-coclaurine
show the reaction diagram
S-adenosyl-L-methionine + (S)-norlaudanosoline
S-adenosyl-L-homocysteine + 6-O-methylnorlaudanosoline
show the reaction diagram
S-adenosyl-L-methionine + (S)-norlaudanosoline
S-adenosyl-L-homocysteine + 6-O-methylnorlaudanosoline + 7-O-methylnorlaudanosoline
show the reaction diagram
S-Adenosyl-L-methionine + (S)-scoulerine
S-Adenosyl-L-homocysteine + jatrorrhizine
show the reaction diagram
-
1% of the activity with (S)-norlaudanosoline
-
-
S-Adenosyl-L-methionine + 2,3-dihydroxy-9,10-dimethoxyprotoberberine
S-Adenosyl-L-homocysteine + tetrahydrojatrorrhizine
show the reaction diagram
-
7% of the activity with (S)-norlaudanosoline
-
-
S-adenosyl-L-methionine + laudanosoline
?
show the reaction diagram
S-Adenosyl-L-methionine + laudanosoline
S-Adenosyl-L-homocysteine + tetrahydrocolumbamine
show the reaction diagram
-
79% of the activity with (S)-norlaudanosoline
-
-
S-Adenosyl-L-methionine + norcoclaurine
S-Adenosyl-L-homocysteine + ?
show the reaction diagram
-
(S)-norcoclaurine and (R)-norcoclaurine
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-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + (S)-reticuline
S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine
show the reaction diagram
Q9LEL6
-
-
-
?
S-adenosyl-L-methionine + (RS)-norcoclaurine
S-adenosyl-L-homocysteine + (RS)-coclaurine
show the reaction diagram
S-adenosyl-L-methionine + (S)-norcoclaurine
S-adenosyl-L-homocysteine + (S)-coclaurine
show the reaction diagram
S-adenosyl-L-methionine + (S)-norlaudanosoline
S-adenosyl-L-homocysteine + 6-O-methylnorlaudanosoline
show the reaction diagram
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putative rate-limiting step enzymes in benzylisoquinoline alkaloid biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme requires divalent cations for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,6-Dihydro-9,10-dimethoxybenzo[g]-1,3-benzodioxolo[5,6-a]quinolizium
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10 mM, 50% inhibition
Iodobenzoate
-
-
-
S-adenosyl-L-homocysteine
additional information
-
not inhibited by chloromercuribenzenesulfonate and iodoacetamide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
WRKY1
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CjWRKY1 is a necessary regulator to control overall gene expression in berberine biosynthesis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
(R,S)-4'-O-methylnorlaudanosoline
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-
0.3
(R,S)-laudanosoline
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-
0.2 - 2.23
(R,S)-norlaudanosoline
3.95
S-adenosyl-L-methionine
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-
0.05
S-adenosylmethionine
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with (S)-norlaudanosoline as cosubstrate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
5,6-Dihydro-9,10-dimethoxybenzo[g]-1,3-benzodioxolo[5,6-a]quinolizium
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-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
S-adenosyl-L-homocysteine
Coptis japonica
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using (S)-norlaudanosoline as cosubstrate, in 0.3 M Tris-HCl (pH 7.5), 25mM sodium ascorbate, at 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
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about 50% of maximal activity at pH 7.0 and 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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culture condition for Coptis japonica
30
OMT enzyme assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low enzyme level
Manually annotated by BRENDA team
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low enzyme level
Manually annotated by BRENDA team
-
sieve elements of the phloem adjacent or proximal to laticifers
Manually annotated by BRENDA team
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constant enzyme level over 16 days of germination
Manually annotated by BRENDA team
additional information
-
gene transcripts detected in all organs with highest levels in root and stem and lowest in leaf
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
immunogold labelling studies show the strict association with electron dense regions of the peripheral cytoplasm of sieve elements
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38500
-
x * 38500, immunoblotting
47000
-
gel filtration
95000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
half-life: 8 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete loss of activity after freezing in 30% glycerol solution
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50% loss of activity after 4 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and Bio-Gel HTP column chromatography
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recombinant protein using His-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli ER2566pLys S
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Eschscholzia californica; full-length cDNA of Coptis japonica 6OMT is cloned into the binary vector pBITXEl2 for introduction into Agrobacterium tumefaciens, for infection Eschscholzia californica seedlings are co-cultured with Agrobacterium tumefaciens; into the pET-21d vector for expression in Escherichia coli BL21DE3 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is upregulated in the high papaverine mutant pap1
the over-expression of regulatory factors AP2G, AN1-like, ERF2, GARP, MDB025 and WRKY1 increases the levels of codeinone reductase, (S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase) and (R,S)-norcoclaurine 6-O-methyltransferase transcripts by 10- to more than 100fold. The transcriptional activations translate into an enhancement of alkaloid production in opium poppy of up to at least 10fold
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis