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Information on EC 2.1.1.128 - (RS)-norcoclaurine 6-O-methyltransferase and Organism(s) Coptis japonica and UniProt Accession Q9LEL6

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.128 (RS)-norcoclaurine 6-O-methyltransferase
IUBMB Comments
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.
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This record set is specific for:
Coptis japonica
UNIPROT: Q9LEL6
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The taxonomic range for the selected organisms is: Coptis japonica
The enzyme appears in selected viruses and cellular organisms
Synonyms
6-omt, norcoclaurine 6-o-methyltransferase, (s)-norcoclaurine-6-o-methyltransferase, (s)-coclaurine n-methyltransferase, s-adenosyl-l-methionine:norcoclaurine 6-o-methyltransferase, ps6omt, (s)-norcoclaurine 6-o-methyltransferase, (r,s)-norcoclaurine 6-o-methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Norcoclaurine 6-O-methyltransferase
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(R,S)-norcoclaurine 6-O-methyltransferase
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(S)-Coclaurine N-methyltransferase
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-
-
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6-OMT
Methyltransferase, (S)-coclaurine N-
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-
-
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Methyltransferase, norlaudanosoline
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-
-
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NLS-OMT
-
-
-
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Norcoclaurine 6-O-methyltransferase
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-
-
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S-Adenosyl-L-methionine:(S)-coclaurine-N-methyltransferase
-
-
-
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S-Adenosyl-L-methionine:norcoclaurine 6-O-methyltransferase
S-Adenosylmethionine:(R),(S)-norlaudanosoline-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
bi-bi ping-pong mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
methyl group transfer
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
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89700-33-4
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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 + (S)-norcoclaurine
S-adenosyl-L-homocysteine + (S)-coclaurine
show the reaction diagram
S-adenosyl-L-methionine + laudanosoline
?
show the reaction diagram
low activity
-
-
?
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)-norlaudanosoline
S-adenosyl-L-homocysteine + 6-O-methylnorlaudanosoline + 7-O-methylnorlaudanosoline
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
-
activity with (R,S)-norlaudanosoline is 76% of the activity with (S)-norcoclaurine
-
-
?
S-Adenosyl-L-methionine + norcoclaurine
S-Adenosyl-L-homocysteine + ?
show the reaction diagram
-
(S)-norcoclaurine and (R)-norcoclaurine
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + (S)-norcoclaurine
S-adenosyl-L-homocysteine + (S)-coclaurine
show the reaction diagram
S-adenosyl-L-methionine + (S)-norcoclaurine
S-adenosyl-L-homocysteine + (S)-coclaurine
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme requires divalent cations for activity
INHIBITOR
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
Co2+
-
5 mM, severe inhibition
Cu2+
-
5 mM, severe inhibition
Fe2+
-
5 mM, severe inhibition
Mn2+
-
5 mM, severe inhibition
Ni2+
-
5 mM, severe inhibition
S-adenosyl-L-homocysteine
-
-
Zn2+
-
5 mM, severe inhibition
additional information
-
not inhibited by chloromercuribenzenesulfonate and iodoacetamide
-
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
2.23
(R,S)-norlaudanosoline
-
-
3.95
S-adenosyl-L-methionine
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-
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
-
-
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
7.5
OMT enzyme assay
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
30
OMT enzyme assay
25
-
culture condition for Coptis japonica
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
6OMT_COPJA
347
0
38700
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
x * 40000, SDS-PAGE
95000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and Bio-Gel HTP column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expressed in Escherichia coli BL21(DE3) cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
production of the economically important analgesic morphine and the antimicrobial agent berberine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sato, F.; Tsujita, T.; Katagiri, Y.; Yoshida, S.; Yamada, Y.
Purification and characterization of S-adenosyl-L-methionine:norcoclaurine 6-O-methyltransferase from cultured Coptis japonica cells
Eur. J. Biochem.
225
125-131
1994
Coptis japonica
Manually annotated by BRENDA team
Inui, T.; Tamura, K.; Fujii, N.; Morishige, T.; Sato, F.
Overexpression of Coptis japonica norcoclaurine 6-O-methyltransferase overcomes the rate-limiting step in Benzylisoquinoline alkaloid biosynthesis in cultured Eschscholzia californica
Plant Cell Physiol.
48
252-262
2007
Coptis japonica (Q9LEL6), Coptis japonica, Eschscholzia californica
Manually annotated by BRENDA team
Kato, N.; Dubouzet, E.; Kokabu, Y.; Yoshida, S.; Taniguchi, Y.; Dubouzet, J.G.; Yazaki, K.; Sato, F.
Identification of a WRKY protein as a transcriptional regulator of benzylisoquinoline alkaloid biosynthesis in Coptis japonica
Plant Cell Physiol.
48
8-18
2007
Coptis japonica
Manually annotated by BRENDA team
Morishige, T.; Tamakoshi, M.; Takemura, T.; Sato, F.
Molecular characterization of O-methyltransferases involved in isoquinoline alkaloid biosynthesis in Coptis japonica
Proc. Jpn. Acad. Ser. B
86
757-768
2010
Coptis japonica
Manually annotated by BRENDA team