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Information on EC 2.1.1.140 - (S)-coclaurine-N-methyltransferase
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EC Tree
2.1.1.140 (S)-coclaurine-N-methyltransferaseIUBMB Comments
The enzyme is specific for the (S)-isomer of coclaurine. Norcoclaurine can also act as an acceptor.
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Word Map
- 2.1.1.140
-
benzylisoquinoline
-
n-methylated
- japonica
- coptis
- isoquinoline
- norreticuline
-
s-reticuline
- n-methyltransferases
- norcoclaurine
- poppy
- scoulerine
- somniferum
-
3\'-hydroxylase
-
4\'omt
- magnoflorine
-
6-o-methyltransferase
-
opium
-
papaver
- tetrahydroisoquinoline
-
aporphine
- medicine
- biotechnology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
coclaurine n-methyltransferase, s-adenosyl-l-methionine:coclaurine n-methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-Coclaurine N-methyltransferase
CNMT
coclaurine N-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of methyl group
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(S)-coclaurine-N-methyltransferase
The enzyme is specific for the (S)-isomer of coclaurine. Norcoclaurine can also act as an acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
167398-06-3
-
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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)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (R)-N-methylcoclaurine
-
-
-
?
(R,S)-6-O-methylnorlaudanosoline + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (R,S)-N-methyl-6-O-methyl-norlaudanosoline
-
-
-
?
(R,S)-norlaudanosoline + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (R,S)-N-methylnorlaudanosoline
-
-
-
?
(R,S)-norreticuline + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (R,S)-N-methylnorreticuline
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
(S)-norcoclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (R)-N-methylnorcoclaurine
-
strictly stereospecific, only (S)-norcoclaurine is N-methylated
-
?
1-methyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-methionine
N-methyl-1-methyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-methionine
-
-
-
?
6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-methionine
N-methyl-6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-methionine
-
-
-
?
S-adenosyl-L-methionine + (R)-coclaurine
S-adenosyl-L-homocysteine + (R)-N-methylcoclaurine
S-adenosyl-L-methionine + (R)-N-methylcoclaurine
S-adenosyl-L-homocysteine + (R)-magnocurarine
-
-
-
?
S-adenosyl-L-methionine + (R,S)-6-O-methylnorlaudanosoline
S-adenosyl-L-homocysteine + (R,S)-6-O-methyllaudanosoline
-
-
-
?
S-adenosyl-L-methionine + (R,S)-6-O-methylnorlaudanosoline
S-adenosyl-L-homocysteine + (R,S)-N-methyl-6-O-methylnorlaudanosoline
S-adenosyl-L-methionine + (R,S)-norlaudanosoline
S-adenosyl-L-homocysteine + (R,S)-N-methylnorlaudanosoline
S-adenosyl-L-methionine + (R,S)-norreticuline
S-adenosyl-L-homocysteine + (R,S)-N-methylnorreticuline
-
55% of the activity with (S)-coclaurine
-
-
?
S-adenosyl-L-methionine + (RS)-coclaurine
S-adenosyl-L-homocysteine + (RS)-N-methylcoclaurine
-
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
S-adenosyl-L-methionine + (S)-N-methylcoclaurine
S-adenosyl-L-homocysteine + ?
weak activity
-
-
?
S-adenosyl-L-methionine + (S)-reticuline
S-adenosyl-L-homocysteine + (S)-tembetarine
-
-
-
?
S-adenosyl-L-methionine + 1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline
S-adenosyl-L-homocysteine + 6,7-dihydroxy-1,N-dimethyl-1,2,3,4-tetrahydroisoquinoline
S-adenosyl-L-methionine + 6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline
S-adenosyl-L-homocysteine + 6,7-dimethoxy-N-methyl-1,2,3,4-tetrahydroisoquinoline
-
39% of the activity with (S)-coclaurine
-
-
?
S-adenosyl-L-methionine + 6,7-dimethoxy-N-methyl-1,2,3,4-tetrahydroisoquinoline
S-adenosyl-L-homocysteine + 6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline
-
180% of the activity with (R,S)-norreticuline
-
-
?
S-adenosyl-L-methionine + heliamine
S-adenosyl-L-homocysteine + N-methylheliamine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Berberis koetineana
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Bocconia cordata
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Corydalis vaginans
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Thalictrum glaucum
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
strictly stereospecific, only (S)-coclaurine is N-methylated
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Tinospora fragosa
-
-
-
?
S-adenosyl-L-methionine + (R)-coclaurine
S-adenosyl-L-homocysteine + (R)-N-methylcoclaurine
-
122% of the activity with (S)-coclaurine
-
-
?
S-adenosyl-L-methionine + (R)-coclaurine
S-adenosyl-L-homocysteine + (R)-N-methylcoclaurine
-
240% of the activity with (R,S)-norreticuline
-
-
?
S-adenosyl-L-methionine + (R)-coclaurine
S-adenosyl-L-homocysteine + (R)-N-methylcoclaurine
-
-
-
?
S-adenosyl-L-methionine + (R,S)-6-O-methylnorlaudanosoline
S-adenosyl-L-homocysteine + (R,S)-N-methyl-6-O-methylnorlaudanosoline
-
38% of the activity with (S)-coclaurine
-
-
?
S-adenosyl-L-methionine + (R,S)-6-O-methylnorlaudanosoline
S-adenosyl-L-homocysteine + (R,S)-N-methyl-6-O-methylnorlaudanosoline
-
69% of the activity with (R,S)-norreticuline
-
-
?
S-adenosyl-L-methionine + (R,S)-norlaudanosoline
S-adenosyl-L-homocysteine + (R,S)-N-methylnorlaudanosoline
-
48% of the activity with (S)-coclaurine
-
-
?
S-adenosyl-L-methionine + (R,S)-norlaudanosoline
S-adenosyl-L-homocysteine + (R,S)-N-methylnorlaudanosoline
-
49% of the activity with (R,S)-norreticuline
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
?
-
pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline: (S)-norcoclaurine is stereoselectively metabolized to (S)-reticuline via (S)-coclaurine, (S)-N-methylcoclaurine and (S)-3'-hydroxy-N-methylcoclaurine
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
?
-
pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline: (S)-norcoclaurine is stereoselectively metabolized to (S)-reticuline via (S)-coclaurine, (S)-N-methylcoclaurine and (S)-3'-hydroxy-N-methylcoclaurine
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
?
-
pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline: (S)-norcoclaurine is stereoselectively metabolized to (S)-reticuline via (S)-coclaurine, (S)-N-methylcoclaurine and (S)-3'-hydroxy-N-methylcoclaurine
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
isoquinoline alkaloid biosynthesis
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
sequential bi-substrate mechanism, ordered bi bi or rapid equilibrium random bi bi
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
sequential mechanism, 153% of the activity with (R,S)-norreticuline
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
isoquinoline alkaloid biosynthesis
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
expression systems tested by analyzing recombinant CMT protein
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
analysis of the evolutionary recruitment of enzymes into plant alkaloid pathways
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
S-Adenosyl-L-homocysteine + N-methylcoclaurine
-
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
S-Adenosyl-L-homocysteine + N-methylcoclaurine
-
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
S-Adenosyl-L-homocysteine + N-methylcoclaurine
-
-
-
?
S-adenosyl-L-methionine + 1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline
S-adenosyl-L-homocysteine + 6,7-dihydroxy-1,N-dimethyl-1,2,3,4-tetrahydroisoquinoline
-
10% of the activity with (S)-coclaurine
-
-
?
S-adenosyl-L-methionine + 1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline
S-adenosyl-L-homocysteine + 6,7-dihydroxy-1,N-dimethyl-1,2,3,4-tetrahydroisoquinoline
-
15% of the activity with (R,S)-norreticuline
-
-
?
additional information
?
-
-
no activity with (R,S)-scoulerine, 1,2,3,4-tetrahydroisoquinoline, 1,2,3,4-tetrahydro-3-isoquinolinecarboxylic acid or (+)-emetine
-
-
?
additional information
?
-
-
no activity with: (R,S)-scoulerine, 1,2,3,4-tetrahydroisoquinoline and 1,2,3,4-tetrahydro-3-isoquinoline carboxylic acid (+)-emetine
-
-
?
additional information
?
-
-
involvement in magnoflorine biosynthesis determined, crude enzyme preparation of recombinant CNMT protein analyzed, recombinant CjCNMT protein shown to convert (S)-corytuberine to magnoflorine
-
-
?
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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
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Berberis koetineana
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Bocconia cordata
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Corydalis vaginans
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Thalictrum glaucum
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
(S)-coclaurine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Tinospora fragosa
-
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
?
-
pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline: (S)-norcoclaurine is stereoselectively metabolized to (S)-reticuline via (S)-coclaurine, (S)-N-methylcoclaurine and (S)-3'-hydroxy-N-methylcoclaurine
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
?
-
pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline: (S)-norcoclaurine is stereoselectively metabolized to (S)-reticuline via (S)-coclaurine, (S)-N-methylcoclaurine and (S)-3'-hydroxy-N-methylcoclaurine
-
-
?
S-Adenosyl-L-methionine + (S)-coclaurine
?
-
pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline: (S)-norcoclaurine is stereoselectively metabolized to (S)-reticuline via (S)-coclaurine, (S)-N-methylcoclaurine and (S)-3'-hydroxy-N-methylcoclaurine
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
isoquinoline alkaloid biosynthesis
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
isoquinoline alkaloid biosynthesis
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
-
?
S-adenosyl-L-methionine + (S)-coclaurine
S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
50% inhibition at 0.062 mM, substrate (S)-coclaurine
additional information
-
no inhibition by PCMB, iodoacetamide; not inhibited by EDTA, iodoacetamide, p-chloromercuribenzoate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
(S)-norcoclaurine
-
probably allosteric enzyme, Hill coeffizient 2.6
0.265
(RS)-coclaurine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.601
(RS)-coclaurine
mutant Y328A, pH not specified in the publication, temperature not specified in the publication
1.033
(RS)-coclaurine
mutant W329A, pH not specified in the publication, temperature not specified in the publication
1.726
(RS)-coclaurine
mutant F332A, pH not specified in the publication, temperature not specified in the publication
0.311
heliamine
wild-type, pH not specified in the publication, temperature not specified in the publication
1.565
heliamine
mutant W329A, pH not specified in the publication, temperature not specified in the publication
2.096
heliamine
mutant Y328A, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
(RS)-coclaurine
mutant W329A, pH not specified in the publication, temperature not specified in the publication
0.02
(RS)-coclaurine
mutant F332A, pH not specified in the publication, temperature not specified in the publication
0.12
(RS)-coclaurine
mutant Y328A, pH not specified in the publication, temperature not specified in the publication
0.53
(RS)-coclaurine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.14
heliamine
mutant W329A, pH not specified in the publication, temperature not specified in the publication
0.2
heliamine
mutant Y328A, pH not specified in the publication, temperature not specified in the publication
0.6
heliamine
wild-type, pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
(RS)-coclaurine
mutant F332A, pH not specified in the publication, temperature not specified in the publication
0.01
(RS)-coclaurine
mutant W329A, pH not specified in the publication, temperature not specified in the publication
0.2
(RS)-coclaurine
mutant Y328A, pH not specified in the publication, temperature not specified in the publication
2
(RS)-coclaurine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.09
heliamine
mutant W329A, pH not specified in the publication, temperature not specified in the publication
0.09
heliamine
mutant Y328A, pH not specified in the publication, temperature not specified in the publication
2
heliamine
wild-type, pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000096
0.0001
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.0003
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.00065
Thalictrum glaucum
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.00066
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.0007
Corydalis vaginans
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.00075
Bocconia cordata
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.00077
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.0013
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.002
0.003
Tinospora fragosa
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
additional information
0.000096
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
0.000096
-
enzyme extract of cell culture, (S)-coclaurine, (R)coclaurine is not methylated
additional information
-
(S)-corytuberine conversion to magnoflorine shown by crude enzyme preparation of recombinant CNMT protein, magnoflorine biosynthesis by CYP80G2 protein and CjCNMT via (S)-corytuberine as an intermediate in vivo, CjCNMT protein catalyzes the crucial N-methylation step from (S)-coclaurine to (S)-N-methylcoclaurine in (S)-reticuline biosynthesis
additional information
-
analysis of inducible expression systems, production of recombinant CMT protein from PprpB promoter 2fold to 4fold higher than that from PT7 promoter, cell growth not reduced after expression form PprpB promoter even when highly induced, propionate-inducible system efficient for protein overproduction that result in growth inhibition, auto-induction experiments performed and protein production monitored
additional information
phylogenetic analysis reveales a monophyletic clade for (S)-coclaurine N-methyltransferase (CNMT) and (S)-tetrahydroprotoberberine cis-N-methyltransferase (TNMT), 48% identity of amino acid sequence, downstream metabolic role suggests that TNMT derives from gene duplication after more ancient recruitment of CNMT, phylogenetic relationship between CNMT and TNMT provides new insights into evolutionary recruitment of enzymes into plant alkaloid pathways
additional information
-
phylogenetic analysis reveales a monophyletic clade for (S)-coclaurine N-methyltransferase (CNMT) and (S)-tetrahydroprotoberberine cis-N-methyltransferase (TNMT), 48% identity of amino acid sequence, downstream metabolic role suggests that TNMT derives from gene duplication after more ancient recruitment of CNMT, phylogenetic relationship between CNMT and TNMT provides new insights into evolutionary recruitment of enzymes into plant alkaloid pathways
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
sieve elements of the phloem adjacent or proximal to laticifers. Sieve elements in the root and hypocotyl of opium poppy seedlings
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
plants exhibiting reduced CNMT transcript levels show a significant fourfold increase in the relative abundance of papaverine, and a reduction in the accumulation of thebaine and noscapine. Norlaudanine is only detected in CNMT-suppressed plants. The levels of several N-methylated compounds, including N-methylcoclaurine, N,N-dimethylcoclaurine, 4'-O-methyl-N-methylcoclaurine, reticuline, N,N-dimethylreticuline, codamine, laudanine, laudanosine and salutaridine, and four phathelideisoquinoline alkaloids (i.e. narcotoline, noscapine, N,N-dimethylnarcotine and another noscapine-like compound) are also reduced in CNMT-suppressed plants
metabolism
-
the enzyme is involved in the biosynthesis pathways of alkaloids in Papaver somniferum, overview. Subsequent 6-O-methylation, N-methylation, 3'-hydroxylation and 4'-O-methylation convert (S)-norcoclaurine to (S)-reticuline, which is a branch-point intermediate in the formation of most BIA structural sub-groups, including morphinan (e.g. morphine), phthalideisoquinoline (e.g. noscapine) and benzophenanthridine (e.g. sanguinarine) alkaloids
physiological function
-
fumisoquin biosynthesis requires the N-methyltransferase FsqC and the FAD-dependent oxidase FsqB, which represent functional analogs of coclaurine N-methyltransferase and berberine bridge enzyme in plants. Deletion of the N-methyltransferase FsqC, phenol 2-monooxygenase FsqG, or FAD-dependent oxidase FsqB in a strain overexpressing FsqA leads to complete abolishment of isoquinoline alkaloid production and accumulation of a series of benzyl pyrroles, including fumipyrrole
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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). CNMT_PAPSO
351
0
41032
Swiss-Prot
other Location (Reliability: 3)
CNMT_THLFG
361
0
41903
Swiss-Prot
other Location (Reliability: 2)
A0A5P9PAN8_9MAGN
355
0
41599
TrEMBL
other Location (Reliability: 5)
A0A5P9PAQ9_9MAGN
359
0
41084
TrEMBL
other Location (Reliability: 2)
I3S3W0_MEDTR
358
0
41799
TrEMBL
other Location (Reliability: 3)
A0A2P6Q1E6_ROSCH
355
0
41362
TrEMBL
other Location (Reliability: 5)
A0A084FVA5_PSEDA
555
1
62076
TrEMBL
Mitochondrion (Reliability: 1)
A0A5P9PAT6_9MAGN
355
0
41140
TrEMBL
other Location (Reliability: 3)
A0A2G9HVP9_9LAMI
82
0
9052
TrEMBL
other Location (Reliability: 4)
A0A5B6YUL9_DAVIN
308
0
35674
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7C8ZID1_OPUST
138
0
15671
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B4VG18_SINHE
370
0
42440
TrEMBL
other Location (Reliability: 3)
A0A5B6YSJ2_DAVIN
355
0
41098
TrEMBL
other Location (Reliability: 4)
A0A0B4VFR5_PODPE
356
0
41517
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8B6BJD2_MYTGA
340
0
39534
TrEMBL
other Location (Reliability: 1)
A0A7C8ZIJ3_OPUST
184
0
21054
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with S-adenosyl-L-homocysteine and N-methylheliamine. Molecular modeling of structure with natural substrate coclaurine.Both enantiomers of coclaurine can be accommodated in the CNMT active site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E204G
mutation to the corresponding residue of Papaver somniferum reticuline N-methyltransferase. Mutant shows a weak activity with (S)-coclaurine and a more substantial activity with (S)-N-methylcoclaurine. Compared to wild-type, activity with (S)-reticuline is 35fold improved
H208A
1% of wild-type activity with substrate heliamine, 4% with substrate coclaurine, respectively
W329A
4% of wild-type activity with substrate heliamine, 0.5% with substrate coclaurine, respectively
Y328A
5% of wild-type activity with substrate heliamine, 10% with substrate coclaurine, respectively
additional information
-
virus-induced gene silencing in opium poppy to functionally characterize six genes potentially involved in papaverine biosynthesis, e.g. the gene encoding coclaurine N-methyltransferase, altered alkaloid content phenotypes, overview. Norlaudanine is only detected in CNMT-suppressed plants
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
30-50% ammonium sulfate, Phenyl Sepharose, Q-Sepharose, Mono Q, Mono P, 343fold purification
-
40% ammonium sulfate, Phenyl Sepharose, TSK Fraktogel, Mono Q, Affinity gel, disc electrophoresis, 115fold purification
-
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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
expressed in Escherichia coli
expressed in Escherichia coli from the Salmonella enterica prpBCDE promoter, comparison to expression products derived from the strongest IPTG-inducible promoter PT7, DH10B strain used for DNA-manipulations, BLRDE3 strain host for pPro and T7 expression systems
-
expression in Escherichia coli
real-time quantitative PCR analysis of target gene transcript levels, comparison of target gene transcript levels and papaverine content in individual opium poppy plants infiltrated with Agrobacterium tumefaciens harboring control and gene-specific pTRV2 constructs
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
CNMT should be quite useful for biotransformation of the intermediates of alkaloid biosynthesis to N-methyltransferred products
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loeffler, S.; Deus-Neumann, B.; Zenk, M.H.
S-Adenosyl-L-methionine:(S)-coclaurine-N-methyltransferase from Tinospora cordifolia
Phytochemistry
38
1387-1395
1995
Berberis canadensis, Berberis koetineana, Berberis stolonifera, Bocconia cordata, Cocculus trilobus, Corydalis vaginans, Lamprocapnos spectabilis, Eschscholzia californica, Fumaria officinalis, Stephania delavayi, Thalictrum dasycarpum, Thalictrum flavum, Thalictrum glaucum, Tinospora cordifolia, Tinospora fragosa
-
brenda
Stadler, R.M.; Zenk, M.H.
A revision of the generally accepted pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline
Liebigs Ann. Chem.
1990
555-562
1990
Berberis stolonifera, Eschscholzia californica, Peumus boldus
-
brenda
Choi, K.B.; Morishige, T.; Sato, F.
Purification and characterization of coclaurine N-methyltransferase from cultured Coptis japonica cells
Phytochemistry
56
649-655
2001
Coptis japonica
brenda
Choi, K.B.; Morishige, T.; Shitan, N.; Yazaki, K.; Sato, F.
Molecular cloning and characterization of coclaurine N-methyltransferase from cultured cells of Coptis japonica
J. Biol. Chem.
277
830-835
2002
Coptis japonica
brenda
Facchini, P.J.; Park, S.U.
Developmental and inducible accumulation of gene transcripts involved in alkaloid biosynthesis in opium poppy
Phytochemistry
64
177-186
2003
Papaver somniferum (Q7XB08)
brenda
Samanani, N.; Alcantara, J.; Bourgault, R.; Zulak, K.G.; Facchini, P.J.
The role of phloem sieve elements and laticifers in the biosynthesis and accumulation of alkaloids in opium poppy
Plant J.
47
547-563
2006
Papaver somniferum
brenda
Liscombe, D.K.; Facchini, P.J.
Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy
J. Biol. Chem.
282
14741-14751
2007
Papaver somniferum (Q7XB08), Papaver somniferum
brenda
Ikezawa, N.; Iwasa, K.; Sato, F.
Molecular cloning and characterization of CYP80G2, a cytochrome P450 that catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in magnoflorine biosynthesis, from cultured Coptis japonica cells
J. Biol. Chem.
283
8810-8821
2008
Coptis japonica
brenda
Lee, S.K.; Keasling, J.D.
Heterologous protein production in Escherichia coli using the propionate-inducible pPro system by conventional and auto-induction methods
Protein Expr. Purif.
61
197-203
2008
Escherichia coli
brenda
Desgagne-Penix, I.; Facchini, P.
Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes reveals the major route to papaverine in opium poppy
Plant J.
72
331-344
2012
Papaver somniferum
brenda
Chang, L.; Hagel, J.M.; Facchini, P.J.
Isolation and characterization of O-methyltransferases involved in the biosynthesis of glaucine in Glaucium flavum
Plant Physiol.
169
1127-1140
2015
Coptis japonica (Q948P7), Coptis japonica
brenda
Pathak, S.; Lakhwani, D.; Gupta, P.; Mishra, B.; Shukla, S.; Asif, M.; Trivedi, P.
Comparative transcriptome analysis using high papaverine mutant of Papaver somniferum reveals pathway and uncharacterized steps of papaverine biosynthesis
PLoS ONE
8
e65622
2013
Papaver somniferum (Q7XB08)
brenda
Galanie, S.; Smolke, C.
Optimization of yeast-based production of medicinal protoberberine alkaloids
Microb. Cell Fact.
14
144
2015
Papaver somniferum (Q7XB08)
brenda
Bennett, M.R.; Thompson, M.L.; Shepherd, S.A.; Dunstan, M.S.; Herbert, A.J.; Smith, D.R.M.; Cronin, V.A.; Menon, B.R.K.; Levy, C.; Micklefield, J.
Structure and biocatalytic scope of coclaurine N-methyltransferase
Angew. Chem. Int. Ed. Engl.
57
10600-10604
2018
Coptis japonica (Q948P7)
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 (A0A5P9PAN8), Stephania intermedia (A0A5P9PAQ9), Stephania intermedia (A0A5P9PAT6)
brenda
Baccile, J.A.; Spraker, J.E.; Le, H.H.; Brandenburger, E.; Gomez, C.; Bok, J.W.; Macheleidt, J.; Brakhage, A.A.; Hoffmeister, D.; Keller, N.P.; Schroeder, F.C.
Plant-like biosynthesis of isoquinoline alkaloids in Aspergillus fumigatus
Nat. Chem. Biol.
12
419-424
2016
Aspergillus fumigatus
brenda
Morris, J.; Yu, L.; Facchini, P.
A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases
Phytochemistry
170
112193
2020
Coptis japonica (Q948P7)
brenda
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