Information on EC 2.1.1.49 - amine N-methyltransferase

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The expected taxonomic range for this enzyme is: Eutheria

EC NUMBER
COMMENTARY
2.1.1.49
-
RECOMMENDED NAME
GeneOntology No.
amine N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
beta-alanine betaine biosynthesis
-
nicotine degradation IV
-
Tryptophan metabolism
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:amine N-methyltransferase
An enzyme of very broad specificity; many primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aromatic alkylamine-N-methyltransferase
-
-
arylamine N-methyltransferase
-
-
-
-
methyltransferase, tryptamine
-
-
-
-
nicotine N-methyltransferase
-
-
-
-
tryptamine methyltransferase
-
-
-
-
tryptamine N-methyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
51377-47-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
amine N-methyltransferase A
-
-
Manually annotated by BRENDA team
amine N-methyltransferase A and B; strain New Zealand, 10-16 week old
-
-
Manually annotated by BRENDA team
strain New Zealand, 10-16 week old
-
-
Manually annotated by BRENDA team
Oryctolagus cuniculus New Zealand
strain New Zealand, 10-16 week old
-
-
Manually annotated by BRENDA team
rats with common bile duct ligation and obstructive jaundice respectively; Sprague-Dawley strain male rats
-
-
Manually annotated by BRENDA team
Sprague-Dawley strain male rats
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 1,2,3,4-tetrahydroisoquinoline
S-adenosyl-L-homocysteine + N-methyl-1,2,3,4-tetrahydroisoquinoline
show the reaction diagram
-
amine N-methyltransferase A
-
?
S-adenosyl-L-methionine + 5-methyloxytryptamine
?
show the reaction diagram
-
higher activity with transferase A
-
-
?
S-adenosyl-L-methionine + 7,8-dichloro-1,2,3,4-tetrahydroisoquinoline
?
show the reaction diagram
-
substrate with highest apparent kcat
-
-
?
S-adenosyl-L-methionine + alpha-N-methyltryptamine
S-adenosyl-L-homocysteine + alpha,alpha-N,N-dimethyltryptamine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + alpha-N-methyltryptamine
S-adenosyl-L-homocysteine + alpha,alpha-N,N-dimethyltryptamine
show the reaction diagram
-
-
no methylation of indolic nitrogen
?
S-adenosyl-L-methionine + alpha-N-methyltryptamine
S-adenosyl-L-homocysteine + alpha,alpha-N,N-dimethyltryptamine
show the reaction diagram
-
-
N,N-dimethyltryptamine as product
?
S-adenosyl-L-methionine + alpha-N-methyltryptamine
S-adenosyl-L-homocysteine + alpha,alpha-N,N-dimethyltryptamine
show the reaction diagram
Oryctolagus cuniculus New Zealand
-
-
no methylation of indolic nitrogen
?
S-adenosyl-L-methionine + alpha-N-methyltryptamine
S-adenosyl-L-homocysteine + alpha,alpha-N,N-dimethyltryptamine
show the reaction diagram
Oryctolagus cuniculus New Zealand
-
-
-
-
?
S-adenosyl-L-methionine + an amine
S-adenosyl-L-homocysteine + an N-methylamine
show the reaction diagram
-
enzymes participate in detoxication, recycling of drugs after initial demethylation
-
-
?
S-adenosyl-L-methionine + an amine
S-adenosyl-L-homocysteine + an N-methylamine
show the reaction diagram
-
xenobiotic biotransforming enzyme, enzyme is leaked easily into the blood stream due to an increased membrane permeability of hepatocytes caused by cholestasis
-
-
?
S-adenosyl-L-methionine + aniline
?
show the reaction diagram
-
poor substrate
-
-
?
S-adenosyl-L-methionine + anisidine
?
show the reaction diagram
-
higher activity with transferase B
-
-
?
S-adenosyl-L-methionine + beta-phenylethylamine
?
show the reaction diagram
-
5-methyltetrahydrofolate can replace S-adenosyl-L-methionine as methyl donor
-
-
?
S-adenosyl-L-methionine + desmethylimipramine
?
show the reaction diagram
Oryctolagus cuniculus, Oryctolagus cuniculus New Zealand
-
higher activity with transferase A
-
-
?
S-adenosyl-L-methionine + imidazole
?
show the reaction diagram
-
higher activity with transferase A
-
-
?
S-adenosyl-L-methionine + isosalsoline
S-adenosyl-L-homocysteine + N-methylisosalsoline
show the reaction diagram
-
isosalsoline is identical with 7-hydroxy-6-methoxy-1-methyl-1,2,3,4-tetrahydroisoquinoline, stereospecific N-methylation by amine N-methyltransferase A, (+)-(R)-enantiomer is preferentially methylated
-
?
S-adenosyl-L-methionine + N-methylbutylamine
S-adenosyl-L-homocysteine + N,N-dimethylbutylamine
show the reaction diagram
-
only transferase A
-
-
?
S-adenosyl-L-methionine + N-methylcyclohexylamine
S-adenosyl-L-homocysteine + N,N-dimethylcyclohexylamine
show the reaction diagram
-
only transferase A
-
-
?
S-adenosyl-L-methionine + N-methyltryptamine
S-adenosyl-L-homocysteine + N,N-dimethyltryptamine
show the reaction diagram
Oryctolagus cuniculus, Oryctolagus cuniculus New Zealand
-
-
-
-
?
S-adenosyl-L-methionine + phenyltetrahydropyridine
?
show the reaction diagram
-
higher activity with transferase A
-
-
?
S-adenosyl-L-methionine + pyrazole
?
show the reaction diagram
-
higher activity with transferase A
-
-
?
S-adenosyl-L-methionine + salsolidine
S-adenosyl-L-homocysteine + N-methylsalsolidine
show the reaction diagram
-
salsolidine is identical with 6,7-dimethoxy-1-methyl-1,2,3,4-tetrahydroisoquinoline, stereospecific N-methylation by amine N-methyltransferase A, (-)-(S)-enantiomer is preferentially methylated
-
?
S-adenosyl-L-methionine + tryptamine
S-adenosyl-L-homocysteine + alpha-N-methyltryptamine
show the reaction diagram
-
two N-methyltransferases, non-specific or specific for tryptamine, 5-methyltetrahydrofolate can replace S-adenosyl-L-methionine as methyl donor
-
?
S-adenosyl-L-methionine + tryptamine
S-adenosyl-L-homocysteine + alpha-N-methyltryptamine
show the reaction diagram
-
S-adenosyl-L-methionine-dependent enzyme
-
?
S-adenosyl-L-methionine + tryptamine
S-adenosyl-L-homocysteine + alpha-N-methyltryptamine
show the reaction diagram
-
i.e. 3-[2-aminoethyl] indole, best substrate, two N-methyltransferases: A and B, non-specific
-
?
S-adenosyl-L-methionine + tryptamine
S-adenosyl-L-homocysteine + alpha-N-methyltryptamine
show the reaction diagram
-
i.e. 3-[2-aminoethyl] indole, best substrate, two N-methyltransferases: A and B, non-specific
-
-
?
S-adenosyl-L-methionine + tryptamine
S-adenosyl-L-homocysteine + alpha-N-methyltryptamine
show the reaction diagram
-
i.e. 3-[2-aminoethyl] indole, best substrate, two N-methyltransferases: A and B, non-specific
-
?
S-adenosyl-L-methionine + tryptamine
S-adenosyl-L-homocysteine + alpha-N-methyltryptamine
show the reaction diagram
Oryctolagus cuniculus New Zealand
-
i.e. 3-[2-aminoethyl] indole, best substrate, two N-methyltransferases: A and B, non-specific
-
-
?
S-adenosyl-L-methionine + tryptamine
S-adenosyl-L-homocysteine + alpha-N-methyltryptamine
show the reaction diagram
Oryctolagus cuniculus New Zealand
-
i.e. 3-[2-aminoethyl] indole, best substrate, two N-methyltransferases: A and B, non-specific
-
?
(R)-isosalsoline + methyl group donor
N-methyl-(R)-isosalsoline + demethylated methyl group donor
show the reaction diagram
-
-
N-methyl-(R)-isosalsoline is enzymatically formed in liver and can be transported into the brain from blood, it may act as neurotransmitter
?
additional information
?
-
Oryctolagus cuniculus, Oryctolagus cuniculus New Zealand
-
two N-methyltransferases A and B with very broad but overlapping substrate specificity for primary and secondary amines, lipophilic substrates, overview poor substrates, no substrates: N-acetylserotonine, 4-aminoacetophenone, 4-aminophenol, benzamide, 4-chloroaniline, deoxyepinephrine, 1,4-diaminobutane, dopamine, 1-ethanol-2-amine, ethylenediamine, histamine, histidine methylester, 3-hydroxytryptamine, indole, pyrrole, methylamine, N-methyldopamine, nicotinamide, octopamine, phenylalanine, phenylethanolamine, theophylline, tryptophan, tyrosine, N,N-dimethyltryptamine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-isosalsoline + methyl group donor
N-methyl-(R)-isosalsoline + demethylated methyl group donor
show the reaction diagram
-
-
N-methyl-(R)-isosalsoline is enzymatically formed in liver and can be transported into the brain from blood, it may act as neurotransmitter
?
S-adenosyl-L-methionine + an amine
S-adenosyl-L-homocysteine + an N-methylamine
show the reaction diagram
-
enzymes participate in detoxication, recycling of drugs after initial demethylation
-
-
?
S-adenosyl-L-methionine + an amine
S-adenosyl-L-homocysteine + an N-methylamine
show the reaction diagram
-
xenobiotic biotransforming enzyme, enzyme is leaked easily into the blood stream due to an increased membrane permeability of hepatocytes caused by cholestasis
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
N,N-Dimethyltryptamine
-
competitive inhibitor
additional information
-
substrate inhibition, but not by tryptamine and 7,8-dichloro-1,2,3,4-tetrahydroisoquinoline
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
biosynthesis of enzyme is induced in response to obstructive jaundice
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01
-
7,8-dichloro-1,2,3,4-tetrahydroisoquinoline
-
transferase A, pH 7.6
2
-
7,8-dichloro-1,2,3,4-tetrahydroisoquinoline
-
transferase B, pH 7.6
7.6
-
Aniline
-
transferase A, pH 7.6
7.8
-
Aniline
-
transferase B, pH 7.6
6.25
-
beta-phenylethylamine
-
5-methyltetrahydrofolate as methyl donor
0.24
-
desmethylimipramine
-
transferase B, pH 8.5
0.3
-
desmethylimipramine
-
transferase A, pH 8.5
0.2
-
imidazole
-
transferase A, pH 8.5
5.1
-
imidazole
-
transferase B, pH 8.5
1.5
-
pyrazole
-
transferase A, pH 7.6
3.2
-
pyrazole
-
transferase B, pH 7.6
0.015
-
S-adenosyl-L-methionine
-
1 mM tryptamine as methyl acceptor, pH 8.5
0.12
-
tryptamine
-
transferase B, pH 8.5
0.3
-
tryptamine
-
transferase A, pH 8.5
8.3
-
tryptamine
-
5-methyltetrahydrofolate as methyl donor
28.3
-
tryptamine
-
mitochondrial enzyme, cholestatic liver, S-adenosyl-L-methionine
32.5
-
tryptamine
-
mitochondrial enzyme, control liver, S-adenosyl-L-methionine
34.1
-
tryptamine
-
microsomal enzyme, cholestatic liver, S-adenosyl-L-methionine
35.6
-
tryptamine
-
microsomal enzyme, control liver, S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.667
-
7,8-dichloro-1,2,3,4-tetrahydroisoquinoline
-
transferase A, pH 7.6
3.67
-
7,8-dichloro-1,2,3,4-tetrahydroisoquinoline
-
transferase B, pH 7.6
0.0333
-
Aniline
-
transferase A, pH 7.6
0.367
-
Aniline
-
transferase B, pH 7.6
0.0333
-
desmethylimipramine
-
transferase B, pH 8.5
0.233
-
desmethylimipramine
-
transferase A, pH 8.5
0.0833
-
imidazole
-
transferase A, pH 8.5
0.167
-
imidazole
-
transferase B, pH 8.5
0.1
-
pyrazole
-
transferase B, pH 7.6
0.25
-
pyrazole
-
transferase A, pH 7.6
0.117
-
S-adenosyl-L-methionine
-
transferase B, pH 8.5
0.2
-
S-adenosyl-L-methionine
-
transferase A, pH 8.5
0.4
-
tryptamine
-
transferase A, pH 8.5
0.45
-
tryptamine
-
transferase B, pH 8.5
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.006
-
N,N-Dimethyltryptamine
-
N-methyltransferase B
0.01
-
N,N-Dimethyltryptamine
-
N-methyltransferase A
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8e-07
-
-
beta-phenylethylamine + S-adenosyl-L-methionine
1.18e-06
-
-
tryptamine + S-adenosyl-L-methionine
1.2e-06
-
-
N-methyltransferase A, (-)-(S)-isosalsoline
2.1e-06
-
-
N-methyltransferase A, (-)-(S)-salsolidine
3.3e-06
-
-
N-methyltransferase A, (+)-(R)-isosalsoline
6.5e-05
-
-
beta-phenylethylamine + 5-methyltetrahydrofolate
6.8e-05
-
-
N-methyltransferase A, aniline
0.000198
-
-
tryptamine + 5-methyltetrahydrofolate
0.00022
-
-
N-methyltransferase B, desmethylimipramine
0.00026
-
-
N-methyltransferase A, desmethylimipramine
0.00044
-
-
N-methyltransferase A, tryptamine
0.00127
-
-
N-methyltransferase B, aniline
0.0031
-
-
N-methyltransferase B, tryptamine
additional information
-
-
specific activities of serum, control and cholestatic liver in cytosolic, mitochondrial and microsomal preparations for 0.5, 1, 2, 3, 7, 14, 28 and 42 days after common bile duct ligation, activities of mitochondrial and microsomal enzyme in cholestatic liver and of serum enzyme increase after common bile duct ligation, Vmax-values
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7
-
5-methyltetrahydrofolate as donor
7.9
-
-
S-adenosyl-L-methionine as donor
additional information
-
-
transferase A: pI 4.9, transferase B: pI 5.1
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
8.9
-
tryptamine, about half-maximal activity at pH 7.2 and 8.9, transferase A
7.5
8.8
-
tryptamine, about half-maximal activity at pH 7.5 and 90% at pH 8.8, transferase B
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
two amine N-methyltransferases, A and B
Manually annotated by BRENDA team
-
investigation of enzyme in cholestatic liver, induced by common bile duct ligation for a period of 42 days
Manually annotated by BRENDA team
Oryctolagus cuniculus New Zealand
-
two amine N-methyltransferases, A and B; two amine N-methyltransferases, A and B
-
Manually annotated by BRENDA team
Oryctolagus cuniculus New Zealand
-
-
-
Manually annotated by BRENDA team
-
investigation of enzyme in serum, after common bile duct ligation for a period of 42 days
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
hepatic membrane-bound enzyme
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
-
-
gel filtration
additional information
-
-
amino acid composition of transferase A
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 30000, SDS-PAGE
monomer
Oryctolagus cuniculus New Zealand
-
1 * 30000, SDS-PAGE
-
additional information
-
aggregation upon denaturation leads to 60 kDa and 90 kDa fractions
additional information
Oryctolagus cuniculus New Zealand
-
aggregation upon denaturation leads to 60 kDa and 90 kDa fractions
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2
-
-
optimal for transferase A
7.8
-
-
optimal for transferase B
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80°C, partially purified, per month, less than 10% loss of activity
-
-80°C, purified, per month, about 25% loss of activity
-
2°C, per week, 25% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
amine N-methyltransferase A
-
two N-methyltransferases A and B separable by ammonium sulfate fractionation, HPLC-ion exchange chromatography
-