Information on EC 2.1.1.103 - phosphoethanolamine N-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.103
-
RECOMMENDED NAME
GeneOntology No.
phosphoethanolamine N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
choline biosynthesis I
-
-
Glycerophospholipid metabolism
-
-
phosphatidylcholine biosynthesis II
-
-
phosphatidylcholine biosynthesis III
-
-
phosphatidylcholine biosynthesis IV
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:ethanolamine-phosphate N-methyltransferase
The enzyme may catalyse the transfer of two further methyl groups to the product.
CAS REGISTRY NUMBER
COMMENTARY hide
145539-90-8
-
171040-79-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
highest activity after prolonged light period
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
highest activity after prolonged light period
-
-
Manually annotated by BRENDA team
; gene pmt-1
-
-
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
duck weed
-
-
Manually annotated by BRENDA team
Limonium perezii
highest activity after prolonged light period
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene ZmPEAMT1; cv. Qi319, gene ZmPEAMT1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the enzyme has a central role in phosphatidylcholine biosynthesis via the methylation pathway and plays a role in cell division and inflorescence meristem
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine
choline phosphate + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
N-methylethanolamine phosphate + S-adenosyl-L-methionine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
show the reaction diagram
S-adenosyl-L-methionine + N,N-dimethylethanolamine phosphate
S-adenosyl-L-homocysteine + phosphocholine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + phosphodimethylethanolamine
S-adenosyl-L-homocysteine + phosphocholine
show the reaction diagram
S-adenosyl-L-methionine + phosphoethanolamine
S-adenosyl-L-homocysteine + methylethanolamine phosphate
show the reaction diagram
S-adenosyl-L-methionine + phosphoethanolamine
S-adenosyl-L-homocysteine + phosphocholine
show the reaction diagram
S-adenosyl-L-methionine + phosphoethanolamine
S-adenosyl-L-homocysteine + phosphomonomethylethanolamine
show the reaction diagram
S-adenosyl-L-methionine + phosphomethylethanolamine
S-adenosyl-L-homocysteine + phosphodimethylethanolamine
show the reaction diagram
S-adenosyl-L-methionine + phosphomonomethylethanolamine
S-adenosyl-L-homocysteine + phosphodimethylethanolamine
show the reaction diagram
additional information
?
-
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-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
show the reaction diagram
S-adenosyl-L-methionine + phosphoethanolamine
S-adenosyl-L-homocysteine + methylethanolamine phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amodiaquine
Chloroquine
diphenhydramine
-
i.e. 2-(diphenylmethoxy)-N,N-dimethylethanamine
dodecyltrimethylammonium
-
25% inhibition at 0.5 mM
hexadecyltrimethylammonium
-
about 50% inhibition at 0.1 mM
miltefosine
N-methylethanolamine phosphate
-
competitive inhibition versus both substrates
NSC-158011
competitive inhibitor
-
NSC158011
-
phosphate
-
-
phosphocholine
primaquine
-
-
S-adenosyl-L-homocysteine
sinefungin
tacrine
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i.e. 1,2,3,4-tetrahydroacridin-9-amine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
removal of EDTA leads to 60% loss of activity
glutathione
-
removal of glutathione leads to almost complete loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0099 - 21.17
Ethanolamine phosphate
0.03 - 0.786
N,N-dimethylethanolamine phosphate
0.16
N-methylethanolamine phosphate
pH and temperature not specified in the publication
0.0668 - 0.217
phosphodimethylethanolamine
0.0542 - 0.106
Phosphoethanolamine
0.181 - 0.424
phosphomonomethylethanolamine
0.0299 - 0.277
S-adenosyl-L-methionine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 1.82
Ethanolamine phosphate
0.367 - 3.08
N,N-dimethylethanolamine phosphate
3.08 - 4.13
phosphodimethylethanolamine
1.82 - 8.63
Phosphoethanolamine
3.63 - 4.9
phosphomonomethylethanolamine
0.058 - 5.82
S-adenosyl-L-methionine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00025 - 33.64
Ethanolamine phosphate
1866
0.474 - 17.04
N,N-dimethylethanolamine phosphate
15853
19.05 - 46.16
phosphodimethylethanolamine
4555
33.52 - 81.45
Phosphoethanolamine
1797
11.56 - 20.07
phosphomonomethylethanolamine
5203
8.24 - 22.72
S-adenosyl-L-methionine
24
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.23 - 5.11
N-methylethanolamine phosphate
5 - 7.81
phosphocholine
0.0048 - 0.0091
S-adenosyl-L-homocysteine
additional information
additional information
-
product inhibition patterns are indicative of a random sequential Bi Bi kinetic mechanism
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 3.4
amodiaquine
0.146 - 0.554
Chloroquine
0.013
diphenhydramine
Haemonchus contortus
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isozyme PMT2, in 0.1 M HEPES (pH 8.0), 2 mM Na2EDTA, 10% glycerol, at 25°C
0.0125 - 0.1252
miltefosine
0.0008
NSC-22225
Plasmodium falciparum
Q8IDQ9
at pH 8.6 and 37°C
-
0.005
NSC-39225
Plasmodium falciparum
Q8IDQ9
at pH 8.6 and 37°C
-
0.05 - 0.099
NSC158011
-
0.46
primaquine
Plasmodium falciparum
-
pH and temperature not specified in the publication
0.0338 - 0.0915
sinefungin
3.5 - 23.4
tacrine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0085
-
with phosphodimethylethanolamine as substrate
0.013
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with phosphoethanolamine as substrate
0.189
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8.5
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-
8.6
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.3
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
calculated from sequence
5.3
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isozyme PMT1, calculated from amino acid sequence
5.5
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isozyme PMT2, calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
1 * 48000, isozyme PMT2, SDS-PAGE
49400
-
1 * 49400, isozyme PMT2, calculated from amino acid sequence
51900
-
isozyme PMT2, gel filtration
52000
-
1 * 52000, SDS-PAGE
52300
-
isozyme PMT1, gel filtration
53100
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1 * 53100, isozyme PMT1, calculated from amino acid sequence
54000
-
SDS-PAGE
55000
-
1 * 55000, isozyme PMT1, SDS-PAGE
55100
-
calculated from sequence
56100
-
calculated from DNA sequence
65000
SDS-PAGE, enzyme from E. coli, contains of 57 kD enzyme protein + 8 kD His-tag
77000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D128A mutant in complex with S-adenosylhomocysteine and either phosphoethanolamine or phosphocholine, hanging drop vapor diffusion method, using 20% (w/v) PEG 8000, 0.1 M sodium cacodylate (pH 6.5), 0.2 M sodium acetate, 20 mM tris(2-carboxyethyl)phosphine, and 5 mM S-adenosyl-L-homocysteine
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in complex with amodiaquine, hanging drop vapor diffusion method
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in complex with either S-adenosyl-L-methionine (1), phosphoethanolamine (2), phosphocholine (3), sinefungin (4), or both phosphoethanolamine and S-adenosylhomocysteine (5), hanging drop vapor diffusion method, using (1) 20% (w/v) PEG-8000, 0.1 M sodium cacodylate, pH 6.5, 0.2 M sodium acetate, 20 mM tris(2-carboxyethyl) phosphine, or (2-5) 20-30% (w/v) PEG8000, 0.1 M sodium cacodylate,pH 6.5, 0.2 M sodium acetate, 5 mM 2-mercaptoethanol
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hanging drop vapor diffusion method, using 100 mM Na-acetate (pH 5.0), and 20% (w/v) PEG 3350
sitting drop vapor diffusion method, using 200 mM NH4-formate and 20% (w/v) PEG 3350
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant His6-tagged PMT from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, the tag is cleaved off by thrombin, followed by benzamidine adsorption chromatography, and gel filtration
-
from E. coli, His-tag used for affinity chromatography
Ni-NTA agarose column chromatography and Superdex 75 gel filtration
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Ni-NTA column chromatography, gel filtration
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Ni2+-nitrilotriacetic acid-agarose resin column chromatography and Superdex-200 gel filtration
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nickel affinity column chromatography; purification of the recombinant protein by affinity chromatography is found to be problematic and subject to losses in enzyme activity. The inclusion of DTT, BSA, and EDTA prevents the loss of enzyme activity during elution from a nickel ion matrix
nickel HisTrap column chromatography and Superdex 75PG gel filtration
nickel-affinity column chromatography and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli by affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-Codon-Plus cells
-
expressed in Escherichia coli BL21-CodonPlus cells
-
expressed in Escherichia coli Rosetta II(DE3) pLysS cells
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expressed in Escherichia coli; expressed in Saccharomyces cerevisiae strain CPBY19 (cho2, opi3 mutant) and in Escherichia coli BL21 (DE3) cells
expression in Escherichia coli; gene pmt-1, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
-
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
expression of wild-type and mutant enzymes in Escherichia coli, and complementation study using the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview
gene PfPMT, expression analysis
-
gene ZmPEAMT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression and promoter analysis: the upstream promoter sequence of ZmPEAMT1 contains four kinds of putative cis-acting regulatory elements, including stress-responsive elements, phytohormone-responsive elements, pollen developmental special activation elements, and light-induced signal transduction elements, overview, overexpression in transgenic Arabidopsis thaliana plants
generation of trangenic Arabidopsis calli that express a chimeric gene construct by fusing the 5'-UTR of the Arabidopsis PEAMT gene (AtNMT1) upstream of the beta-glucuronidase gene
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generation of transgenic tobacco plants
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in Escherichia coli
in Saccharomyces cerevisiae opi3
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in Schizosaccharomyces pombe
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tobacco transformed with spinach cDNA
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via RNA isolated from different blood stages
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D110A
-
the mutant shows about 37% of wild type activity
D110N
-
the mutant shows about 80% of wild type activity
D128Q
-
compared to the wild type enzyme, the mutant shows almost complete loss of activity with phosphoethanolamine but not with the final substrate of the methylation pathway (about 89% activity)
D61E
site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview
D85A
-
inactive
D85N
-
inactive
G153A
site-directed mutagenesis, the PfPMT mutant complements the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview
G63A
site-directed mutagenesis, the PfPMT mutant complements the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview
G83A
site-directed mutagenesis, inactive mutant, which fails to complement the mutant Saccharomyces cerevisiae strain pem1DELTApem2DELTA, overview
H132A
-
inactive
H132N
-
inactive
H132Q
-
inactive
I86A
-
the mutant shows about 10% of wild type activity
I86F
-
the mutant shows about 16% of wild type activity
K247A
-
inactive
K247M
-
inactive
Q18N
-
the mutant shows about 20% of wild type activity
R179A
-
inactive; the mutant shows about 5% of wild type activity
R179K
-
the mutant shows about 45% of wild type activity
S37A
-
the mutant shows about 85% of wild type activity
Y160A
-
inactive
Y160F
-
inactive
Y175A
-
the mutant shows about 10% of wild type activity
Y175F
-
the mutant shows about 9% of wild type activity
Y181A
-
the mutant shows about 7% of wild type activity
Y181F
-
the mutant shows about 5% of wild type activity
Y19A
-
inactive
Y19F
-
the mutant shows about 30% of wild type activity
Y27A
-
the mutant shows about 5% of wild type activity
Y27F
-
the mutant shows about 8% of wild type activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the enzyme is a potential target for development of inhibitors
medicine
-
the enzyme is an antiparasitic target