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Information on EC 2.1.1.103 - phosphoethanolamine N-methyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q944H0
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2.1.1.103 phosphoethanolamine N-methyltransferaseIUBMB Comments
The enzyme may catalyse the transfer of two further methyl groups to the product.
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Word Map
- 2.1.1.103
- phosphatidylcholine
- phosphocholine
- choline
- phospholipid
- plasmodium
- falciparum
- malaria
- betaine
- s-adenosylhomocysteine
-
plant-like
-
osmoprotectant
- cdp-choline
-
s-adenosylmethionine-dependent
-
transmethylation
- medicine
-
halophyte
-
s-adenosyl-l-methionine-dependent
-
nematicide
- amodiaquine
- drug development
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
pfpmt, peamt, phosphoethanolamine n-methyltransferase, phosphoethanolamine methyltransferase, pmt-1, atnmt1, pmeamt, s-adenosyl-l-methionine:phosphoethanolamine n-methyltransferase, peamt1, phosphomethylethanolamine n-methyltransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphodimethylethanolamine methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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
145539-90-8
-
171040-79-2
-
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
ethanolamine phosphate + S-adenosyl-L-methionine
N-methylethanolamine phosphate + S-adenosyl-L-homocysteine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine
choline phosphate + S-adenosyl-L-homocysteine
N-methylethanolamine phosphate + S-adenosyl-L-methionine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + 2-(methylamino)ethyl phosphate
S-adenosyl-L-homocysteine + 2-(dimethylamino)ethyl phosphate
-
-
-
?
S-adenosyl-L-methionine + phosphodimethylethanolamine
S-adenosyl-L-homocysteine + phosphocholine
-
-
-
?
ethanolamine phosphate + S-adenosyl-L-methionine
N-methylethanolamine phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine
choline phosphate + S-adenosyl-L-homocysteine
N-methylethanolamine phosphate + S-adenosyl-L-methionine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + 2-(methylamino)ethyl phosphate
S-adenosyl-L-homocysteine + 2-(dimethylamino)ethyl phosphate
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
S-adenosyl-L-methionine + phosphodimethylethanolamine
S-adenosyl-L-homocysteine + phosphocholine
-
-
?
ethanolamine phosphate + S-adenosyl-L-methionine
N-methylethanolamine phosphate + S-adenosyl-L-homocysteine
-
-
-
?
ethanolamine phosphate + S-adenosyl-L-methionine
N-methylethanolamine phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine
choline phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine
choline phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N-methylethanolamine phosphate + S-adenosyl-L-methionine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N-methylethanolamine phosphate + S-adenosyl-L-methionine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine
choline phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine
choline phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N-methylethanolamine phosphate + S-adenosyl-L-methionine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
-
-
-
?
N-methylethanolamine phosphate + S-adenosyl-L-methionine
N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
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-
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in production of free choline
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
main step in phosphocholine biosynthesis. Inhibition of phosphocholine biosynthesis in xpl1 mutants not only alters several root developmental traits but also induces cell death in root epidermal cells
-
-
?
additional information
?
-
-
the enzyme cannot use phosphoethanolamine as substrate
-
-
?
additional information
?
-
the enzyme cannot use phosphoethanolamine as substrate
-
-
?
additional information
?
-
the two NMT2 isoforms have the in vitro capacity to catalyze the triple methylation of phosphoethanolamine to produce choline phosphate, but with different efficiencies
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-
-
additional information
?
-
-
the two NMT2 isoforms have the in vitro capacity to catalyze the triple methylation of phosphoethanolamine to produce choline phosphate, but with different efficiencies
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-
-
additional information
?
-
-
PMEAMT cannot use phosphoethanolamine as a substrate, but assays using phosphomethylethanolamine as a substrate result in both phosphodimethylethanolamine and phosphocholine as products. PMEAMT is inhibited by the reaction products PCho and S-adenosyl-L-homocysteine
-
-
?
additional information
?
-
PMEAMT cannot use phosphoethanolamine as a substrate, but assays using phosphomethylethanolamine as a substrate result in both phosphodimethylethanolamine and phosphocholine as products. PMEAMT is inhibited by the reaction products PCho and S-adenosyl-L-homocysteine
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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-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in production of free choline
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
main step in phosphocholine biosynthesis. Inhibition of phosphocholine biosynthesis in xpl1 mutants not only alters several root developmental traits but also induces cell death in root epidermal cells
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphocholine
47% activity in the presence of 1 mM, 17% activity in the presence of 5 mM
S-adenosyl-L-homocysteine
73% activity in the presence of 0.01 mM, 18% activity in the presence of 0.2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.408
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.653
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.577
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.212
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.308
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.156
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.284
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.03
N,N-dimethylethanolamine phosphate
pH and temperature not specified in the publication
0.249
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.507
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.16
N-methylethanolamine phosphate
pH and temperature not specified in the publication
0.201
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.278
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.069
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.0897
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.093
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.215
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.27
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.21
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.21
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.27
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.09
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.21
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.04
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.22
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.04
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.14
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.03
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.06
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.13
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.17
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.658
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.408
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.367
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.866
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
1.006
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.305
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
1.314
Ethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.161
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.433
N,N-dimethylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.209
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.489
N-methylethanolamine phosphate
pH 8.0, temperature not specified in the publication
0.266
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.767
S-adenosyl-L-methionine
cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication
0.897
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
1.453
S-adenosyl-L-methionine
cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the isoforms NMT1/NMT3 double knock-out mutant is viable. This is enabled by residual phosphoethanolamine N-methyltransferase activity through isoform NMT2. The triple NMT1/NMT2/NMT3 knock-out mutant cannot synthesize phosphatidylcholine from phosphoethanolamine and is lethal. Through alternative use of its promoter, NMT2 encodes two phosphoethanolamine N-methyltransferase variants, which greatly differ in their ability to perform the initial phosphobase methylation of phosphoethanolamine
malfunction
Arabidopsis pmeamt T-DNA mutant (atpmeamt) lacks transcripts associated with PMEAMT but has no overt phenotype. The leaf membrane phospholipid profiles show a greater content of PtdMEA as the 34:3 lipid molecular species in atpmeamt plants relative to wild type
physiological function
physiological function
enzyme can rescue a choline auxotroph of yeast
physiological function
isoform NMT1 is essential for normal growth and salt tolerance. The NMT1 mutant displays a short root phenotype under normal growth conditions and hypersensitivity, as determined by root length, under salt-stress conditions
physiological function
loss of function of DPR2/PEAMT1 affects root stem cell niche, division zone, elongation and differentiation zone. PIN-FORMED (PIN) protein abundance, PIN2 polar distribution and general endocytosis are impaired in the root tip of the mutant. Excess hydrogen peroxide and auxin accumulate in the elongation and differentiation zone, leading to root apical meristem consumption by accelerating cell differentiation
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in complex with S-adenosyl-L-methionine, to 1.5 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Arabidopsis mutant strain t365 with silenced gene for EC 2.1.1.103 enzyme shows pale green leaves, early senescence, temperature-sensitive male sterility and hypersensitivity to salt stress
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain CPBY19 (cho2, opi3 mutant) and in Escherichia coli BL21 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bolognese, C.P.; McGraw, P.
The isolation and characterization in yeast of a gene for Arabidopsis S-adenosylmethionine:phospho-ethanolamine N-methyltransferase
Plant Physiol.
124
1800-1813
2000
Arabidopsis thaliana (Q9FR44)
Mou, Z.; Wang, X.; Fu, Z.; Dai, Y.; Han, C.; Ouyang, J.; Bao, F.; Hu, Y.; Li, J.
Silencing of phosphoethanolamine N-methyltransferase results in temperature-sensitive male sterility and salt hypersensitivity in Arabidopsis
Plant Cell
14
2031-2043
2002
Arabidopsis thaliana (Q9FR44)
Cruz-Ramirez, A.; Lopez-Bucio, J.; Ramirez-Pimentel, G.; Zurita-Silva, A.; Sanchez-Calderon, L.; Ramirez-Chavez, E.; Gonzalez-Ortega, E.; Herrera-Estrella, L.
The xipotl mutant of Arabidopsis reveals a critical role for phospholipid metabolism in root system development and epidermal cell integrity
Plant Cell
16
2020-2034
2004
Arabidopsis thaliana
BeGora, M.D.; Macleod, M.J.; McCarry, B.E.; Summers, P.S.; Weretilnyk, E.A.
Identification of phosphomethylethanolamine N-methyltransferase from Arabidopsis and its role in choline and phospholipid metabolism
J. Biol. Chem.
285
29147-29155
2010
Arabidopsis thaliana, Arabidopsis thaliana (Q944H0)
Lee, S.G.; Jez, J.M.
Conformational changes in the di-domain structure of Arabidopsis phosphoethanolamine methyltransferase leads to active-site formation
J. Biol. Chem.
292
21690-21702
2017
Arabidopsis thaliana (Q944H0), Arabidopsis thaliana (Q9C6B9), Arabidopsis thaliana (Q9FR44)
Zou, Y.; Zhang, X.; Tan, Y.; Huang, J.B.; Zheng, Z.; Tao, L.Z.
Phosphoethanolamine N-methyltransferase 1 contributes to maintenance of root apical meristem by affecting ROS and auxin-regulated cell differentiation in Arabidopsis
New Phytol.
224
258-273
2019
Arabidopsis thaliana (Q9FR44)
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