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EC Tree
IUBMB Comments The enzyme also catalyses the transfer of a further methyl group, producing phosphatidylcholine.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
phospholipid methyltransferase, methyltransferase ii, pemt-l, pemt-s, phosphatidyl-n-methylethanolamine methyltransferase, phosphatidylethanolamine methyltransferase i, phosphatidylmonomethylethanolamine methyltransferase, phosphatidyl-n-methylethanolamine n-methyltransferase,
more
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methyltransferase II
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PEMT-L
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longer isoform of PEMT
PEMT-S
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shorter isoform of PEMT
phosphatidyl-N-methylethanolamine methyltransferase
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phosphatidyl-N-monomethylethanolamine methyltransferase
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phosphatidylethanolamine methyltransferase I
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phosphatidylethanolamine N-methyltransferase
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phosphatidylmonomethylethanolamine methyltransferase
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phospholipid methyltransferase
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phospholipid N-methyltransferase
class I PLMT
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phospholipid N-methyltransferase
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phospholipid N-methyltransferase
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PLMT
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S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
the enzyme also catalyzes the transfer of a further methyl group, producing phosphatidylcholine
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methyl group transfer
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S-adenosyl-L-methionine:phosphatidyl-N-methylethanolamine N-methyltransferase
The enzyme also catalyses the transfer of a further methyl group, producing phosphatidylcholine.
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2 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
S-adenosyl-L-methionine + dipalmitoylphosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + dipalmitoylphosphatidylcholine
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?
S-adenosyl-L-methionine + dipalmitoylphosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + dipalmitoylphosphatidyl-N,N-dimethylethanolamine dipalmitoylphosphatidyl-N-methylethanolamine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
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S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-monomethylethanolamine
additional information
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2 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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2 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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2 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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2 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
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S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
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S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
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S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
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S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-monomethylethanolamine
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S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-monomethylethanolamine
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S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-monomethylethanolamine
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additional information
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cannot utilize phosphatidyl-N-ethanolamine as a substrate
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additional information
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enzyme methylates only exogenously added mono-and dimethyl derivatives of phosphatidylethanolamine, but not phosphatidylethanolamine
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additional information
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cannot utilize phosphatidyl-N-ethanolamine as a substrate
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Ca2+
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leads to a stimulation of activity
Mg2+
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requires magnesium ions for full activity
Mg2+
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leads to a stimulation of activity
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adriamycin
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doxorubicin, antitumor drug
p-chloromercuriphenylsulfonic acid
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phosphatidylcholine
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inhibits the incorporation of [3H]-methyl groups from S-adenosyl-L-methionine into phosphatidyl-N-monomethylethanolamine and phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine
S-adenosyl-L-homocysteine
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competitive inhibition
S-adenosyl-L-homocysteine
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Triton X-100
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Colonic Neoplasms
1,2-Dimethylhydrazine-induced premalignant alterations in the S-adenosylmethionine/S-adenosylhomocysteine ratio and membrane lipid lateral diffusion of the rat distal colon.
Leukemia
Differences in activity of N2-guanine tRNA methyltransferase II among several inbred strains of mice.
Leukemia
Rat basophilic leukemia cell lines defective in phospholipid methyltransferase enzymes, Ca2+ influx, and histamine release: reconstitution by hybridization.
Sarcoidosis, Pulmonary
[Methylation of membrane phospholipids of alveolar macrophages in pulmonary sarcoidosis and diffuse interstitial pulmonary fibrosis]
Virus Diseases
Effect of Friend virus infection on the biosynthetic enzymes of phosphatidylcholine biosynthesis in spleen microsomes.
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0.059 - 0.18
phosphatidyl-N-dimethylethanolamine
0.054 - 0.38
phosphatidyl-N-monomethylethanolamine
0.016 - 0.1
S-adenosyl-L-methionine
0.059
phosphatidyl-N-dimethylethanolamine
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0.18
phosphatidyl-N-dimethylethanolamine
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0.054
phosphatidyl-N-monomethylethanolamine
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0.067
phosphatidyl-N-monomethylethanolamine
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0.08
phosphatidyl-N-monomethylethanolamine
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0.38
phosphatidyl-N-monomethylethanolamine
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0.016
S-adenosyl-L-methionine
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substrate phosphatidyl-N,N-dimethylethanolamine
0.022
S-adenosyl-L-methionine
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0.037
S-adenosyl-L-methionine
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pH 8.5
0.038
S-adenosyl-L-methionine
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pH 10.0
0.1
S-adenosyl-L-methionine
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0.0049 - 0.32
S-adenosyl-L-homocysteine
0.0049
S-adenosyl-L-homocysteine
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0.0067
S-adenosyl-L-homocysteine
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inhibition of the last step in the synthesis of phosphatidylcholine
0.054
S-adenosyl-L-homocysteine
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phosphatidyl-N-dimethylethanolamine as substrate, competitive inhibition
0.057
S-adenosyl-L-homocysteine
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phosphatidyl-N-monomethylethanolamine as substrate, competitive inhibition
0.12
S-adenosyl-L-homocysteine
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phosphatidyl-N-dimethylethanolamine as substrate, noncompetitive inhibition
0.32
S-adenosyl-L-homocysteine
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phosphatidyl-N-monomethylethanolamine as substrate, noncompetitive inhibition
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additional information
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activity of PEMT-S is much higher than of its isoform PEMT-L
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8.5
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low substrate concentrations about 0.01 M S-adenosyl-L-methionine
10
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10
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high substrate concentrations about 0.2 M S-adenosyl-L-methionine
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UniProt
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bovine
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UniProt
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mouse
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rabbit
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Sprague-Dawley
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fission yeast
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human
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rat
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Sprague-Dawley
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white rats
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baker's yeast
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synaptosomes
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skeletal muscle
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islet cells
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microvilli
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rod outer segments
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present in red blood cells on the interior side of the membrane
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sarcolemma, sarcolemmal vesicles
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sarcolemma, sarcolemmal vesicles
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localized mainly in the extracytoplasmic luminal part of the membrane
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synaptosomal plasma membrane
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metabolism
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PEMT-L and PEMT-S expression increase the cellular phosphatidylcholine content, whereas the phosphatidylethanolamine content is decreased by PEMT-S expression, but is hardly affected by PEMT-L expression. The cellular content of phosphatidylserine is also reduced by the expression of PEMT-L or PEMT-S
physiological function
although the accumulation of the PLMT substrates phosphatidyl-N-monomethylethanolamine and phosphatidyl-N,N-dimethylethanolamine is considerably elevated in the plmt knock-out line, phosphatidylcholine levels remain normal, and no obvious differences are observed in plant morphology or development under standard growth conditions
physiological function
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PEMT-L and PEMT-S expression promote the proliferation of HEK-293 cells
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23150
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predicted from amino acid sequence
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glycoprotein
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N-glycosylated with high-mannose oligosaccharides
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-70°C, not stable to freezing
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2°C, loses 30% of its activity within 12 h
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enzyme is encoded by PEM2/OPI3 gene, cloned by complementation
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expressed in Saccharomyces cerevisiae
stably expressed in human embryonic kidney-293 cells
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expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae
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the expression level of PEMT-L is 4.4fold higher than that of PEMT-S
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medicine
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adriamycin, an effective anticancer chemotherapeutic agent depresses enzyme activity in vivo and in vitro
medicine
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adriamycin, an effective anticancer chemotherapeutic agent depresses enzyme activity in vivo and in vitro
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Gaynor, P.M.; Carman, G.M.
Phosphatidylethanolamine methyltransferase and phospholipid methyltransferase activities from Saccharomyces cerevisiae. Enzymological and kinetic properties
Biochim. Biophys. Acta
1045
156-163
1990
Saccharomyces cerevisiae
brenda
Guan, Z.Z.; Wang, Y.N.; Xiao, K.Q.; Hu, P.S.; Liu, J.L.
Activity of phosphatidylethanolamine-N-methyltransferase in brain affected by Alzheimer's disease
Neurochem. Int.
34
41-47
1999
Homo sapiens
brenda
Roque, M.E.; Giusto, N.M.
Phosphatidylethanolamine N-methyltransferase activity in isolated rod outer segments from bovine retina
Exp. Eye Res.
60
631-643
1995
Bos taurus, Rattus norvegicus
brenda
Schneider, W.J.; Vance, D.E.
Conversion of phosphatidylethanolamine to phosphatidylcholine in rat liver. Partial purification and characterization of the enzymatic activities
J. Biol. Chem.
254
3886-3891
1979
Rattus norvegicus, Rattus norvegicus Wistar
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Hirata, F.; Viveros, O.H.; Diliberto, E.J.; Axelrod, J.
Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine
Proc. Natl. Acad. Sci. USA
75
1718-1721
1978
Bos taurus, Neurospora crassa, Rattus norvegicus
brenda
Kanipes, M.I.; Henry, S.A.
The phospholipid methyltransferases in yeast
Biochim. Biophys. Acta
1348
134-141
1997
Bos taurus, Saccharomyces cerevisiae, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe
brenda
Iliskovic, N.; Panagia, V.; Slezak, J.; Kumar, D.; Li, T.; Singal, P.K.
Adriamycin depresses in vivo and in vitro phosphatidylethanolamine N-methylation in rat heart sarcolemma
Mol. Cell. Biochem.
176
235-240
1997
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
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Sastry, B.V.R.; Statham, C.N.; Axelrod, J.; Hirata, F.
Evidence for two methyltransferase involved in the conversion of phosphatidylethanolamine to phosphatidylcholine in the rat liver
Arch. Biochem. Biophys.
211
762-773
1981
Bos taurus, Homo sapiens, Neurospora crassa, Rattus norvegicus
brenda
Tanaka, Y.; Amano, F.; Maeda, M.; Nishijima, M.; Akamatsu, Y.
Purification and properties of phosphatidyl-N-monomethylethanolamine N-methyltransferase, the enzyme catalyzing the second and the third steps in the phosphatidylethanolamine N-methyltransferase system, from mouse liver microsomes
Jpn. J. Med. Sci. Biol.
43
59-73
1990
Mus musculus
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Pilarska, M.; Pikula, S.; Szymanska, G.; Sarzala, M.G.
Properties and topology of enzymes methylating phosphatidylethanolamine to phosphatidylcholine in sarcoplasmic reticulum
Int. J. Biochem.
19
705-711
1987
Oryctolagus cuniculus
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Keogh, M.R.; Courtney, P.D.; Kinney, A.J.; Dewey, R.E.
Functional characterization of phospholipid N-methyltransferases from Arabidopsis and soybean
J. Biol. Chem.
284
15439-15447
2009
Glycine max (C3VD33), Arabidopsis thaliana (Q9SAH5)
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Morita, S.Y.; Takeuchi, A.; Kitagawa, S.
Functional analysis of two isoforms of phosphatidylethanolamine N-methyltransferase
Biochem. J.
432
387-398
2010
Homo sapiens
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