Any feedback?
Information on EC 2.1.1.17 - phosphatidylethanolamine N-methyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q08388
for references in articles please use BRENDA:EC2.1.1.17Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.1.17 phosphatidylethanolamine N-methyltransferaseSpecify your search results
Word Map
- 2.1.1.17
- phosphatidylcholine
- choline
- homocysteine
- cytidylyltransferase
- cdp-choline
- betaine
- s-adenosylhomocysteine
-
ctp:phosphocholine
- cdp-diacylglycerol
- phosphatidyl-n,n-dimethylethanolamine
- phosphatidyl-n-monomethylethanolamine
-
choline-deficient
-
transmethylation
- n-methyltransferases
-
kennedy
- adomet
-
vance
- phosphatidylmonomethylethanolamine
- medicine
-
ptdcho
- analysis
- phosphatidyldimethylethanolamine
- mthfd1
-
remethylation
-
cholinephosphotransferase
-
adohcy
-
choline-supplemented
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
pemt, phosphatidylethanolamine n-methyltransferase, phosphatidylethanolamine methyltransferase, phospholipid n-methyltransferase, phosphatidylethanolamine-n-methyltransferase, pe n-mtase, pmtx1, pe-nmt, pmtx3, s-adenosyl-l-methionine:phosphatidylethanolamine n-methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lipid methyl transferase
-
-
-
-
LMTase
-
-
-
-
methyltransferase, phosphatidylethanolamine
-
-
-
-
PE N-MTase
-
-
-
-
PEMT
phosphatidylethanolamine methyltransferase
-
-
-
-
phosphatidylethanolamine-N-methylase
-
-
-
-
phosphatidylethanolamine-S-adenosylmethionine methyltransferase
-
-
-
-
PEMT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:phosphatidylethanolamine N-methyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
37256-91-0
-
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
3 S-adenosyl-L-methionine + phosphatidylethanolamine
3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+
2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
2 S-adenosyl-L-homocysteine + phosphatidylcholine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-methionine + phosphatidylethanolamin
-
-
-
-
?
S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
-
the enzyme catalyzes the stepwise methylation of phosphatidylethanolamine to phosphatidylcholine, in addition to the main pathway that synthesizes phosphatidylcholine directly from choline
-
?
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
3 S-adenosyl-L-methionine + phosphatidylethanolamine
3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+
-
-
-
?
3 S-adenosyl-L-methionine + phosphatidylethanolamine
3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+
betaine attenuates alcoholic steatosis by restoring phosphatidylcholine generation via the phosphatidylethanolamine methyltransferase pathway, overview
-
-
?
2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
2 S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
-
?
2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
2 S-adenosyl-L-homocysteine + phosphatidylcholine
-
phospholipid substrates and products are the first to bind and the last to dissociate from the active site
-
-
?
2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
2 S-adenosyl-L-homocysteine + phosphatidylcholine
-
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
-
-
?
2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
2 S-adenosyl-L-homocysteine + phosphatidylcholine
-
ordered bi-bi mechanism
-
-
?
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
-
-
-
?
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
phospholipid substrates and products are the first to bind and the last to dissociate from the active site
-
-
?
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
-
-
?
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
ordered bi-bi mechanism
-
-
?
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
the enzyme catalyzes the stepwise methylation of phosphatidylethanolamine to phosphatidylcholine, in addition to the main pathway that synthesizes phosphatidylcholine directly from choline
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
485167, 485168, 485169, 485170, 485171, 485174, 485179, 485180, 485181, 485183, 485184, 485186, 485188, 485189, 485191, 485192, 485195
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
transfer of three methyl groups to the amino head group of phosphatidylethanolamine
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
the transfer of a methyl group to monomethyl-N-phosphatidylcholine and dimethyl-N,N-phosphatidylcholine is catalyzed by a second enzyme
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
methylation of phosphatidylethanolamine may play a role in very low density lipoprotein secretion
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
possible role of PEMT2 in the suppression of liver proliferation, and perhaps in hepatic carcinogenesis
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
activation of phosphatidylethanolamine methylation at the level of gene expression may be the mechanism by which choline-deficient rats compensate for the lack of dietary choline
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
enzyme form PEMT2 plays an important role in the regulation of hepatocyte cell division and as a liver tumor suppressor
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
the enzyme catalyzes the stepwise methylation of phosphatidylethanolamine to phosphatidylcholine, in addition to the main pathway that synthesizes phosphatidylcholine directly from choline. Loss of PEMT function may contribute to malignant transformation of hepatocytes
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
inactivation of enzyme form PEMT2 may have a role in the regulation of non-neoplastic growth of liver
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
enzyme form PEMT2 may have a role in the regulation of in vivo hepatoma and hepatocyte cell division as well as hepatocyte cell death by apoptosis
-
-
?
additional information
additional information
-
-
the total hepatic S-adenosylmethionine levels remain unchanged by ethanol consumption for 4 weeks
S-adenosylhomocysteine levels increase by ethanol consumption for 4 weeks. The S-adenosylmethionine:S-adenosylhomocysteine ratios are significantly lower in ethanol fed rats. Supplementation of betaine in the ethanol diet increases the hepatocellular S-adenosylmethionine:S-adenosylhomocysteine ratios to values that are statistically similar to those from rats fed the regular control diet. There is an significant inverse relationship between triglycerids and S-adenosylmethionine:S-adenosylhomocysteine ratio (r = - 0.36).
-
?
additional information
additional information
-
the total hepatic S-adenosylmethionine levels remain unchanged by ethanol consumption for 4 weeks
S-adenosylhomocysteine levels increase by ethanol consumption for 4 weeks. The S-adenosylmethionine:S-adenosylhomocysteine ratios are significantly lower in ethanol fed rats. Supplementation of betaine in the ethanol diet increases the hepatocellular S-adenosylmethionine:S-adenosylhomocysteine ratios to values that are statistically similar to those from rats fed the regular control diet. There is an significant inverse relationship between triglycerids and S-adenosylmethionine:S-adenosylhomocysteine ratio (r = - 0.36).
-
?
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
3 S-adenosyl-L-methionine + phosphatidylethanolamine
3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+
betaine attenuates alcoholic steatosis by restoring phosphatidylcholine generation via the phosphatidylethanolamine methyltransferase pathway, overview
-
-
?
S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
-
the enzyme catalyzes the stepwise methylation of phosphatidylethanolamine to phosphatidylcholine, in addition to the main pathway that synthesizes phosphatidylcholine directly from choline
-
?
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
the enzyme catalyzes the stepwise methylation of phosphatidylethanolamine to phosphatidylcholine, in addition to the main pathway that synthesizes phosphatidylcholine directly from choline
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
methylation of phosphatidylethanolamine may play a role in very low density lipoprotein secretion
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
possible role of PEMT2 in the suppression of liver proliferation, and perhaps in hepatic carcinogenesis
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
activation of phosphatidylethanolamine methylation at the level of gene expression may be the mechanism by which choline-deficient rats compensate for the lack of dietary choline
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
enzyme form PEMT2 plays an important role in the regulation of hepatocyte cell division and as a liver tumor suppressor
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
the enzyme catalyzes the stepwise methylation of phosphatidylethanolamine to phosphatidylcholine, in addition to the main pathway that synthesizes phosphatidylcholine directly from choline. Loss of PEMT function may contribute to malignant transformation of hepatocytes
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
inactivation of enzyme form PEMT2 may have a role in the regulation of non-neoplastic growth of liver
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
enzyme form PEMT2 may have a role in the regulation of in vivo hepatoma and hepatocyte cell division as well as hepatocyte cell death by apoptosis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
3-5 fold activation of formation of phosphatidylcholine and phosphatidyl N,N-dimethylethanolamine. Synthesis of phosphatidyl N-monomethylethanolamine is not affected
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
phosphatidylethanolamine, monomethyl-phosphatidylethanolamine and dimethyl-phosphatidylethanolamine compete for a common active site
-
additional information
-
phosphatidylethanolamine, monomethyl-phosphatidylethanolamine and dimethyl-phosphatidylethanolamine compete for a common active site
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
betaine
attenuates alcoholic steatosis by restoring phosphatidylcholine generation via the phosphatidylethanolamine methyltransferase pathway, the effect is enhanced by ethanol, which alone has no effect on expression levels of the enzyme, overview
ethanol
enhances the inducing and protecting effects of betaine on the enzyme, alone has only a slightly activating effect on the enzyme activity, overview
1-methyl-4-phenylpyridinium
-
enhances activity. S-Adenosylmethionine hypermethylation can be involved in the etiology of Parkinsons disease and an increase of phospholipid methylation could be one of the mechanisms by which 1-methyl-4-phenyl-pyridinium causes parkinsonism
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0136
S-adenosylmethionine
-
reaction with phosphatidyl-N,N-dimethylethanolamine
0.016
S-adenosylmethionine
-
reaction with phosphatidyl-N,N-dimethylethanolamine
0.022
S-adenosylmethionine
-
reaction with phosphatidyl-N-monomethylethanolamine
0.0397
S-adenosylmethionine
-
reaction with phosphatidyl-N-monomethylethanolamine
0.08
S-adenosylmethionine
-
with phosphatidyl-N-monomethylethanolamine as substrate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0739
S-adenosylhomocysteine
-
reaction with phosphatidyl-N-dimethylethanolamine
0.0049
S-adenosyl-L-homocysteine
-
reaction with phosphatidyl-N-monomethylethanolamine
0.0067
S-adenosyl-L-homocysteine
-
reaction with phosphatidyl-N,N-dimethylethanolamine
0.138
S-adenosyl-L-homocysteine
-
reaction with phosphatidyl-N-monomethylethanolamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the activity of phosphatidylethanolamine N-methyltransferase increases (58% higher on day 5, 72% higher on day 7) over 7 d following the injection of streptozotocin (injection of 60 mg/kg on day 0). Diabetes increases the phosphatidylethanolamine N-methyltransferase activity and abundance. Administration of all-trans-retinoic acid alone or in combination with streptozotocin has no effect on phosphatidylethanolamine N-methyltransferase activity. Phosphatidylethanolamine N-methyltransferase activity and abundance in the streptozotocin + insulin group is not significantly different from control values. The enzymatic activity of phosphatidylethanolamine N-methyltransferase is determined by measuring the incorporation of radiolabled methyl groups from S-adenosyl-L-[methyl-3H]methionine into phospholipids.
additional information
-
there is a significant positive linear relationship between phosphatidylethanolamine N-methyltransferase activity and S-adenosylmethionine:S-adenosylhomocysteine ratio (r = 0.45). There is a significant inverse relationship between phosphatidylethanolamine N-methyltransferase activity and triglycerids. The metabolic conversion of radiolabeled phosphatidylethanolamine to phosphatidylcholine over 3 h incubation period is taken as a measure of phosphatidylethanolamine N-methyltransferase.
additional information
there is a significant positive linear relationship between phosphatidylethanolamine N-methyltransferase activity and S-adenosylmethionine:S-adenosylhomocysteine ratio (r = 0.45). There is a significant inverse relationship between phosphatidylethanolamine N-methyltransferase activity and triglycerids. The metabolic conversion of radiolabeled phosphatidylethanolamine to phosphatidylcholine over 3 h incubation period is taken as a measure of phosphatidylethanolamine N-methyltransferase.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
additional information
-
activity increases in nearly a linear fashion between pH 6.0 and 9.5
10
-
methylation of phosphatidylethanolamine, phosphatidyl-N-monomethylethanolamine and phosphatidyl-N,N-dimethylethanolamine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high level of activity is expressed in defined extranuclear regions
-
enzyme form PEMT2 is absent in hepatoma cells growing exponentially in vivo. Both PEMT2 and mRNA appears when cells enter the stationary phase of tumor growth
-
PEMT2 protein decreases in preneoplastic nodules and virtually disappears in hepatocellular carcinoma
-
-
485164, 485165, 485167, 485168, 485169, 485170, 485171, 485174, 485179, 485184, 485186, 485188, 485189, 485191, 485192, 485195, 675185
-
in prenatal livers enzyme form PEMT2 is completely absent, high level of PEMT2 appears at birth and is sustained throughout adult life
-
normal liver, nodules, advanced nodules and hepatomas. Enzyme form PEMT2 is diminished during liver carcinogenesis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). PEMT_RAT
199
5
22486
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18300
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
the catalytic subunit of 15000-18000 Da exists in the native form as a complex of approximately 200000 Da in association with other membrane-bound proteins and lipids
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
the dimeric enzyme form can be phosphorylated by cyclic AMP-dependent protein kinase
phosphoprotein
-
the enzyme can be converted by cyclic AMP dependent protein kinase from a low activity dephosphorylated enzyme form to a high activity phosphorylated form
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% loss of activity after trypsin treatment, 0.001 mg trypsin per 0.05 mg membrane protein
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ridgway, N.D.; Vance, D.E.
Phosphatidylethanolamine N-methyltransferase from rat liver
Methods Enzymol.
209
366-374
1992
Rattus norvegicus
Vance, D.E.; Schneider, W.J.
Conversion of phosphatidylethanolamine to phosphatidylcholine
Methods Enzymol.
71
581-588
1981
Rattus norvegicus
Pajares, M.A.; Villalba, M.; Mato, J.M.
Purification of phospholipid methyltransferase from rat liver microsomal fraction
Biochem. J.
237
699-705
1986
Rattus norvegicus
McBride, K.; Furness, L.M.; Gibbons, W.A.
Lipid methyltransferase: purification and structure
Biochem. Soc. Trans.
15
924-925
1987
Rattus norvegicus
-
Fonteh, A.N.; Gibbons, W.A.
Solubilization and purification of lipid methyltransferase
Biochem. Soc. Trans.
18
266-267
1990
Rattus norvegicus
Varela, I.; Merida, I.; Pajares, M.; Villalba, M.; Mato, J.M.
Activation of partially purified rat liver lipid methyltransferase by phosphorylation
Biochem. Biophys. Res. Commun.
122
1065-1070
1984
Rattus norvegicus
Ridgway, N.D.; Vance, D.E.
Kinetic mechanism of phosphatidylethanolamine N-methyltransferase
J. Biol. Chem.
263
16864-16871
1988
Rattus norvegicus
Prasad, C.; Edwards, R.M.
Synthesis of phosphatidylcholine from phosphatidylethanolamine by at least two methyltransferases in rat pituitary extracts
J. Biol. Chem.
256
13000-13003
1981
Rattus norvegicus
-
Dudeja, P.K.; Foster, E.S.; Brasitus, T.A.
Synthesis of phosphatidylcholine by two distinct methyltransferases in rat colonic brush-border membranes: evidence for extrinsic and intrinsic membrane activities
Biochim. Biophys. Acta
875
493-500
1986
Rattus norvegicus
Ridgway, N.D.; Vance, D.E.
Purification of phosphatidylethanolamine N-methyltransferase from rat liver
J. Biol. Chem.
262
17231-17239
1987
Rattus norvegicus
Vance, D.E.; Walkey, C.J.; Cui, Z.
Phosphatidylethanolamine N-methyltransferase from liver
Biochim. Biophys. Acta
1348
142-150
1997
Rattus norvegicus
Cui, Z.; Shen, Y.J.; Vance, D.E.
Inverse correlation between expression of phosphatidylethanolamine N-methyltransferase-2 and growth rate of perinatal rat livers
Biochim. Biophys. Acta
1346
10-16
1997
Rattus norvegicus
Nishimaki-Mogami, T.; Suzuki, K.; Takahashi, A.
The role of phosphatidylethanolamine methylation in the secretion of very low density lipoproteins by cultured rat hepatocytes: rapid inhibition of phosphatidylethanolamine methylation by bezafibrate increases the density of apolipoprotein B48-containing lipoproteins
Biochim. Biophys. Acta
1304
21-31
1996
Rattus norvegicus
Tessitore, L.; Dianzani, I.; Cui, Z.; Vance, D.E.
Diminished expression of phosphatidylethanolamine N-methyltransferase 2 during hepatocarcinogenesis
Biochem. J.
337
23-27
1999
Rattus norvegicus
-
Tessitore, L.; Cui, Z.; Vance, D.E.
Transient inactivation of phosphatidylethanolamine N-methyltransferase-2 and activation of cytidine triphosphate:phosphocholine cytidylyltransferase during non-neoplastic liver growth
Biochem. J.
322
151-154
1997
Rattus norvegicus
-
Cui, Z.; Vance, D.E.
Expression of phosphatidylethanolamine N-methyltransferase-2 is markedly enhanced in long term choline-deficient rats
J. Biol. Chem.
271
2839-2843
1996
Rattus norvegicus
Lee, E.S.Y.; Charlton, C.G.
1-Methyl-4-phenyl-pyridinium increases S-adenosyl-L-methionine dependent phospholipid methylation
Pharmacol. Biochem. Behav.
70
105-114
2001
Rattus norvegicus
Tessitore, L.; Sesca, E.; Bosco, M.; Vance, D.E.
Expression of phosphatidylethanolamine N-methyltransferase in Yoshida ascites hepatoma cells and the livers of host rats
Carcinogenesis
20
561-567
1999
Rattus norvegicus
Kim, Y.J.; Park, H.S.; Choi, M.U.
Detection of cytosolic phosphatidylethanolamine N-methyltransferase in rat brain
J. Biochem. Mol. Biol.
31
170-176
1998
Rattus norvegicus
-
Vance, D.E.
Phosphatidylethanolamine N-methyltransferase: Unexpected findings from curiosity-driven research
Eur. J. Med. Res.
1
182-188
1996
Rattus norvegicus
Tessitore, L.; Sesca, E.; Vance, D.E.
Inactivation of phosphatidylethanolamine N-methyltransferase-2 in aflatoxin-induced liver cancer and partial reversion of the neoplastic phenotype by PEMT transfection of hepatoma cells
Int. J. Cancer
86
362-367
2000
Rattus norvegicus
Kharbanda, K.K.; Mailliard, M.E.; Baldwin, C.R.; Beckenhauer, H.C.; Sorrell, M.F.; Tuma, D.J.
Betaine attenuates alcoholic steatosis by restoring phosphatidylcholine generation via the phosphatidylethanolamine methyltransferase pathway
J. Hepatol.
46
314-321
2007
Rattus norvegicus, Rattus norvegicus (Q08388)
EXTERNAL LINKS (specific for EC-Number 2.1.1.17)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
