2.1.1.17: phosphatidylethanolamine N-methyltransferase
This is an abbreviated version!
For detailed information about phosphatidylethanolamine N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.17
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2.1.1.17
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phosphatidylcholine
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choline
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homocysteine
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cytidylyltransferase
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cdp-choline
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betaine
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s-adenosylhomocysteine
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ctp:phosphocholine
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cdp-diacylglycerol
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phosphatidyl-n,n-dimethylethanolamine
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phosphatidyl-n-monomethylethanolamine
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choline-deficient
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transmethylation
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n-methyltransferases
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kennedy
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adomet
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vance
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phosphatidylmonomethylethanolamine
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medicine
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ptdcho
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analysis
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phosphatidyldimethylethanolamine
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mthfd1
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remethylation
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cholinephosphotransferase
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adohcy
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choline-supplemented
- 2.1.1.17
- phosphatidylcholine
- choline
- homocysteine
- cytidylyltransferase
- cdp-choline
- betaine
- s-adenosylhomocysteine
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ctp:phosphocholine
- cdp-diacylglycerol
- phosphatidyl-n,n-dimethylethanolamine
- phosphatidyl-n-monomethylethanolamine
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choline-deficient
-
transmethylation
- n-methyltransferases
-
kennedy
- adomet
-
vance
- phosphatidylmonomethylethanolamine
- medicine
-
ptdcho
- analysis
- phosphatidyldimethylethanolamine
- mthfd1
-
remethylation
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cholinephosphotransferase
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adohcy
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choline-supplemented
Reaction
Synonyms
lipid methyl transferase, LMTase, methyltransferase, phosphatidylethanolamine, PE N-MTase, PE-NMT, PEMT, PEMT shorter isoform, phosphatidylethanolamine methyltransferase, phosphatidylethanolamine N-methyltransferase, phosphatidylethanolamine-N-methylase, phosphatidylethanolamine-N-methyltransferase, phosphatidylethanolamine-S-adenosylmethionine methyltransferase, phospholipid N-methyltransferase, PmtA, PmtX1, PmtX3
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General Information
General Information on EC 2.1.1.17 - phosphatidylethanolamine N-methyltransferase
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malfunction
physiological function
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PEMT deficiency reduces plasma homocysteine by 34% to 52% in mice deficient in both PEMT and low-density lipoprotein receptors, deletion of PEMT modestly reduces hepatic very low density lipoprotein secretion in low-density lipoprotein receptors knockout mice and alters the rate of very low density lipoprotein clearance from plasma
malfunction
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lack of PEMT decreases liver damage in Abcb4-/- mice caused by exposure of the liver to excess bile acids. PEMT deficiency affects intestinal Na+ absorption resulting in an impaired Na+ concentration gradient along the length of the small intestine and abnormal absorption of bile acids mediated by apical sodium-dependent bile acid transporter
expression of PEMT increases the cellular phosphatidylcholine (PC) content, lowers the phosphatidylethanolamine (PE) content, but has no effect on the sphingomyelin content. Consequently, PEMT expression leads to reductions in PE/PC and sphingomyelin /PC ratios. PEMT expression enhances the resistance to duramycin and lysenin. PEMT expression increases the diameter of microvilli. The expression of PEMT results in reduced resistance to unconjugated bile salts, but in increased resistance to conjugated bile salts
physiological function
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the PEMT pathway in human liver is selective for polyunsaturated phosphatidylcholine species, especially those containing docosahexaenoic acid
physiological function
hepatic PEMT activity does not differ between intact female and male cats and no changes upon spaying/neutering are observed. No significant differences in liver phosphatidylcholine content and PEMT-specific polyunsaturated phosphatidylcholine species are found between the sexes and before or after spaying/neutering
physiological function
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recombinant expression of phosphatidylethanolamine methyltransferase from Acetobacter aceti, fused with a mitochondrial targeting signal from yeast, in Saccharomyces cerevisiae. The expression suppresses the choline auxotrophy of a double deletion mutant of endogenous phosphatidylethanolamine methyltransferases PEM1 and PEM2 and enables synthesis of phosphatidylcholine in the absence of choline. This growth suppression is observed even if the Kennedy pathway is inactivated by the repression of PCT1 encoding CTP:phosphocholine cytidylyltransferase
physiological function
a transgenic HO mouse model of classical homocystinuria exhibits only mild liver injury. Hepatic expression of PEMT in both the cystathionine beta-synthase-/- and HO models is post-translationally repressed with decreased levels of PEMT protein and activity that inversely correlates with the scale of liver injury. PEMT in HO mice is not further induced by increased homocysteine, methionine and S-adenosylhomocysteine or depletion of glutathione
physiological function
In chow-fed Pemt-/- mice, the hepatic phosphatidylcholine/phosphatidylethanolamine ratio in the ER is lower than in Pemt+/+ mice, and levels of ER stress markers, CHOP and BIP, are higher without activation of the unfolded protein response. In livers of high-fat-diet-fed Pemt-/- mice the ER has a lower phosphatidylcholine/phosphatidylethanolamine ratio, and exhibits more ER stress and unfolded protein response activation. The unfolded protein response is repressed in McArdle cells expressing PEMT compared with those lacking PEMT
physiological function
in Pemt-/- mice, treatment with vitamin E (0.5 g/kg) for 3 weeks improves very low-density lipoprotein-triglyceride secretion and normalizes cholesterol metabolism, but fails to reduce hepatic triglyceride content. Vitamin E treatment is able to reduce hepatic oxidative stress, inflammation and fibrosis. Pemt-/- mice fed a high-fat diet show abnormal ceramide metabolism, with elevation of ceramides and other sphingolipids and higher expression of mRNAs for acid ceramidase (Asah1) and ceramide kinase (Cerk)
physiological function
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recombinant expression of phosphatidylethanolamine methyltransferase from Acetobacter aceti, fused with a mitochondrial targeting signal from yeast, in Saccharomyces cerevisiae. The expression suppresses the choline auxotrophy of a double deletion mutant of endogenous phosphatidylethanolamine methyltransferases PEM1 and PEM2 and enables synthesis of phosphatidylcholine in the absence of choline. This growth suppression is observed even if the Kennedy pathway is inactivated by the repression of PCT1 encoding CTP:phosphocholine cytidylyltransferase
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