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
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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
ECTree
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Engineering
Engineering on EC 2.1.1.17 - phosphatidylethanolamine N-methyltransferase
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DeltaN30
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truncated PmtA variant missing the first 30 amino acids, completely inactive
E58A
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mutant is inactive, CD spectroscopy profile similar to wild-type
E84A
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mutant is inactive, CD spectroscopy profile similar to wild-type
G162A
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mutant as active as wild-type, CD spectroscopy profile similar to wild-type
G60A
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mutant produces only traces of monomethylphosphatidylethanolamine and no dimethylphosphatidylethanolamine and phosphatidylcholine, CD spectroscopy profile similar to wild-type
G62A
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mutant produces only traces of monomethylphosphatidylethanolamine and no dimethylphosphatidylethanolamine and phosphatidylcholine, CD spectroscopy profile similar to wild-type
K6Q/R8Q/K12Q
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mutant produced wild-type-like amounts of the first intermediate monomethyl-phosphatidylethanolamine (C18:1) and reduced amounts of dimethyl-phosphatidylethanolamine (C18:1) and phosphatidylcholine
P61A
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mutant as active as wild-type, CD spectroscopy profile similar to wild-type
R18Q/K21Q/K28Q/K29Q
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mutations of the positively charged residues in the C-terminal part of the alphaA helix, do not influence polar localization
V175M
H196S
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protein is barely detectable due to poor expression or rapid degradation
K197S
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fails to localize to endoplasmic reticulum, but localize to Golgi apparatus, mutant is catalytically active
K197S/R198S
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fails to localize to endoplasmic reticulum, but localize to Golgi apparatus, mutant is catalytically active
additional information
the naturally occuring mutation is associated with diminished enzyme activity and may confer susceptibility to nonalcoholic fatty liver disease
V175M
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mutant with diminished activity, the PEMT polymophism is not associated with alcoholic and nonalcoholic fatty liver disease
V175M
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the mutation causes a loss of function and an increased risk of nonalcoholic fatty liver disease
the PEMT G774C, i.e. rs12325817, and the CHDH G432T, i.e. rs12676, polymorphisms, causing PEMT GG genotype and the variant CC genotype, are related to breast cancer risk, while the BHMT rs3733890 polymorphism of the enzyme is not associated with breast cancer risk, genotyping, overview
additional information
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the A5465G variant form of the PEMT protein is less able to compete for S-adenosyl-L-methionine especially in a folate deplete-environment and is linked to fatty liver disease
additional information
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animals with homozygous disruption of enzyme gene, develop severe steatosis when fed a diet deficient in choline. Animals have substantially diminished concentrations of docosahexaenoic acid and arachidonic acid in plasma
additional information
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construction of Pemt-/- mice lacking all enzyme activity, but with no abnormal phenotype, normal hepatocyte morphology, normal plasma lipid levels, and no differences in bile composition compared to the wild-type mice, but the phenotype is altered after withdrawal of phosphatidylcholine and production of it, overview. In the liver-specific CTP:phosphocholine cytidylyltransferase alpha knock-out mice, PEMT activity is increased nearly 2fold above control levels. The double knockout mutant shows a dramatic decrease in hepatic phosphatidylcholine, overview
additional information
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enzyme-deficient female Pemt-/- mice maintain hepatic PC/total choline levels during the first day of choline deprivation and escaped liver damage whereas male Pemt-/- mice do not, plasma phosphocholine levels in high-density lipoproteins are higher in male Pemt-/- mice than those in females before choline deprivation, overview