Information on EC 2.1.1.17 - phosphatidylethanolamine N-methyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.1.1.17
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RECOMMENDED NAME
GeneOntology No.
phosphatidylethanolamine N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Glycerophospholipid metabolism
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Metabolic pathways
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phosphatidylcholine biosynthesis V
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phosphatidylethanolamine bioynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:phosphatidylethanolamine N-methyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37256-91-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain USDA110
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Manually annotated by BRENDA team
strain USDA110
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
5-6-months old farm-bred mink. Mink fed on 67LNGB diet (67% extracted lipids from natural gas-utilising bacteria, fed for 25 d, total phosphatidylethanolamine 25.7 mg/g) have a significantly higher homocysteine plasma concentrations, plasma total phospholipids, phosphatidylcholine, lysophosphatidylcholine and phospholipids are significantly lower and the phosphatidylethanolamine:phosphatidylcholine ratio in plasma increases significantly compared to SB diet (0% extracted lipids from natural gas-utilising bacteria, but 100% soyabean oil, fed for 25 d, total phosphatidylethanolamine 0.04 mg/g). Plasma homocysteine is negatively correlated with phosphatidylcholine (r = -0.74). There is a significant negative correlation between plasma homocysteine and total phospholipids (r = -0.022). Faecal excretion of phosphatidylcholine, lysophosphatidylcholine and phosphatidylethanolamine is higher in the mink fed the 67LNGB diet than in those fed the SB diet, and significantly higher in mink fed the 67LNGB diet than in animal fed the 17LNGB (17% extraceted lipids from natural gas-utilising bacteria, fed for 25 d, total phosphatidylethanolamine 2.6 mg/g) diet.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
phosphatidylethanolamine N-methyltransferase is used to radioisotopically label the envelope of Autographa californica recombinant strain vGFPuv through the methylation of phosphatidylethanolamine. The modification of envelope phospholipids by phosphatidylethanolamine N-methyltransferase does not affect the infectivity of Autographa californica recombinant strain vGFPuv.
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + phosphatidylethanolamine
3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+
show the reaction diagram
S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
show the reaction diagram
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
show the reaction diagram
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
show the reaction diagram
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + phosphatidylethanolamine
3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+
show the reaction diagram
Q08388
betaine attenuates alcoholic steatosis by restoring phosphatidylcholine generation via the phosphatidylethanolamine methyltransferase pathway, overview
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?
S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
show the reaction diagram
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
show the reaction diagram
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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1 mM, increases activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bezafibrate
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potent inhibitor of methylation of phosphoethanolamine
Clofibric acid
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potent inhibitor of methylation of phosphoethanolamine
HgCl2
NEM
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S-adenosyl-L-homocysteine
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S-adenosylhomocysteine
Triton X-100
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methyl-4-phenylpyridinium
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enhances activity. S-Adenosylmethionine hypermethylation can be involved in the etiology of Parkinson‘s disease and an increase of phospholipid methylation could be one of the mechanisms by which 1-methyl-4-phenyl-pyridinium causes parkinsonism
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
L-Cys
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enhances activity, optimal concentration 10 mM
progesterone
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physiological levels of progesterone activate PE-NMT and sphingomyelin synthase
Triton X-100
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enhances activity, optimal concentration 0.04%
Tween 20
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stimulates
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45 - 2.12
phosphatidyl-N,N-dimethylethanolamine
0.0175 - 0.74
phosphatidyl-N-monomethylethanolamine
0.0336 - 5
phosphatidylethanolamine
0.02
S-adenosyl-L-methionine
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0.0019 - 0.11
S-adenosylmethionine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0048 - 0.2775
S-adenosyl-L-homocysteine
0.0739
S-adenosylhomocysteine
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reaction with phosphatidyl-N-dimethylethanolamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.63
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activity with phosphatidylethanolamine
3.75
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activity with phosphatidyl-N-monomethylethanolamine
8.59
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activity with phosphatidyl-N,N-dimethyl-ethanolamine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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and a second optimum at pH 9.5
7.5
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assay at
9.5
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and a second optimum at pH 9.5
additional information
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activity increases in nearly a linear fashion between pH 6.0 and 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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phosphatidylethanolamine N-methyltransferase assays demonstrate salinity-dependent activities in the digestive gland and hemocytes
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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phosphatidylethanolamine N-methyltransferase assays demonstrate salinity-dependent activities in the digestive gland and hemocytes
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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plasma membranes from Rana oocytes are used
Manually annotated by BRENDA team
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rod outer segment
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
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SDS-PAGE
22000
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x * 22000, SDS-PAGE, epitope-tagged protein
25000
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1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
42000
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3 * 42000, SDS-PAGE
50000
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alphaxbetay, x * 50000 + y * 50000, SDS-PAGE
120000
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gel filtration
200000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
monomer
tetramer
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alphaxbetay, x * 50000 + y * 50000, SDS-PAGE
trimer
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3 * 42000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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30 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% loss of activity after trypsin treatment, 0.001 mg trypsin per 0.05 mg membrane protein
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, 30% of the activity is lost after 12 h
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a LLC-PK1 cell line stably expressing PEMT shorter isoform (LLC-PK1 /PEMT) is established
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DNA and amino acid sequence determination and analysis including a estrogen response sequence, the PEMT gene has three unique transcription start sites, which are indicative of either multiple promoters and/or alternative splicing
DNA and amino acid sequence determination and analysis, population-based PEMT genotyping, overview
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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PEMT gene encodes enzyme form PEMT1 and PEMT2
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the PEMT gene is localized to chromosome 11 and spans 25 kb with seven exons and six introns, expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PEMT mRNA and protein levels increase dramatically in 3T3-L1 cells upon differentiation to adipocytes. Expression is regulated through transcription factor Sp1
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D106A
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protein completely insoluble and thus inactive
D106E
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protein insoluble
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
G64A
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protein completely insoluble and thus inactive
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
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