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
-
choline-deficient
-
transmethylation
- n-methyltransferases
-
kennedy
- adomet
-
vance
- phosphatidylmonomethylethanolamine
- medicine
-
ptdcho
- analysis
- phosphatidyldimethylethanolamine
- mthfd1
-
remethylation
-
cholinephosphotransferase
-
adohcy
-
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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Localization
Localization on EC 2.1.1.17 - phosphatidylethanolamine N-methyltransferase
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enzyme attaches to the membrane via electrostatic interactions with anionic lipids, which do not serve as substrate. Increasing phosphatidylcholine concentrations trigger membrane dissociation suggesting that membrane binding of PmtA is negatively regulated by its end product phosphatidylcholine. alpha-Helical regions alphaA and alphaF contribute to membrane binding. The latter undergoes a structural transition from disordered to alpha-helical conformation in the presence of anionic lipids. The basic amino acids R8 and K12 and the hydrophobic amino acid F19 are critical for membrane binding by alphaA as well as for activity of full-length PmtA
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topographical model: 4 transmembrane regions span the membrane such that both the N and C termini of the enzyme are localized external to the ER. Two hydrophilic connecting loops protrude into the luminal face of the microsomes whereas a corresponding loop protrudes on the cytosolic side remains proximate to the membrane