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Literature summary extracted from

  • Ridgway, N.D.; Vance, D.E.
    Kinetic mechanism of phosphatidylethanolamine N-methyltransferase (1988), J. Biol. Chem., 263, 16864-16871.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.17 additional information phosphatidylethanolamine, monomethyl-phosphatidylethanolamine and dimethyl-phosphatidylethanolamine compete for a common active site Rattus norvegicus
2.1.1.17 S-adenosyl-L-homocysteine
-
 Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.17 0.0136
-
 S-adenosylmethionine reaction with phosphatidyl-N,N-dimethylethanolamine Rattus norvegicus
2.1.1.17 0.0296
-
 S-adenosylmethionine reaction with phosphatidylethanolamine Rattus norvegicus
2.1.1.17 0.0397
-
 S-adenosylmethionine reaction with phosphatidyl-N-monomethylethanolamine Rattus norvegicus
2.1.1.17 0.74
-
 phosphatidyl-N-methylethanolamine
-
 Rattus norvegicus
2.1.1.17 2.12
-
 phosphatidyl-N,N-dimethylethanolamine
-
 Rattus norvegicus
2.1.1.17 5
-
 phosphatidylethanolamine
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.17 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.17 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.17 2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine phospholipid substrates and products are the first to bind and the last to dissociate from the active site Rattus norvegicus 2 S-adenosyl-L-homocysteine + phosphatidylcholine
-
 ?
2.1.1.17 2 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine ordered bi-bi mechanism Rattus norvegicus 2 S-adenosyl-L-homocysteine + phosphatidylcholine
-
 ?
2.1.1.17 S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
 Rattus norvegicus S-adenosyl-L-methionine + phosphatidylethanolamin
-
 ?
2.1.1.17 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine phospholipid substrates and products are the first to bind and the last to dissociate from the active site Rattus norvegicus S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
 ?
2.1.1.17 S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine ordered bi-bi mechanism Rattus norvegicus S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
 ?
2.1.1.17 S-adenosyl-L-methionine + phosphatidylethanolamine
-
 Rattus norvegicus S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.17 0.138
-
 S-adenosyl-L-homocysteine reaction with phosphatidyl-N-monomethylethanolamine Rattus norvegicus
2.1.1.17 0.2775
-
 S-adenosyl-L-homocysteine reaction with phosphatidylethanolamine Rattus norvegicus