BRENDA - Enzyme Database

Kinetic mechanism of phosphatidylethanolamine N-methyltransferase

Ridgway, N.D.; Vance, D.E.; J. Biol. Chem. 263, 16864-16871 (1988)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
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-monomethylethanolamine
-
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
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.1.17
Rattus norvegicus
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
liver
-
Rattus norvegicus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
485171
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
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
-
-
?
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
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
ordered bi-bi mechanism
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidylethanolamine
-
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
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
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
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
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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-monomethylethanolamine
-
Rattus norvegicus
2.1.1.17
2.12
-
phosphatidyl-N,N-dimethylethanolamine
-
Rattus norvegicus
2.1.1.17
5
-
phosphatidylethanolamine
-
Rattus norvegicus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
liver
-
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
485171
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
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
-
-
?
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
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
ordered bi-bi mechanism
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidylethanolamine
-
485171
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?