BRENDA - Enzyme Database

Partial purification and characterization of phospholipid N-methyltransferases from murine thymocyte microsomes

Makishima, F.; Toyoshima, S.; Osawa, T.; Arch. Biochem. Biophys. 238, 315-324 (1985)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
2.1.1.17
S-adenosylhomocysteine
-
Mus musculus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1.1.17
0.02
-
S-adenosyl-L-methionine
-
Mus musculus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
plasma membrane
-
Mus musculus
5886
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
2.1.1.17
Ca2+
1 mM, increases activity
Mus musculus
2.1.1.17
Mg2+
10 mM, increases activity
Mus musculus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.1.17
Mus musculus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
2.1.1.17
partial
Mus musculus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
thymocyte
-
Mus musculus
-
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
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
485177
Mus musculus
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
-
-
-
2.1.1.17
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
485177
Mus musculus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
-
2.1.1.17
S-adenosyl-L-methionine + phosphatidylethanolamine
the transfer of a methyl group to monomethyl-N-phosphatidylcholine and dimethyl-N,N-phosphatidylcholine is catalyzed by a second enzyme
485177
Mus musculus
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.1.1.17
9
-
-
Mus musculus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
2.1.1.17
S-adenosylhomocysteine
-
Mus musculus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1.1.17
0.02
-
S-adenosyl-L-methionine
-
Mus musculus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
plasma membrane
-
Mus musculus
5886
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
2.1.1.17
Ca2+
1 mM, increases activity
Mus musculus
2.1.1.17
Mg2+
10 mM, increases activity
Mus musculus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.1.17
partial
Mus musculus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
thymocyte
-
Mus musculus
-
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
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
485177
Mus musculus
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
-
-
-
2.1.1.17
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
485177
Mus musculus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
-
2.1.1.17
S-adenosyl-L-methionine + phosphatidylethanolamine
the transfer of a methyl group to monomethyl-N-phosphatidylcholine and dimethyl-N,N-phosphatidylcholine is catalyzed by a second enzyme
485177
Mus musculus
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.1.1.17
9
-
-
Mus musculus