BRENDA - Enzyme Database

Purification of phospholipid methyltransferase from rat liver microsomal fraction

Pajares, M.A.; Villalba, M.; Mato, J.M.; Biochem. J. 237, 699-705 (1986)

Data extracted from this reference:

Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
microsome
-
Rattus norvegicus
-
-
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.1.17
25000
-
1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
Rattus norvegicus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.1.17
Rattus norvegicus
-
-
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
2.1.1.17
phosphoprotein
the dimeric enzyme form can be phosphorylated by cyclic AMP-dependent protein kinase
Rattus norvegicus
Purification (Commentary)
EC Number
Commentary
Organism
2.1.1.17
-
Rattus norvegicus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
2.1.1.17
0.273
-
-
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
-
485167
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
-
485167
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidylethanolamine
-
485167
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
2.1.1.17
dimer
1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
Rattus norvegicus
2.1.1.17
monomer
1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
Rattus norvegicus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
microsome
-
Rattus norvegicus
-
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.1.17
25000
-
1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
Rattus norvegicus
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
2.1.1.17
phosphoprotein
the dimeric enzyme form can be phosphorylated by cyclic AMP-dependent protein kinase
Rattus norvegicus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.1.17
-
Rattus norvegicus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
2.1.1.17
0.273
-
-
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
-
485167
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N,N-dimethylethanolamine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine
-
485167
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidylcholine
-
-
-
?
2.1.1.17
S-adenosyl-L-methionine + phosphatidylethanolamine
-
485167
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.1.1.17
dimer
1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
Rattus norvegicus
2.1.1.17
monomer
1 * 25000, enzyme can exist as monomer and as dimer, SDS-PAGE
Rattus norvegicus