BRENDA - Enzyme Database

Synthesis of phosphatidylcholine by two distinct methyltransferases in rat colonic brush-border membranes: evidence for extrinsic and intrinsic membrane activities

Dudeja, P.K.; Foster, E.S.; Brasitus, T.A.; Biochim. Biophys. Acta 875, 493-500 (1986)

Data extracted from this reference:

General Stability
EC Number
General Stability
Organism
2.1.1.17
20% loss of activity after trypsin treatment, 0.001 mg trypsin per 0.05 mg membrane protein
Rattus norvegicus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1.1.17
0.11
-
S-adenosylmethionine
-
Rattus norvegicus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
brush border
-
Rattus norvegicus
5903
-
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
colon
-
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
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
485173
Rattus norvegicus
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
485173
Rattus norvegicus
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
485173
Rattus norvegicus
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.1.1.17
8
-
-
Rattus norvegicus
General Stability (protein specific)
EC Number
General Stability
Organism
2.1.1.17
20% loss of activity after trypsin treatment, 0.001 mg trypsin per 0.05 mg membrane protein
Rattus norvegicus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1.1.17
0.11
-
S-adenosylmethionine
-
Rattus norvegicus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
brush border
-
Rattus norvegicus
5903
-
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
colon
-
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
the transfer of a methyl group to phosphatidyl-N-methylethanolamine and phosphatidyl-N,N-dimethylethanolamine is catalyzed by a second enzyme
485173
Rattus norvegicus
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
485173
Rattus norvegicus
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
485173
Rattus norvegicus
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
8
-
-
Rattus norvegicus