BRENDA - Enzyme Database

Synthesis of phosphatidylcholine from phosphatidylethanolamine by at least two methyltransferases in rat pituitary extracts

Prasad, C.; Edwards, R.M.; J. Biol. Chem. 256, 13000-13003 (1981)
No PubMed abstract available

Data extracted from this reference:

KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1.1.17
0.0067
-
S-adenosylmethionine
-
Rattus norvegicus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
membrane
loosely bound to membrane
Rattus norvegicus
16020
-
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
pituitary gland
-
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
485172
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
485172
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
485172
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
6.5
-
and a second optimum at pH 9.5
Rattus norvegicus
2.1.1.17
9.5
-
and a second optimum at pH 9.5
Rattus norvegicus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1.1.17
0.0067
-
S-adenosylmethionine
-
Rattus norvegicus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.1.1.17
membrane
loosely bound to membrane
Rattus norvegicus
16020
-
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.17
pituitary gland
-
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
485172
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
485172
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
485172
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
6.5
-
and a second optimum at pH 9.5
Rattus norvegicus
2.1.1.17
9.5
-
and a second optimum at pH 9.5
Rattus norvegicus