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Ligand phosphatidyl-N-monomethylethanolamine Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C1 0 H1 8 NO8 PR2
phosphatidyl-N-monomethylethanolamine
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (2 results)
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2 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine = S-adenosyl-L-homocysteine + phosphatidylcholine
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S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
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Product in Enzyme-catalyzed Reactions (1 result)
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S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-monomethylethanolamine
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Enzyme Kinetic Parameters
KM Value (4 results)
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References & Links Literature References (5)
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Phosphatidylethanolamine methyltransferase and phospholipid methyltransferase activities from Saccharomyces cerevisiae. Enzymological and kinetic properties
1990
Gaynor, P.M.; Carman, G.M.
Biochim. Biophys. Acta
1045
156-163
Conversion of phosphatidylethanolamine to phosphatidylcholine in rat liver. Partial purification and characterization of the enzymatic activities
1979
Schneider, W.J.; Vance, D.E.
J. Biol. Chem.
254
3886-3891
Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine
1978
Hirata, F.; Viveros, O.H.; Diliberto, E.J.; Axelrod, J.
Proc. Natl. Acad. Sci. USA
75
1718-1721
Evidence for two methyltransferase involved in the conversion of phosphatidylethanolamine to phosphatidylcholine in the rat liver
1981
Sastry, B.V.R.; Statham, C.N.; Axelrod, J.; Hirata, F.
Arch. Biochem. Biophys.
211
762-773
Functional characterization of phospholipid N-methyltransferases from Arabidopsis and soybean
2009
Keogh, M.R.; Courtney, P.D.; Kinney, A.J.; Dewey, R.E.
J. Biol. Chem.
284
15439-15447
Links to other databases for phosphatidyl-N-monomethylethanolamine