Abstract
The phosphatidylethanolamine (PE) N-methyltransferase (MT) system is known to convert PE to phosphatidylcholine by three successive N-methylations. Phosphatidyl-N-monomethylethanolamine (PME) MT was purified 1,400-fold from mouse liver microsomes and separated from the PE-MT activity for the first time. This enzyme catalyzes N-methylations of PME and phosphatidyl-N,N-dimethylethanolamine, the intermediates of PE-MT system, but not PE, the initial substrate of the PE-MT system. In addition, a preparation with a different affinity to S-adenosyl-L-homocysteine catalyzing all the three methylations was obtained. These results suggest that at least two enzymes are involved in the PE-MT system.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Edetic Acid / pharmacology
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Hydrogen-Ion Concentration
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In Vitro Techniques
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Magnesium Chloride / pharmacology
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Male
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Methylation
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Methyltransferases / isolation & purification*
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Methyltransferases / metabolism
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Mice
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Microsomes, Liver / metabolism
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Phosphatidyl-N-Methylethanolamine N-Methyltransferase
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Phosphatidylcholines / metabolism
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Phosphatidylethanolamine N-Methyltransferase
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Phosphatidylethanolamines / metabolism
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Substrate Specificity
Substances
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Phosphatidylcholines
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Phosphatidylethanolamines
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phosphatidyl-N-monomethylaminoethanol
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Magnesium Chloride
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Edetic Acid
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Methyltransferases
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Phosphatidylethanolamine N-Methyltransferase
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Phosphatidyl-N-Methylethanolamine N-Methyltransferase