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    Jpn J Med Sci Biol. 1990 Jun;43(3):59-73.

    Purification and properties of phosphatidyl-N-monomethylethanolamine N-methyltransferase, the enzyme catalyzing the second and the third steps in the phosphatidylethanolamine N-methyltransferase system, from mouse liver microsomes.

    Tanaka Y, Amano F, Maeda M, Nishijima M, Akamatsu Y.

    Source

    Department of Chemistry, National Institute of Health, Tokyo, Japan.

    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.

    PMID:
    2126577
    [PubMed - indexed for MEDLINE]

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