Literature DB >> 2126577

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.

Y Tanaka1, F Amano, M Maeda, M Nishijima, Y Akamatsu.   

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.

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Year:  1990        PMID: 2126577     DOI: 10.7883/yoken1952.43.59

Source DB:  PubMed          Journal:  Jpn J Med Sci Biol        ISSN: 0021-5112


  2 in total

1.  In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity.

Authors:  Rachel Zufferey
Journal:  J Vis Exp       Date:  2016-01-05       Impact factor: 1.355

2.  Characterization of phospholipid methylation in rat brain myelin.

Authors:  V Tsvetnitsky; L Auchi; A Nicolaou; W A Gibbons
Journal:  Biochem J       Date:  1995-04-01       Impact factor: 3.857

  2 in total

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