Identification and Properties of Two Methyltransferases in Conversion of Phosphatidylethanolamine to Phosphatidylcholine

Two methyltransferases involved in the methylation of phosphatidylethanolamine to form phosphatidylcholine were demonstrated in a microsomal fraction of bovine adrenal medulla. The first methyltransferase catalyzes the methylation of phosphatidylethanolamine to form phosphatidyl-N-monomethylethanola...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1978-04, Vol.75 (4), p.1718-1721
Main Authors: Hirata, Fusao, Viveros, O. Humberto, Diliberto, Emanuel J., Axelrod, Julius
Format: Article
Language:English
Subjects:
Adrenal medulla
Adrenal Medulla - enzymology
Animals
Cattle
Enzymes
Hydrogen-Ion Concentration
Kinetics
Magnesium - pharmacology
Methylation
Methyltransferases - metabolism
Microsomes - enzymology
Phosphatidylcholines
Phosphatidylcholines - biosynthesis
Phosphatidylethanolamines
Phosphatidylethanolamines - metabolism
Phospholipids
Radioactive decay
S-Adenosylmethionine - metabolism
Sodium
Solvents
Ungulates
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Summary:Two methyltransferases involved in the methylation of phosphatidylethanolamine to form phosphatidylcholine were demonstrated in a microsomal fraction of bovine adrenal medulla. The first methyltransferase catalyzes the methylation of phosphatidylethanolamine to form phosphatidyl-N-monomethylethanolamine. This enzyme has an optimum pH of 6.5, a low Kmfor S-adenosyl-L-methionine (1.4 μ M), and an absolute requirement for Mg2+. The second methyltransferase catalyzes the two successive methylations of phosphatidyl-N-monomethylethanolamine to phosphatidyl-N,N-dimethylethanolamine and phosphatidylcholine. In contrast to the first methyltransferase, it has an optimum pH of 10 and a high Kmfor S-adenosyl-L-methionine (0.1 mM) and does not require Mg2+.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.75.4.1718