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. 1978 Apr;75(4):1718–1721. doi: 10.1073/pnas.75.4.1718

Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine.

F Hirata, O H Viveros, E J Diliberto Jr, J Axelrod
PMCID: PMC392410  PMID: 25437

Abstract

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 Km for S-adenosyl-L-methionine (1.4 micron), and an absolute requirement for Mg2+. The second methyltransferase catalyzes the two successive methylations of phodphatidyl-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 Km for S-adenosyl-L-methionine (0.1 mM) and does not require Mg2+.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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