Hirata F, Viveros O H, Diliberto E J, Axelrod J
Proc Natl Acad Sci U S A. 1978 Apr;75(4):1718-21. doi: 10.1073/pnas.75.4.1718.
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+.
在牛肾上腺髓质的微粒体部分发现了两种参与磷脂酰乙醇胺甲基化形成磷脂酰胆碱的甲基转移酶。第一种甲基转移酶催化磷脂酰乙醇胺甲基化形成磷脂酰 - N - 单甲基乙醇胺。这种酶的最适pH为6.5,对S - 腺苷 - L - 甲硫氨酸的Km值较低(1.4微米),并且绝对需要Mg2 +。第二种甲基转移酶催化磷脂酰 - N - 单甲基乙醇胺连续两次甲基化形成磷脂酰 - N,N - 二甲基乙醇胺和磷脂酰胆碱。与第一种甲基转移酶相反,它的最适pH为10,对S - 腺苷 - L - 甲硫氨酸的Km值较高(0.1 mM),并且不需要Mg2 +。