Hirata F, Axelrod J
Proc Natl Acad Sci U S A. 1978 May;75(5):2348-52. doi: 10.1073/pnas.75.5.2348.
The synthesis of phosphatidylcholine from phosphatidylethanolamine is carried out by two methyltransferases in erythrocyte membranes. The first enzyme uses phosphatidylethanolamine as a substrate, requires Mg2+, and has a high affinity for methyl donor, S-adenosyl-L-methionine. The second enzyme methylates phosphatidyl-N-monomethylethanolamine to phosphatidylcholine and has a low affinity for S-adenosyl-L-methionine. The first enzyme is localized on the cytoplasmic side of the membrane and the second enzyme faces the external surface. This asymmetric arrangement of the two enzymes across the membrane makes possible the stepwide methylation of phosphatidylethanolamine localized on the cytoplasmic side and facilitates the rapid transmembrane transfer of the final product, phosphatidylcholine, to the external surface of the membrane. A mechanism for an enzyme-mediated flip-flop of phospholipids from the cytoplasmic to the outer surface of erythrocyte membranes is described.
红细胞膜中由磷脂酰乙醇胺合成磷脂酰胆碱是由两种甲基转移酶完成的。第一种酶以磷脂酰乙醇胺为底物,需要Mg2+,且对甲基供体S-腺苷-L-甲硫氨酸具有高亲和力。第二种酶将磷脂酰-N-单甲基乙醇胺甲基化为磷脂酰胆碱,对S-腺苷-L-甲硫氨酸的亲和力较低。第一种酶定位于膜的细胞质侧,第二种酶面向外表面。这两种酶在膜上的这种不对称排列使得位于细胞质侧的磷脂酰乙醇胺能够逐步甲基化,并促进最终产物磷脂酰胆碱快速跨膜转运至膜的外表面。本文描述了一种由酶介导的磷脂从红细胞膜细胞质侧翻转至外表面的机制。