Lipid dependence and activity control of phosphatidylserine synthase from Escherichia coli

被引：13

作者：

Linde, K ^{[1
]}

Gröbner, G ^{[1
]}

Rilfors, L ^{[1
]}

机构：

[1] Umea Univ, Dept Biophys Chem, SE-90187 Umea, Sweden

来源：

FEBS LETTERS | 2004年 / 575卷 / 1-3期

关键词：

phosphatidylserine synthase; mixed micelles; cooperative hill kinetics; lipid activation; Escherichia coli;

D O I：

10.1016/j.febslet.2004.08.038

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The activity of phosphatidylserine synthase from Escherichia coli depends significantly on the nature and level of the lipids in the matrix, at which the enzyme is operating. To elucidate the role of anionic lipids in the regulation of PtdSer synthase, its activity was studied in mixed micelles containing phosphatidylglycerol (one charge) or diphosphatidylglycerol (two charges), the two main anionic membrane lipids in E. coli. Membrane association and activity of PtdSer synthase were increased by the two lipids, indicating their essential role in the positive regulation mechanism of the phosphatidylethanolamine level in the E. coli membrane. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：77 / 80

页数：4

共 29 条

[1]

[Anonymous], 1985, Enzyme Structure and Mechanism

[2]

CARMAN GM, 1979, J BIOL CHEM, V254, P8391

[3] LIPID SIGNALING ENZYMES AND SURFACE DILUTION KINETICS [J].