Multiple phospholipid substrates of phospholipase C/sphingomyelinase HR2 from Pseudomonas aeruginosa

被引：15
|
作者：
Lopez, David J. [1 ,2 ]
Isabel Collado, M. [3 ]
Ibarguren, Maitane [1 ,2 ]
Vasil, Adriana I. [4 ]
Vasil, Michael L. [4 ]
Goni, Felix M. [1 ,2 ]
Alonso, Alicia [1 ,2 ]
机构：
[1] Univ Basque Country, Unidad Biofis, Ctr Mixto CSIC UPV EHU, Bilbao 48940, Spain
[2] Univ Basque Country, Dept Bioquim, Bilbao 48940, Spain
[3] Univ Basque Country, Serv Gen Resonancia Magnet Nucl, Bilbao 48940, Spain
[4] Univ Colorado Denver, Anschutz Med Ctr, Dept Microbiol, Aurora, CO USA
来源：
CHEMISTRY AND PHYSICS OF LIPIDS | 2011年 / 164卷 / 01期
关键词：
Phospholipase C/sphingomyelinase HR2; Pseudomonas aeruginosa; Phospholipase C; Sphingomyelinase; MEMBRANE-FUSION; SPHINGOMYELINASE; MODULATION; PURIFICATION; VESICLES;
D O I：
10.1016/j.chemphyslip.2010.11.001
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 phospholipase C/sphingomyelinase HR2 (PlcHR(2)) from Pseudomonas aeruginosa was characterized on a variety of substrates. The enzyme was assayed on liposomes (large unilamellar vesicles) composed of PC:SM:Ch:X (1:1:1:1; mol ratio) where X could be PE, PS, PG, or CL Activity was measured directly as disappearance of substrate after TLC lipid separation. Previous studies had suggested that PlcHR(2) was active only on PC or SM. However we found that, of the various phospholipids tested, only PS was not a substrate for PlcHR2. All others were degraded, in an order of preference PC > SM > CL > PE > PG. PlcHR(2) activity was sensitive to the overall lipid composition of the bilayer, including non-substrate lipids. (C) 2010 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码：78 / 82
页数：5
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