Phospholipases C and sphingomyelinases: Lipids as substrates and modulators of enzyme activity

被引：46
作者：
Goni, Felix M. [1 ]
Montes, L-Ruth
Alonso, Alicia [1 ]
机构：
[1] Univ Basque Country, Unidad Biofis, Ctr Mixto CSIC UPV EHU, E-48080 Bilbao, Spain
来源：
PROGRESS IN LIPID RESEARCH | 2012年 / 51卷 / 03期
关键词：
Phospholipase C; Sphingomyelinase; Lipid-protein interactions; Enzyme regulation; Vesicle aggregation; Vesicle fusion; PERFRINGENS ALPHA-TOXIN; PLECKSTRIN HOMOLOGY DOMAIN; HUMAN ACID SPHINGOMYELINASE; PLATELET-ACTIVATING-FACTOR; LARGE UNILAMELLAR VESICLES; SITE-DIRECTED MUTAGENESIS; CERAMIDE-ENRICHED DOMAINS; MEMBRANE-DAMAGING ACTION; LOW-DENSITY-LIPOPROTEIN; CLOSTRIDIUM-PERFRINGENS;
D O I：
10.1016/j.plipres.2012.03.002
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：
This review article deals with phospholipases C (PLC), sphingomyelinases (SMases) and related lipases. Bacterial PC-preferring PLC and PI-specific PLC, bacterial SMases and PLC/SMases, eukaryotic SMases and ceramide phosphorylinositol hydrolases are discussed. The aim of the review is to offer a coherent description of lipid-protein interactions for the above enzymes, considering that (a) the enzyme activity is influenced by the physical properties of the substrate lipid, (b) the enzyme activity is modulated by non-substrate lipids. (c) enzyme end-products often change the physical properties of the lipid matrix, hence the enzyme activity. This approach allows a certain degree of understanding of phenomena such as: latency periods (lag times), enzyme interfacial activation, effects of intrinsic lipid curvature and of overall bilayer curvature on enzyme activity, and enzyme-promoted vesicle aggregation and fusion. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码：238 / 266
页数：29
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