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

页码：238 / 266

页数：29

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