title: Phospholipases C and sphingomyelinases: Lipids as substrates and modulators of enzyme activity.
abstract: 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.
authors.affiliation: Unidad de Biofísica, Centro Mixto CSIC-UPV/EHU, Universidad del País Vasco, Aptdo. 644, 48080 Bilbao, Spain. felix.goni@ehu.es
authors.forename: Félix M
authors.initials: FM
authors.lastname: Goñi
authors.forename: L-Ruth
authors.initials: LR
authors.lastname: Montes
authors.forename: Alicia
authors.initials: A
authors.lastname: Alonso
mesh_terms: D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D050356:Lipid Metabolism; D013108:Sphingomyelin Phosphodiesterase / Q000378:metabolism*; D010738:Type C Phospholipases / Q000378:metabolism*
chemical_list: D010738:Type C Phospholipases; D013108:Sphingomyelin Phosphodiesterase