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Updated: May 23, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Phospholipases C and sphingomyelinases: Lipids as substrates and modulators of enzyme activity
Félix M Goñi1, L-Ruth Montes, Alicia Alonso
1Unidad de Biofísica, Centro Mixto CSIC-UPV/EHU, Universidad del País Vasco, Aptdo. 644, 48080 Bilbao, Spain. felix.goni@ehu.es
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.
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