Acyl glycerol hydrolases: inhibitors, interface and catalysis
Related Experiment Video
Updated: Nov 4, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
C Cambillau1, S Longhi, A Nicolas
1Architecture et Fonction des Macromolécules Biologiques, UPR 9039, CNRS, IFR, 131 Chemin Joseph Aiguier, 13402 Marseille, CEDEX 20, France. cambilau@ibsm.cnrs-mrs.fr
Abstract:
The last five years have witnessed the solution of a large number of lipase structures, which has led, among other insights, to the structural interpretation of the interfacial activation phenomenon in terms of 'lid' opening. This interpretation has been extended this year to include phospholipase A2. Recent structural studies on lipases have provided data on the detailed mechanisms underlying the behaviour of lipases: how they bind to inhibitors or substrates, and what interactions occur between their hydrophobic face and hydrophobic molecules, for example. In addition, studies on cutinase point mutants have shed some light on the role of the oxyanion hole in lipolytic catalysis.
Related Concept Videos
Enzyme Inhibition
Enzymes
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
Lysosomal Hydrolases
Protein-protein Interfaces
Catalytically Perfect Enzymes
