title: Exploring the specific features of interfacial enzymology based on lipase studies.
abstract: Many enzymes are active at interfaces in the living world (such as in the signaling processes at the surface of cell membranes, digestion of dietary lipids, starch and cellulose degradation, etc.), but fundamental enzymology remains largely focused on the interactions between enzymes and soluble substrates. The biochemical and kinetic characterization of lipolytic enzymes has opened up new paths of research in the field of interfacial enzymology. Lipases are water-soluble enzymes hydrolyzing insoluble triglyceride substrates, and studies on these enzymes have led to the development of specific interfacial kinetic models. Structure-function studies on lipases have thrown light on the interfacial recognition sites present in the molecular structure of these enzymes, the conformational changes occurring in the presence of lipids and amphiphiles, and the stability of the enzymes present at interfaces. The pH-dependent activity, substrate specificity and inhibition of these enzymes can all result from both "classical" interactions between a substrate or inhibitor and the active site, as well as from the adsorption of the enzymes at the surface of aggregated substrate particles such as oil drops, lipid bilayers or monomolecular lipid films. The adsorption step can provide an alternative target for improving substrate specificity and developing specific enzyme inhibitors. Several data obtained with gastric lipase, classical pancreatic lipase, pancreatic lipase-related protein 2 and phosphatidylserine-specific phospholipase A1 were chosen here to illustrate these specific features of interfacial enzymology.
authors.affiliation: Laboratoire d'Enzymologie Interfaciale et de Physiologie de la Lipolyse, CNRS UPR 9025, 31 Chemin Joseph Aiguier, 13009 Marseille Cedex 20, France.
authors.forename: Ahmed
authors.initials: A
authors.lastname: Aloulou
authors.forename: Jorge A
authors.initials: JA
authors.lastname: Rodriguez
authors.forename: Sylvie
authors.initials: S
authors.lastname: Fernandez
authors.forename: Dirk
authors.initials: D
authors.lastname: van Oosterhout
authors.forename: Delphine
authors.initials: D
authors.lastname: Puccinelli
authors.forename: Frédéric
authors.initials: F
authors.lastname: Carrière
mesh_terms: D000327:Adsorption; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism*; D004789:Enzyme Activation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry*; D008958:Models, Molecular; D010741:Phospholipases A / Q000737:chemistry / Q000378:metabolism; D054466:Phospholipases A1; D011487:Protein Conformation; D013379:Substrate Specificity; D013499:Surface Properties; D014280:Triglycerides / Q000378:metabolism
chemical_list: D008049:Lipase; D008055:Lipids; D010741:Phospholipases A; D054466:Phospholipases A1; D014280:Triglycerides; C485982:LIPF protein, human; C075988:pancreatic lipase related protein 2; C512665:PLA1A protein, human