Fatty Acid Photodecarboxylase Is an Interfacial Enzyme That Binds to Lipid–Water Interfaces to Access Its Insoluble Substrate

• DOI: 10.1021/acs.biochem.1c00317
• Publication Date: 2021-10-11T13:35:09Z
• Authors: Cyril Aselmeyer; Bertrand Légeret; Anaïs Bénarouche; Damien Sorigué; Goetz Parsiegla; Fred Beisson; Frédéric Carrière
• Keywords: Hydrophobic effect

Fatty acid photodecarboxylase (FAP), one of the few natural photoenzymes characterized so far, is a promising biocatalyst for lipid-to-hydrocarbon conversion using light. However, optimum supramolecular organization under which fatty (FA) substrate should be presented to FAP has not been addressed. Using palmitic embedded in phospholipid liposomes, phospholipid-stabilized microemulsions, and mixed micelles, we show that displays preference FAs present liposomes at surface microemulsions. The kinetics adsorption onto galactolipid monomolecular films further suggests ability bind penetrate into membranes, with higher affinity presence FAs. structure reveals potential interfacial recognition site clusters hydrophobic basic residues surrounding active entrance. resulting dipolar moment orientation negatively charged interfaces. These findings provide important clues about mode action development FAP-based bioconversion processes.