Fatty Acid Photodecarboxylase Is an Interfacial Enzyme That Binds to Lipid–Water Interfaces to Access Its Insoluble Substrate - Archive ouverte HAL Access content directly
Journal Articles Biochemistry Year : 2021

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

Abstract

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, the optimum supramolecular organization under which the fatty acid (FA) substrate should be presented to FAP has not been addressed. Using palmitic acid embedded in phospholipid liposomes, phospholipid-stabilized microemulsions and mixed micelles, we show that FAP displays a preference for FAs present in liposomes and at the surface of microemulsions. Adsorption kinetics onto phospholipid and galactolipid monomolecular films further suggests the ability of FAP to bind to and penetrate into membranes, with higher affinity in the presence of FAs. FAP structure reveals a potential interfacial recognition site with clusters of hydrophobic and basic residues surrounding the active site entrance. The resulting dipolar moment suggests the orientation of FAP at negatively charged interfaces. These findings provide important clues for the mode of action of FAP and the development of FAP-based bioconversion processes.
Fichier principal
Vignette du fichier
Aselmeyer-2021_accepted manuscript.pdf (2.85 Mo) Télécharger le fichier
Origin : Files produced by the author(s)

Dates and versions

hal-03381197 , version 1 (16-10-2021)

Identifiers

Cite

Cyril Aselmeyer, Bertrand Légeret, Anaïs Bénarouche, Damien Sorigué, Goetz Parsiegla, et al.. Fatty Acid Photodecarboxylase Is an Interfacial Enzyme That Binds to Lipid–Water Interfaces to Access Its Insoluble Substrate. Biochemistry, 2021, ⟨10.1021/acs.biochem.1c00317⟩. ⟨hal-03381197⟩
90 View
219 Download

Altmetric

Share

Gmail Facebook X LinkedIn More