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Fatty Acid Photodecarboxylase Is an Interfacial Enzyme That Binds to Lipid-Water Interfaces to Access Its Insoluble Substrate
- Source :
- Biochemistry, Biochemistry, 2021, ⟨10.1021/acs.biochem.1c00317⟩, Biochemistry, American Chemical Society, 2021, ⟨10.1021/acs.biochem.1c00317⟩
- Publication Year :
- 2021
-
Abstract
- International audience; 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.
- Subjects :
- congenital, hereditary, and neonatal diseases and abnormalities
[SDV.BIO]Life Sciences [q-bio]/Biotechnology
Photoenzyme
Carboxy-Lyases
Phospholipid
Palmitic Acid
Chlorella
7. Clean energy
01 natural sciences
Biochemistry
Micelle
03 medical and health sciences
chemistry.chemical_compound
Biofuel
Animals
Microemulsion
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]
neoplasms
Micelles
Unilamellar Liposomes
030304 developmental biology
chemistry.chemical_classification
0303 health sciences
Liposome
biology
010405 organic chemistry
Algal Proteins
beta-Cyclodextrins
Active site
Fatty acid
Substrate (chemistry)
Water
Serum Albumin, Bovine
Lipids
digestive system diseases
Hydrocarbons
0104 chemical sciences
Kinetics
Membrane
chemistry
biology.protein
Biophysics
Biocatalysis
Cattle
Emulsions
Adsorption
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 60
- Issue :
- 42
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....0395bc0a3e8b4130c0c99c3b00cf7358