Insight into Arthrospira platensis Δ9 desaturase: a key enzyme in poly-unsaturated fatty acid synthesis

Molecular Biology Reports
Faten Ben AmorImen Fendri

Abstract

Membrane-bound Δ9 desaturase perform oxygenated desaturation reactions to insert the first double bonds within fatty acyl chains between C9 and C10 positions of most saturated substrates. Arthrospira platensis, a blue green microalga, is an important source of polyunsaturated fatty acids (PUFA) such as oleic, linoleic and linolenic acids lending benefits and functions in dietetics and therapeutic uses. In this paper, we report homology modeling and docking studies of a Δ9 desaturase from Arthrospira platensis strain. The protein model showed high topology resemblance compared to membrane-bound desaturases with a cytoplasmic core displaying the catalytic site and a transmembrane domain created by four α-helices. The cytoplasmic cap contained the three conserved-histidine boxes typical for all membrane bound desaturases. The protein model was used to perform protein-protein docking and the dimer structure was generated. The two monomers are tightly related with hydrophobic interactions between the transmembrane domain helices. The study highlighted also the potent role of a particular 53 residues sequence located at the N terminal end of the enzyme.

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Citations

Nov 18, 2020·International Journal of Biological Macromolecules·Jihen ElleuchSlim Abdelkafi

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Methods Mentioned

BETA
PCR
acetylation

Software Mentioned

TMHMM
NetAcet
NetNGlyc
PyMol Molecular Graphics System
PROCHECK
NetCGlyc
coffee
NetPhos
MSA viewer
MPI Bioinformatics Toolkit

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