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.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Ben Amor F,Ben Hlima H,Abdelkafi S,Fendri Idoi
10.1007/s11033-018-4333-2subject
Has Abstractpub_date
2018-12-01 00:00:00pages
1873-1879issue
6eissn
0301-4851issn
1573-4978pii
10.1007/s11033-018-4333-2journal_volume
45pub_type
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