03440nas a2200313   4500008004100000245016600041210006900207260000800276300000800284490000700292520240600299653000902705653001602714653002502730653002402755653001302779653001002792653000802802653002402810100002002834700002002854700001902874700002102893700001902914700002202933700002002955700002402975856012702999       2022                        eng d00aComparative analysis and structural modeling of elaeis oleifera FAD2, a fatty acid desaturase involved in unsaturated fatty acid composition of american oil palm0 aComparative analysis and structural modeling of elaeis oleifera   cAPR  a5290 v113 a<p>
	Simple Summary Palm oil has become the world's most important vegetable oil in terms of production quantity, and its overall demand is exponentially growing with the global population. The fatty acid composition and particularly the oleic/linoleic acid ratio are major factors influencing palm oil quality. In this study, we focused on FAD2, a fatty acid desaturase enzyme involved in the desaturation and conversion of oleic acid to linoleic acid in Elaeis oleifera, identified through in silico annotation analysis. Our phylogenetic and comparative studies revealed two SNP markers, SNP278 and SNP851, significantly correlated with the oleic/linoleic acid contents. Our study provides fundamental insights into the mechanism of fatty acids synthesis in oil palm and could support the application of molecular biology techniques to enhance the enzymatic activity and substrate affinity of EoFAD2. American oil palm (Elaeis oleifera) is an important source of dietary oil that could fulfill the increasing worldwide demand for cooking oil. Therefore, improving its production is crucial and could be realized through breeding and genetic engineering approaches aiming to obtain high-yielding varieties with improved oil content and quality. The fatty acid composition and particularly the oleic/linoleic acid ratio are major factors influencing oil quality. Our work focused on a fatty acid desaturase (FAD) enzyme involved in the desaturation and conversion of oleic acid to linoleic acid. Following the in silico identification and annotation of Elaeis oleifera FAD2, its molecular and structural features characterization was performed to better understand the mechanistic bases of its enzymatic activity. EoFAD2 is 1173 nucleotides long and encodes a protein of 390 amino acids that shares similarities with other FADs. Interestingly, the phylogenetic study showed three distinguished groups where EoFAD2 clustered among monocotyledonous taxa. EoFAD2 is a membrane-bound protein with five transmembrane domains presumably located in the endoplasmic reticulum. The homodimer organization model of EoFAD2 enzyme and substrates and respective substrate-binding residues were predicted and described. Moreover, the comparison between 24 FAD2 sequences from different species generated two interesting single-nucleotide polymorphisms (SNPs) associated with the oleic/linoleic acid contents.</p>
10aFAD210aFatty acids10ain silico annotation10alinoleic acid ratio10aoil palm10aoleic10aSNP10astructural modeling1 aBen Ayed, Rayda1 aChirmade, Tejas1 aHanana, Mohsen1 aKhamassi, Khalil1 aErcisli, Sezai1 aChoudhary, Ravish1 aKadoo, Narendra1 aKarunakaran, Rohini  uhttps://library.ncl.res.in/content/comparative-analysis-and-structural-modeling-elaeis-oleifera-fad2-fatty-acid-desaturase