<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ben Ayed, Rayda</style></author><author><style face="normal" font="default" size="100%">Chirmade, Tejas</style></author><author><style face="normal" font="default" size="100%">Hanana, Mohsen</style></author><author><style face="normal" font="default" size="100%">Khamassi, Khalil</style></author><author><style face="normal" font="default" size="100%">Ercisli, Sezai</style></author><author><style face="normal" font="default" size="100%">Choudhary, Ravish</style></author><author><style face="normal" font="default" size="100%">Kadoo, Narendra</style></author><author><style face="normal" font="default" size="100%">Karunakaran, Rohini</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparative analysis and structural modeling of elaeis oleifera FAD2, a fatty acid desaturase involved in unsaturated fatty acid composition of american oil palm</style></title><secondary-title><style face="normal" font="default" size="100%">Biology-Basel</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">FAD2</style></keyword><keyword><style  face="normal" font="default" size="100%">Fatty acids</style></keyword><keyword><style  face="normal" font="default" size="100%">in silico annotation</style></keyword><keyword><style  face="normal" font="default" size="100%">linoleic acid ratio</style></keyword><keyword><style  face="normal" font="default" size="100%">oil palm</style></keyword><keyword><style  face="normal" font="default" size="100%">oleic</style></keyword><keyword><style  face="normal" font="default" size="100%">SNP</style></keyword><keyword><style  face="normal" font="default" size="100%">structural modeling</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">11</style></volume><pages><style face="normal" font="default" size="100%">529</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
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	5.168&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Salunke, Gayatri</style></author><author><style face="normal" font="default" size="100%">Badhe, Yogesh</style></author><author><style face="normal" font="default" size="100%">Singh, Vrijendra</style></author><author><style face="normal" font="default" size="100%">Ghorpade, Prakash</style></author><author><style face="normal" font="default" size="100%">Hegde, Mahabaleshwar</style></author><author><style face="normal" font="default" size="100%">Kadoo, Narendra</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular insights into the oleic acid accumulation in safflower</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of the American Oil Chemists Society</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Carthamus tinctorius</style></keyword><keyword><style  face="normal" font="default" size="100%">FAD2</style></keyword><keyword><style  face="normal" font="default" size="100%">FATB</style></keyword><keyword><style  face="normal" font="default" size="100%">Fatty acid desaturase</style></keyword><keyword><style  face="normal" font="default" size="100%">fatty acid thioesterase</style></keyword><keyword><style  face="normal" font="default" size="100%">linoleic acid</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">102</style></volume><pages><style face="normal" font="default" size="100%">351-363</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Most of the Indian safflower (Carthamus tinctorius L.) varieties produce oil rich in linoleic acid (LA, similar to 75%) and low in oleic acid (OA, similar to 15%). In the fatty acid biosynthetic pathway, the fatty acid desaturase 2 (FAD2) enzyme converts OA to LA. Safflower is reported to have 12-20 FAD2 genes. Gene expression analysis of four FAD2 genes during seed development in a high LA variety, PBNS-12, revealed high expression of FAD2-1 at 21 days after flowering (DAF), correlating with high LA accumulation. Fatty acid profiling of 448 Indian safflower germplasm accessions revealed four lines to have high (58%-77%) OA content, with NASF-39 having the highest OA content. Interestingly, all four high OA lines showed the same mutation in the FAD2-1 gene. The DNA sequence of FAD2-1 from the four high OA lines showed a deletion of C at the +606 position, resulting in a premature stop codon at the +733 position and a truncated protein of 244 amino acids. Hence, despite the high expression levels of FAD2-1 in NASF-39 at 18-21 DAF, it exhibited high OA (77%). The dysfunctional nature of the truncated FAD2-1 in NASF-39 was evident in molecular docking studies with 1-stearoyl-2-oleoyl phosphatidylcholine. We also sequenced FATB, a thioesterase responsible for releasing stearic acid from acyl carrier protein for further desaturation to oleic acid, where an A773G substitution was observed. This resulted in E258G substitution in NASF-39 FATB compared to that of PBNS-12. This probably made the acyl-binding pocket of NASF-39 FATB unstable, contributing to high OA accumulation. Thus, the outcomes of this study can help develop super and ultra-high oleic safflower varieties through various genetics and genomics approaches.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
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	1.9&lt;/p&gt;
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