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dc.contributor.authorFİLİZ, Ertuğrul
dc.contributor.authorKURT, Fırat
dc.date.accessioned2024-02-19T12:11:55Z
dc.date.available2024-02-19T12:11:55Z
dc.date.issued2019
dc.identifier.issn2147-3188
dc.identifier.urihttp://dspace.beu.edu.tr:8080/xmlui/handle/123456789/14129
dc.description.abstractCinnamyl alcohol dehydrogenase (CAD) (EC 1.1.1.195) is an enzyme functioning in the reduction of various phenylpropenyl aldehyde derivatives which are precursors in lignin and lignan production. Species-specific CAD genes have been extensively identified in recent years. In this study, we used bioinformatics tools to characterize and classify plant CADs. The amino acid and nucleotide sequences of 16 CADs from different plant species were used to compare their physiological properties, phylogeny, and conserved motifs. For this purpose, sequence, phylogenetical, structural analyses of proteins were conducted using various servers. All plant CADs had the characteristic alcohol dehydrogenase (PF08240) and zinc-binding dehydrogenase domains (PF00107). According to the physicochemical analysis, it was revealed that the most of plant CADs (81.25%) were in acidic character. Sequence length (aa) and molecular weight (kDa) of CAD proteins were found in range of 356 -367 and 38.6-40.5 respectively. The highest sequence similarities were found between Sorghum bicolor and Zea mays (95.3%), Panicum virgatum and Sorghum bicolor (90.9%), and Oryza sativa and Zea mays (87.1%) respectively. Plant CADs showed divergent exon-intron structures in which exon numbers were ranged from two to six. Four monocot species (S. bicolor, P. virgatum, Z. mays, and O. sativa) have four exons, whereas Brachypodium distachyon contains only two exons. Phylogenetic analysis revealed that the CAD proteins mainly divided into two groups. The highest bootstrap values were found as follows: Fragaria vesca-Prunus persica clade (100%), Glycine maxMedicago truncatula (81%), and S. bicolor-Z. mays (72%). The 3D structures of plant CADs showed that Oryza and Vitis had the most divergent structures when compared to the other plant species. Eventually, the data represented here contribute to studies aiming at evaluating the plant CADs extensively and at identifying new CAD genes in other plants.tr_TR
dc.language.isoEnglishtr_TR
dc.publisherBitlis Eren Üniversitesitr_TR
dc.rightsinfo:eu-repo/semantics/openAccesstr_TR
dc.subject3D structuretr_TR
dc.subjectCinnamyl alcohol dehydrogenase (CADs)tr_TR
dc.subjectcomparative phylogeneticstr_TR
dc.subjectin silico analysistr_TR
dc.titleBioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant speciestr_TR
dc.typeArticletr_TR
dc.identifier.issue1tr_TR
dc.identifier.startpage26tr_TR
dc.identifier.endpage38tr_TR
dc.relation.journalBitlis Eren Üniversitesi Fen Bilimleri Dergisitr_TR
dc.identifier.volume8tr_TR


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