Yıl 2019, Cilt 8 , Sayı 1, Sayfalar 26 - 38 2019-03-12

Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species
Analysis of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species

Fırat KURT [1] , Ertuğrul FİLİZ [2]


Cinnamyl 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.

Cinnamyl 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. 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 value was found as follows:  Fragaria vesca-Prunus persica clade (100%), Glycine max-Medicago 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.

  • 1. Lange, B.M., Lapierre, C. and Sandermann, J.H. (1995) Elicitor-induced spruce stress lignin. Structural similarity to early developmental lignins. Plant Physiol. 108: 1277–1287
  • 2. Tronchet M, Balagué C, Kroj T, Jouanin L, Roby D 2010. Cinnamyl alcohol dehydrogenases-C and D, key enzymes in lignin biosynthesis, play an essential role in disease resistance in Arabidopsis. Molecular Plant Pathology 11: 83–92
Birincil Dil en
Konular Fen
Bölüm Araştırma Makalesi
Yazarlar

Yazar: Fırat KURT
Kurum: MUŞ ALPARSLAN UNIVERSITY, FACULTY OF APPLIED SCIENCES
Ülke: Turkey


Yazar: Ertuğrul FİLİZ (Sorumlu Yazar)
Kurum: ÇİLİMLİ VOCATIONAL SCHOOL
Ülke: Turkey


Tarihler

Yayımlanma Tarihi : 12 Mart 2019

Bibtex @araştırma makalesi { bitlisfen462778, journal = {Bitlis Eren Üniversitesi Fen Bilimleri Dergisi}, issn = {2147-3129}, eissn = {2147-3188}, address = {}, publisher = {Bitlis Eren Üniversitesi}, year = {2019}, volume = {8}, pages = {26 - 38}, doi = {10.17798/bitlisfen.462778}, title = {Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species}, key = {cite}, author = {KURT, Fırat and FİLİZ, Ertuğrul} }
APA KURT, F , FİLİZ, E . (2019). Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species. Bitlis Eren Üniversitesi Fen Bilimleri Dergisi , 8 (1) , 26-38 . DOI: 10.17798/bitlisfen.462778
MLA KURT, F , FİLİZ, E . "Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species". Bitlis Eren Üniversitesi Fen Bilimleri Dergisi 8 (2019 ): 26-38 <https://dergipark.org.tr/tr/pub/bitlisfen/issue/43819/462778>
Chicago KURT, F , FİLİZ, E . "Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species". Bitlis Eren Üniversitesi Fen Bilimleri Dergisi 8 (2019 ): 26-38
RIS TY - JOUR T1 - Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species AU - Fırat KURT , Ertuğrul FİLİZ Y1 - 2019 PY - 2019 N1 - doi: 10.17798/bitlisfen.462778 DO - 10.17798/bitlisfen.462778 T2 - Bitlis Eren Üniversitesi Fen Bilimleri Dergisi JF - Journal JO - JOR SP - 26 EP - 38 VL - 8 IS - 1 SN - 2147-3129-2147-3188 M3 - doi: 10.17798/bitlisfen.462778 UR - https://doi.org/10.17798/bitlisfen.462778 Y2 - 2019 ER -
EndNote %0 Bitlis Eren Üniversitesi Fen Bilimleri Dergisi Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species %A Fırat KURT , Ertuğrul FİLİZ %T Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species %D 2019 %J Bitlis Eren Üniversitesi Fen Bilimleri Dergisi %P 2147-3129-2147-3188 %V 8 %N 1 %R doi: 10.17798/bitlisfen.462778 %U 10.17798/bitlisfen.462778
ISNAD KURT, Fırat , FİLİZ, Ertuğrul . "Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species". Bitlis Eren Üniversitesi Fen Bilimleri Dergisi 8 / 1 (Mart 2019): 26-38 . https://doi.org/10.17798/bitlisfen.462778
AMA KURT F , FİLİZ E . Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species. Bitlis Eren Üniversitesi Fen Bilimleri Dergisi. 2019; 8(1): 26-38.
Vancouver KURT F , FİLİZ E . Bioinformatical Analyses of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species. Bitlis Eren Üniversitesi Fen Bilimleri Dergisi. 2019; 8(1): 38-26.