Comparative and evolutionary analysis of α-amylase gene across monocots and dicots

Abstract

α-amylase is an important enzyme involved in starch degradation to provide energy to the germinating seedling. The present study was conducted to reveal structural and functional evolution of this gene among higher plants. Discounting polyploidy, most plant species showed only a single copy of the gene making multiple isoforms in different tissues and developmental stages. Genomic length of the gene ranged from 1472 bp in wheat to 2369 bp in soybean, and the size variation was mainly due to differences in the number and size of introns. In spite of this variation, the intron phase distribution and insertion sites were mostly conserved. The predicted protein size ranged from 414 amino acid (aa) in soybean to 449aa in Brachypodium. Overall, the protein sequence similarity among orthologs ranged from 56.4 to 97.4 %. Key motifs and domains along with their relative distances were conserved among plants although several species, genera, and class specific motifs were identified. The glycosyl hydrolase superfamily domain length varied from 342aa in soybean to 384aa in maize and sorghum while length of the C-terminal β-sheet domain was highly conserved with 61aa in all monocots and Arabidopsis but was 59aa in soybean and Medicago. Compared to rice, 3D structure of the proteins showed 89.8 to 91.3 % similarity among the monocots and 72.7 to 75.8 % among the dicots. Sequence and relative location of the five key aa required for the ligand binding were highly conserved in all species except rice.

Gas chromatography-mass spectrometry analysis of variations in the essential leaf oil of 6 Eucalyptus Species and allelopathy of mechanism 1,8-cineole

“…The allelopathy of 1,8-cineole was the strongest and exerted a huge effect on wheat germination. For further investigation of the allelopathic mechanism, wheat seeds that were germinated by adding 1,8-cineole in the above experiments were selected (i) to determine the differences in the α-amylase activity (amylase strongly influences seed germination) (SETHI et al, 2016) and (ii) to study the differences in the mRNA expression that affected the synthesis of amylase in the seeds. Simultaneously, the inhibition of 1,8-cineole was evaluated in further detail.…”

New insight in cereal starch degradation: identification and structural characterization of four α-amylases in bread wheat

“…Amino acid sequence genesis, alignments, annotations and comparisons were performed according to recent study by Sethi et al [44] as well as using the Geneious …”

Genome-Wide Identification and Preliminary Functional Analysis of BAM (β-Amylase) Gene Family in Upland Cotton

“…Starch is temporarily stored in chloroplasts, seeds, and other specialized starch storage organs for a long time [2,3]. Starch is degraded by a series of enzymes (including α-amylase (AMY), β-amylase (BAM), limit dextrinase (PUL), β-glucosidase and α-glucan phosphorylase (PHO)) to release primary chemical energy and organic matter for plant growth, development, and response to abiotic stress [4][5][6][7][8][9]. The β-amylase (BAM) family is named for the ability to catalyze the hydrolysis of starch into maltose units by its catalytic members.…”