Analysis of HMG-CoA Reductase Protein in Poaceae Family and Animals Samples by using Bioinformatics ToolsJournal: International Journal of Science and Research (IJSR) (Vol.9, No. 10)
Publication Date: 2020-10-05
Authors : Rodhan Patke;
Page : 335-342
Keywords : HMG-CoA; Terpenoids; Bioinformatics;
Chemically Terpenoids are made up of a basic five-carbon isoprene unit (2-methyl-1, 3-butadiene) and are among the first known biomolecules, with hopanoids having been recouped from residues as old as 2.5 billion years. The isoprenoids are the biggest category of organic products, enveloping more than 55, 000 known compounds till date with various biochemical abilities, of which some are quinones in electron transport chains, as segments of membrane, in cell regulation, as photosynthetic colours, as hormones, and as plant defence compounds. Dimethylallyl diphosphate and isopentenyl diphosphate (IPP) are two fundamental compounds required for production of Terpenoids. Plants utilize two specific process of IPP biosynthesis- the mevalonate pathway and deoxyxylulose 5-phosphate pathway. The developmental history of the compounds associated with the two courses and the phylogenetic relation of their qualities across genomes propose that the mevalonate pathway has its origin accredited to archae bacteria, and the DXP pathway has its roots of origin to eubacteria, and that eukaryotes have acquired their properties for IPP biosynthesis from prokaryotes. The HMG-CoA Reductase enzyme catalyses the transformation of HMG-CoA to mevalonate, which is the initial stage in the mevalonate pathway for biosynthesis of trepenoids in plants. In this examination, multiple sequence alignment of an aggregate of ninety nine HMG-CoA Reductase protein sequences from Poaceae family and three protein sequences from animal samples including Homo sapiens (humans), Mus pahari (mouse) and Drosophila mojavensis (fruit fly) was done and they were studied by free to use bioinformatics softwares available on internet. The protein properties of the sequences was studied (molecularmass, pI, signal peptide, transmembrane helices and conserved domains, secondary and 3D structures). The study of HMG-CoA Reductase protein sequences uncovered that there is high identity between the HMG-CoA Reductase Protein present in plants and animals. PROCHECK tool was used to draw Ramchandran plot of the Triticum aestivum HMG-CoA Reductase protein (Accession Number: AAB29929.1) and the structure of the protein was studied. The study demonstrated that most of the residues of the protein sequence were situated in the most preferred areas in Ramachandran plot, showing that the simulated three-dimensional structure was authentic. Evolutionary investigation demonstrated that there is a relationship betweenthe HMG-CoA Reductase proteins in species of Poaceae family and other animal samples under study. As indicated by theanalysis, HMG-CoA Reductases ought to be derived from a common predecessor.
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