Comparative Computational Analysis of Badh Isozyme of Selected Monocot and Dicot

摘要

Glycine betaine is a key osmoprotectant to protect plants from high salinity. In all betaine producers, it is synthesizedby a two-step oxidation of choline. In first step the enzyme choline monooxygenase (CMO) in plants, choline dehydrogenase(CDH) in animals and bacteria and choline oxidase in some bacteria oxidizes choline to an intermediate compound, betainealdehyde. The second step is catalyzed by betaine aldehyde dehydrogenase (BADH) in the all organisms, to produce the endproduct, glycine betaine. The betaine aldehyde dehydrogenase (BADH) enzyme is known as the key enzyme for glycine betainebiosynthesis. Comparative genomic analysis is the cornerstone of in-silico based approaches to understand biological systemsand processes across plant species in order to identify genes of agronomic interest. Thus, our aim was to use existingcomputational tools to comparatively analyze BADH isozymes of Hordeum vulgare, Oryza sativa, Sorghum bicolor, Arabidopsisthaliana, Glycine max, Leymus chinensis, Amaranthus hypochondriacus, Chrysanthemum lavandulifolium, Zoysia tenuifolia,Populus euphratica and Atriplex prostrate. In this study, we compiled detailed comparative information about BADH isozymesin selected plants by analyzing their structural features e.g. amino acid content, physico-chemical properties and secondarystructural features. Functional characterization was done by predicting motifs, patterns, disulfide bridges and secondarystructure. Functional analysis of these proteins includes identification of important 10 to 20 amino acids long motifs arisebecause specific residues and regions proved to be important for the biological function of a group of proteins, which areconserved in both structure and sequence during evolution. Present investigation will provide an insight for the biologistsworking with BADH isozymes in order to understand the functionality of BADH.