| الوصف: |
Background:: In-silico study plays an important role in bioinformatics. It is a fastexpanding field to modelling, predicting and explaining biological activity at the molecular level using computational methods. Peroxidases are heme or non-heme-containing key antioxidant enzyme belonging to the oxidoreductase family. They can bioremediate the different environmental pollutants such as dioxins, petroleum hydrocarbons, synthetic dyes, herbicides, pesticides, chlorinated hydrocarbons, different phenolic and nonphenolic compounds etc. The current work aims to extend knowledge among researchers in better understanding structure of peroxidase purified from Raphanus sativus by analysing it’s physicochemical properties, secondary structure prediction, and 3D modelling of protein sequences and its validation using a variety of conventional computational methods. Objective:: Using bioinformatics techniques, it is feasible to figure out the relationship between sequence, structure, and function using enzyme protein sequences. To improve catalytic efficacy, thermostability, structure prediction, and validation, in-silico studies of the protein sequences of several industrially important enzymes have been performed recently. Method:: The physical and chemical parameters of radish peroxidase was analysed by using protparam tool-Expasy. SOPMA, SWISS MODEL, PROCHECK, ERRAT and Verify3D tools were used for structural analysis and validation of peroxidase protein sequence of Raphanus Sativus. The Molecular Evolutionary Genetics Analysis (MEGA 11) tool was used to align the protein sequences automatically and manually using the query sequence and peroxidase from various plant sources. Interaction of Radish peroxidase with the different organic substrates like guaiacol, o-cresol, mcresol, p-cresol, hydroquinone, catechol, resorcinol, benzaldehyde and aniline were analysed by molecular docking technique. Result:: This research gave critical information regarding the properties and functioning of Raphanus sativus peroxidase. The ... |