Bioinformatics Based Investigation on the Assortment of Industrially Accessible Azodyes with Azoreductase Enzyme of Pseudomonas putida

Bioinformatics Based Investigation on the Assortment of Industrially Accessible Azodyes with Azoreductase Enzyme of Pseudomonas putida

Azo dyes are the most widely applied chemical dyes that have also raised great concerns for environmental contamination and human health issues. There has been an increased interest in discovering new novel bioremediation strategies to degrade azo dyes for environmental issues and also economic purposes. Azoreductase are key enzymes evolved in nature capable of degrading the azo dyes. As azoreductase enzyme is a key enzyme in degrading these azo dyes, they are good and potential candidates for industrial wastewater treatment and environmental restoration. The initial critical step of reduction of azo bond during the metabolism of azo dyes is catalysed by a group of NADH and FAD dependant enzyme called azoreductase. Although several azoreductase have been identified from microorganisms and partially characterized, very little is known about the structural basis of the substrate specificity and the nature of catalysis. Azoreductase enzyme of Pseudomonas putida has a wider broad spectrum of substrate specificity and capable of degrading a wide variety of azo dyes. In the present study, the crystal structure of the enzyme from PDB and 10 azo dyes from NCBI PubChem compound were retrieved and their interactions were studied. These azo dyes were then docked with the FMN-dependent NADH-azoreductase enzyme to analyse the binding affinity of the azo dyes with the enzyme and predict the catalytic sites. Consequently, the catalytic residues of FMN-dependent and NADH dependent enzyme were then analysed in terms of properties including function, hydrogen bonding and flexibility. The results suggest that Ala-114, Phe-172 and Glu-174 play a predominant role as catalytic site residues in the enzyme. Furthermore, the approach emphasis on predicting the active sites of this enzyme where substrates can bind in order to give a better understanding of the biodegradation of some of the commercially important azodyes mediated by azoreductase. These results will pave way for further increase in azoreductase activity and for better understanding of the dye degradation pathway. In addition to it, the different types of azo reductases can be further biochemically characterized for their novelty in near future.

Author(s) Details
Mr. Bikash Thakuria
Bioinformatics Centre, Department of Biotechnology, St. Edmund’s College, Shillong – 793003, Meghalaya, India.

Dr. Samrat Adhikari
Bioinformatics Centre, Department of Biotechnology, St. Edmund’s College, Shillong – 793003, Meghalaya, India

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