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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 azoreductases. Although several azoreductases 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 analyze 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. Keywords: Azoreductase , NADH, FMN, chemical properties, docking, active sites.

african journal of biotechnology

Functional and catalytic active sites prediction and docking analysis of azoreductase enzyme in Pseudomonas putida with a variety of commercially available azodyes