alexa Evolutionary Trace Analysis of Azoreductase at the Liga
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Evolutionary Trace Analysis of Azoreductase at the Ligand Binding Site and Enhancing the Active Site through Site Directed Mutagenesis

Shobana S1*, Berla Thangam E2 and Kasmir Raja SV3

1Department of Bioinformatics, SRM University, Kattankulathur, Chennai- 603203, India

2Department of Biotechnology, SRM University, Kattankulathur, Chennai- 603203, India

3Dean, Research, SRM University, Kattankulathur, Chennai- 603203, India

*Corresponding Author:
Shobana S
Department of Bioinformatics, SRM University
Kattankulathur, Chennai- 603203, India
E-mail: [email protected]

Received Date: August 16, 2012; Accepted Date: September 11, 2012; Published Date: September 13, 2012

Citation: Shobana S, Berla TE, Kasmir Raja SV (2012) Evolutionary Trace Analysis of Azoreductase at the Ligand Binding Site and Enhancing the Active Site through Site Directed Mutagenesis. J Proteomics Bioinform 5: 222-225. doi: 10.4172/jpb.1000240

Copyright: © 2012 Shobana S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

Azoreductases belong to the family of oxidoreductases and are characterized with detoxification of azo dyes. Azoreductases are involved in bioremediation, to eliminate the color effluents found in waste waters. In this study, the effectiveness of azoreductase in bioremediation was analysed, and the aim was to find a way to increase the efficiency of the enzyme towards toxic compound degradation, more rapidly. To estimate this, the structure function relationship was determined by evolutionary trace (ET) analysis at ligand binding site. The class specific site of ET analysis was mapped with the crystal structure of azoreductase (1NNI). Site directed mutagenesis was performed at the residues, in very close proximity to the active site residues, hydrogen bonded to ligand. Based on the work done, it was found that Glycine at 106th position plays a crucial role in enzyme activity.

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