Computational Studies on Physicochemical Properties, Substrate Specificity Prediction and Binding Mode Analysis of Aliphatic Nitrilase (Research Article)

Author(s): Fenil Parmar, Khushi Salvi, Deep Somani, Kinjal Makwana, Meenu Saraf and Dweipayan Goswami

Abstract: Nitrilase enzyme catalyze conversion of nitrile compounds to its corresponding carboxylic acid and ammonia. With the rise of digital era, the use of computational analysis to revel hidden characteristics of enzymes is continuously growing because of its cost effectiveness and faster output. Highly developed sequencing technology provides an opportunity to conduct virtual studies and explore unique properties and applications of various enzymes. Physico-chemical properties of aliphatic nitrilase evaluated results show quite similar properties of all 13 studied aliphatic nitrilase. The 3D structures of aliphatic nitrilase were generated by using Swiss-Model server and validated using different tools describes that quality of 3D structure of all 13 protein is good. Docking of 13 nitriles with all 13 aliphatic nitrilase was done by using Autodock v4.2.6 software, reveals that cis-cis Mucononitrile has highest binding affinity with most of studied protein, while Glycolonitrile and Propionitrile has less binding affinity toward major studied nitrilase.

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