Structural comparison, docking and substrate interaction study of modeled endo-1, 4-beta xylanase enzyme of Bacillus brevis.

Xylanase belongs to, Glycoside hydrolase family, playing a major role in xylan degradation. Bacterial and most of the fungal Xylanase, are categorized as true Xylanase belong to GH 10 and GH 11 families. Xylanase is an industrially important enzyme. Most of the research has progressed in the field of isolation, purification and characterization of Xylanases, without giving much emphasis on the interaction of the substrate and the enzyme. To study the structure and ligand interaction, xylanase form Bacillus brevis was modeled, docking studies were performed and ligand interactions were studied. The comparative study gave detailed insight into the conserved amino acids which are involved in ligand interaction and complex stability. The amino acids like Tyrosine, Glutamic acid, Aspartic acid, Aspartate, Arginine play a major role in placing the substrate accurately in the binding cavity; also interact with the ligand for the specific activity. This study clarifies that amino acid Tyrosine at position 69, 166 and 174, is conserved among the different microbial Xylanase, specifying its importance in ligand binding and enzyme activity.