Publication Date:
2014-01-01
Description:
beta-D-N-Acetylhexosaminidase, a family 20 glycosyl hydrolase, catalyzes the removal ofβ-1,4-linkedN-acetylhexosamine residues from oligosaccharides and their conjugates. We constructed phylogenetic tree ofβ-hexosaminidases to analyze the evolutionary history and predicted functions of plant hexosaminidases. Phylogenetic analysis reveals the complex history of evolution of plantβ-hexosaminidase that can be described by gene duplication events. The 3D structure of tomatoβ-hexosaminidase (β-Hex-Sl) was predicted by homology modeling using 1now as a template. Structural conformity studies of the best fit model showed that more than 98% of the residues lie inside the favoured and allowed regions where only 0.9% lie in the unfavourable region. Predicted 3D structure contains 531 amino acids residues with glycosyl hydrolase20b domain-I and glycosyl hydrolase20 superfamily domain-II including the (β/α)8barrel in the central part. Theαandβcontents of the modeled structure were found to be 33.3% and 12.2%, respectively. Eleven amino acids were found to be involved in ligand-binding site; Asp(330) and Glu(331) could play important roles in enzyme-catalyzed reactions. The predicted model provides a structural framework that can act as a guide to develop a hypothesis forβ-Hex-Sl mutagenesis experiments for exploring the functions of this class of enzymes in plant kingdom.
Print ISSN:
2356-6140
Electronic ISSN:
1537-744X
Topics:
Natural Sciences in General
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