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Molecular Phylogeny and Predicted 3D Structure of Plant beta-D-N-Acetylhexosaminidase

Identifieur interne : 000A05 ( Main/Exploration ); précédent : 000A04; suivant : 000A06

Molecular Phylogeny and Predicted 3D Structure of Plant beta-D-N-Acetylhexosaminidase

Auteurs : Md. Anowar Hossain [Bangladesh, Malaisie] ; Hairul Azman Roslan [Malaisie]

Source :

RBID : PMC:4129151

Abstract

beta-D-N-Acetylhexosaminidase, a family 20 glycosyl hydrolase, catalyzes the removal of β-1,4-linked N-acetylhexosamine residues from oligosaccharides and their conjugates. We constructed phylogenetic tree of β-hexosaminidases to analyze the evolutionary history and predicted functions of plant hexosaminidases. Phylogenetic analysis reveals the complex history of evolution of plant β-hexosaminidase that can be described by gene duplication events. The 3D structure of tomato β-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)8 barrel in the central part. The α and β contents 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 for β-Hex-Sl mutagenesis experiments for exploring the functions of this class of enzymes in plant kingdom.


Url:
DOI: 10.1155/2014/186029
PubMed: 25165734
PubMed Central: 4129151


Affiliations:


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Le document en format XML

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<italic>beta</italic>
-D-
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-Acetylhexosaminidase, a family 20 glycosyl hydrolase, catalyzes the removal of
<italic>β</italic>
-1,4-linked
<italic>N</italic>
-acetylhexosamine residues from oligosaccharides and their conjugates. We constructed phylogenetic tree of
<italic>β</italic>
-hexosaminidases to analyze the evolutionary history and predicted functions of plant hexosaminidases. Phylogenetic analysis reveals the complex history of evolution of plant
<italic>β</italic>
-hexosaminidase that can be described by gene duplication events. The 3D structure of tomato
<italic>β</italic>
-hexosaminidase (
<italic>β</italic>
-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 (
<italic>β</italic>
/
<italic>α</italic>
)
<sub>8</sub>
barrel in the central part. The
<italic>α</italic>
and
<italic>β</italic>
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<italic>β</italic>
-Hex-Sl mutagenesis experiments for exploring the functions of this class of enzymes in plant kingdom.</p>
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