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Title

Molecular modeling and analysis of human and plant endo-β-N-acetyl- glucosaminidases for mutations effects on function

 

Authors

Shechinah Felice Choragudi1, Ganesh Kumar Veeramachaneni1, BV Raman2 & Bondili JS1*

 

Affiliation

1Department of Biotechnology, K L University, Green fields, Vaddeswaram, Guntur, A.P-522502; 2Department of Basic Sciences, Madanapalle Institute of Technology and sciences, Madanapalle, A.P-517325

 

Email

jksingh@kluniversity.in; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received July 02, 2014; Accepted July 10, 2014; Published August 30, 2014

 

Abstract

Endo- β-N-acetylgucosaminidases (ENGases) are the enzymes that catalyze both hydrolysis and transglycosylation reactions. It is of interest to study ENGases because of their ability to synthesize glycopeptides. Homology models of Human, Arabidopsis thaliana and Sorghum ENGases were developed and their active sites marked based on information available from Arthrobacter protophormiae (PDB ID: 3FHQ) ENGase. Further, these models were docked with the natural substrate GlcNAc-Asn and the inhibitor Man3GlcNAc-thiazoline. The catalytic triad of Asn, Glu and Tyr (N171, E173 and Y205 of bacteria) were found to be conserved across the phyla. The crucial Y299F mutation showing 3 times higher transglycosylation activity than in wild type Endo-A is known. The hydrolytic activity remained unchanged in bacteria, while the transglycosylation activity increased. This Y to F change is found to be naturally evolved and should be attributing higher transglycosylation rates in human and Arabidopsis thaliana ENGases. Ligand interactions Ligplots revealed the interaction of amino acids with hydrophobic side chains and polar uncharged side chain amino acids. Thus, structure based molecular model-ligand interactions provide insights into the catalytic mechanism of ENGases and assist in the rational engineering of ENGases.

 

Keywords

ENGases, Transglycosylation, Modeling, Mutations.

 

Citation

Choragudi et al. Bioinformation 10(8): 507-511 (2014)
 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.