Title

Authors

Affiliation

Department of Bioinformatics and Biotechnology, Government College University (GCU), Faisalabad, Pakistan

Email

waseemsarwar@live.com; *Corresponding author

Article Type

Hypothesis

Date

Received November 11, 2013; Accepted November 19, 2013; Published December 06, 2013

Background: Arabitol dehydrogenase (ArDH) is involved in the production of different sugar alcohols like arabitol, sorbitol, mannitol, erythritol and xylitol by using five carbon sugars as substrate. Arabinose, d-ribose, d-ribulose, xylose and d-xylulose are known substrate of this enzyme. ArDH is mainly produced by osmophilic fungi for the conversion of ribulose to arabitol under stress conditions. Recently this enzyme has been used by various industries for the production of pharmaceutically important sugar alcohols form cheap source than glucose. But the information at structure level as well as its binding energy analysis with different substrates was missing. Results: The present study was focused on sequence analysis, insilico characterization and substrate binding analysis of ArDH from a fungus specie candida albican. Sequence analysis and physicochemical properties showed that this protein is highly stable, negatively charged and having more hydrophilic regions, these properties made this enzyme to bind with number of five carbon sugars as substrate. The predicted 3D model will helpful for further structure based studies. Docking analysis provided free energy of binding of substrate from a best pose as arabinose -9.8224cal/mol, d-ribose -11.3701cal/mol, d-ribulose -8.9230cal/mol, xylose -9.7007cal/mol and d-xylulose 9.7802 cal/mol. Conclusion: Our study provided insight information of structure and interactions of ArDH with its substrate. These results obtained from this clearly indicate that d-ribose is best substrate for ArDH for the production of sugar alcohols. This information will be helpful for better usage of this enzyme for hyper-production of sugar alcohols by different industries.  

Keywords

Arabitol dehydrogenase, Homology Modeling, Insilico, Charaterization, Molecular Docking.

Citation

Sarwar et al. Bioinformation 9(19): 952-957 (2013)

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.