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Molecular Modeling and Docking of Ribitol Dehydrogenase Exploring Enzyme NAD+ and D-psicose Interaction
American Journal of Bioscience and Bioengineering
Volume 4, Issue 3, June 2016, Pages: 34-40
Received: Apr. 14, 2016; Accepted: Apr. 25, 2016; Published: May 10, 2016
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Authors
Hinawi A. M. Hassanin, State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China
Wanmeng Mu, State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China
Marwa Y. F. Koko, State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China
Tao Zhang, State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China
Ammar Alfarga, State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China
Mandour H. Abdelhai, State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China
Bo Jiang, State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China
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Abstract
Allitol is an alcohol monosaccharide, is a reduction of D-psicose. It is functions as a cross linking of D- and L-hexoses. It existed in too small quantities in commercial sugars and is difficult to synthesize by using chemical methods. It has a hypoglycemic function, and can use as Laxative in treating of constipation, which can exploit in production of diabetes drugs. The present report investigates about the production of allitol by ribitol dehydrogenase (RDH), its action of the enzyme through homology and molecular docking studies. We have investigated ribitol dehydrogenase (RDH) from providencia alcalifaciens RIMD 1656011. The protein sequence of RDH was conducted for homology modeling through Swiss model. 3D structure revealed was docked with NAD+ and D-psicose using AutoDock Vina software version 5.6. The results of homology modeling and docking studies revealed that the conserved residues of RDH were Tyr 153, Tyr 92, Ser 17 and Lys157 with NAD+, while conserved residues with D-psicose were GLN67 and ASP61. NAD+ has good interaction with RDH showing grid score of -49.84, which is a good score for binding.
Keywords
Homology Modeling, Docking, AutoDock Vina, Ribitol Dehydrogenase
To cite this article
Hinawi A. M. Hassanin, Wanmeng Mu, Marwa Y. F. Koko, Tao Zhang, Ammar Alfarga, Mandour H. Abdelhai, Bo Jiang, Molecular Modeling and Docking of Ribitol Dehydrogenase Exploring Enzyme NAD+ and D-psicose Interaction, American Journal of Bioscience and Bioengineering. Vol. 4, No. 3, 2016, pp. 34-40. doi: 10.11648/j.bio.20160403.11
Copyright
Copyright © 2016 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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