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.
| Published in | American Journal of Bioscience and Bioengineering (Volume 4, Issue 3) |
| DOI | 10.11648/j.bio.20160403.11 |
| Page(s) | 34-40 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2024. Published by Science Publishing Group |
Homology Modeling, Docking, AutoDock Vina, Ribitol Dehydrogenase
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APA Style
Hinawi A. M. Hassanin, Wanmeng Mu, Marwa Y. F. Koko, Tao Zhang, Ammar Alfarga, et al. (2016). Molecular Modeling and Docking of Ribitol Dehydrogenase Exploring Enzyme NAD+ and D-psicose Interaction. American Journal of Bioscience and Bioengineering, 4(3), 34-40. https://doi.org/10.11648/j.bio.20160403.11
ACS Style
Hinawi A. M. Hassanin; Wanmeng Mu; Marwa Y. F. Koko; Tao Zhang; Ammar Alfarga, et al. Molecular Modeling and Docking of Ribitol Dehydrogenase Exploring Enzyme NAD+ and D-psicose Interaction. Am. J. BioSci. Bioeng. 2016, 4(3), 34-40. doi: 10.11648/j.bio.20160403.11
AMA Style
Hinawi A. M. Hassanin, Wanmeng Mu, Marwa Y. F. Koko, Tao Zhang, Ammar Alfarga, et al. Molecular Modeling and Docking of Ribitol Dehydrogenase Exploring Enzyme NAD+ and D-psicose Interaction. Am J BioSci Bioeng. 2016;4(3):34-40. doi: 10.11648/j.bio.20160403.11
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Download@article{10.11648/j.bio.20160403.11,
author = {Hinawi A. M. Hassanin and Wanmeng Mu and Marwa Y. F. Koko and Tao Zhang and Ammar Alfarga and Mandour H. Abdelhai and Bo Jiang},
title = {Molecular Modeling and Docking of Ribitol Dehydrogenase Exploring Enzyme NAD+ and D-psicose Interaction},
journal = {American Journal of Bioscience and Bioengineering},
volume = {4},
number = {3},
pages = {34-40},
doi = {10.11648/j.bio.20160403.11},
url = {https://doi.org/10.11648/j.bio.20160403.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bio.20160403.11},
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.},
year = {2016}
}
TY - JOUR T1 - Molecular Modeling and Docking of Ribitol Dehydrogenase Exploring Enzyme NAD+ and D-psicose Interaction AU - Hinawi A. M. Hassanin AU - Wanmeng Mu AU - Marwa Y. F. Koko AU - Tao Zhang AU - Ammar Alfarga AU - Mandour H. Abdelhai AU - Bo Jiang Y1 - 2016/05/10 PY - 2016 N1 - https://doi.org/10.11648/j.bio.20160403.11 DO - 10.11648/j.bio.20160403.11 T2 - American Journal of Bioscience and Bioengineering JF - American Journal of Bioscience and Bioengineering JO - American Journal of Bioscience and Bioengineering SP - 34 EP - 40 PB - Science Publishing Group SN - 2328-5893 UR - https://doi.org/10.11648/j.bio.20160403.11 AB - 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. VL - 4 IS - 3 ER -
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