International Journal of Pure & Applied Bioscience (IJPAB)
Year : 2016, Volume : 4, Issue : 2
First page : (71) Last page : (77)
Article doi: http://dx.doi.org/10.18782/2320-7051.2255
In-Silico Structural Modelling of Transaldolase from Helicobacter pylori (Strain G27) A Class I Transaldolase
Rabiu Salihu1,2*, Ismail Haruna1,3, Hassana Abubakar1,4, Mohd Shahir Shamsir1 and Sepideh Parvizpour1
1Faculty of Biosciences and Medical Engineering, University Technology Malaysia, 81310 Skudai, Johor, Malaysia
2Department of Biological Sciences, Federal University Dutse, PMB 7156 Dutse Jigawa State, Nigeria
3Department of Microbiology, Bauchi State University Gadau, PMB 65 Gadau Bauchi State, Nigeria
4Department of Biochemistry, Ibrahim Badamasi Babangida University Lapai, PMB 11 Niger State, Nigeria
*Corresponding Author E-mail: salihu.r@fud.edu.ng
Received: 29.03.2016 | Revised: 10.04.2016 | Accepted: 12.04.2016
Abstract
Numerous biotechnological applications of enzymes including rational drug design, turbidity reducing in the brewing industry and animal feeds digestibility enhancement have been recorded. An enzyme Transaldolase from Helicobacter pylori G27 (an important causative agent for gastric ulcers worldwide) plays an important role in NADPH synthesis regulation. However, an experimental structure of this enzyme is yet to be known. In this paper, we modelled an in-silico 3-Dimentional structure of a Transaldolase from H. pylori G27 using several Bioinformatics tools. Reliability and precision of the modelled structure were also evaluated. This work is anticipated to be found useful in reviewing structure/function relationship as well as rational drug design for the treatment of gastric ulcers.
Key words: In-silico, Transaldolase, Helicobacter pylori
Full Text : PDF; Journal doi : http://dx.doi.org/10.18782
Cite this article: Salihu, R., Haruna, I., Abubakar, H., Shamsir, M.S. and Parvizpour, S., In-Silico Structural Modelling of Transaldolase from Helicobacter pylori (Strain G27) A Class I Transaldolase, Int. J. Pure App. Biosci. 4(2): 71-77 (2016). doi: http://dx.doi.org/10.18782/2320-7051.2255
