Please use this identifier to cite or link to this item: https://open.uns.ac.rs/handle/123456789/3953
Title: Homology modelling and docking analysis of l-lactate dehydrogenase from streptococcus thermopilus
Authors: Vukić, Vladimir 
Milanović, Spasenija
Iličić (Panić), Mirela 
Kanurić (Duraković), Katarina 
Vukić (Hrnjez), Dajana 
Issue Date: 2016
Publisher: Novi Sad: University of Novi Sad, Faculty of Technology, Novi Sad
Journal: Acta Periodica Technologica
Abstract: The aim of this research was to create a three-dimensional model of L-lactate dehydrogenase from the main yoghurt starter culture - Streptococcus thermopilus, to analyse its structural features and investigate substrate binding in the active site. NCBI BlastP was used against the Protein Data Bank database in order to identify the template for construction of homology models. Multiple sequence alignment was performed using the program MUSCULE within the UGENE 1.11.3 program. Homology models were constructed using the program Modeller v. 9.17. The obtained 3D model was verified by Ramachandran plots. Molecular docking simulations were performed using the program Surflex-Dock. The highest sequence similarity was observed with L-lactate dehydrogenase from Lactobacillus casei subsp. casei, with 69% identity. Therefore, its structure (PDB ID: 2ZQY:A) was selected as a modelling template for homology modelling. Active residues are by sequence similarity predicted: S. thermophilus - HIS181 and S. aureus -HIS179. Binding energy of pyruvate to L-lactate dehydrogenase of S. thermopilus was -7.874 kcal/mol. Pyruvate in L-lactate dehydrogenase of S. thermopilus makes H bonds with catalytic HIS181 (1.9 A), as well as with THR235 (3.6 A). Although our results indicate similar position of substrates between L-lactate dehydrogenase of S. thermopilus and S. aureus, differences in substrate distances and binding energy values could influence the reaction rate. Based on these results, the L-lactate dehydrogenase model proposed here could be used as a guide for further research, such as transition states of the reaction through molecular dynamics.
URI: https://open.uns.ac.rs/handle/123456789/3953
ISSN: 14507188
DOI: 10.2298/APT1647241V
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