Document Type : Article
Department of Biotechnology-Graduate University of Advanced Technology, Kerman, Iran.
Department of Biotechnology, Institute of Sciences, High Technology and Environmental Sciences, Graduate University of Advanced Technology, Kerman, Iran
Pharmaceutical Sciences Research Centre, Faculty of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
Legal Medicine Research Center, Legal Medicine Organization of Iran, Tehran
Gastroenterohepatology Research Center, Shiraz University of Medical Sciences, Shiraz, IR Iran;
Department of biology, faculty of basic sciences, Shahrekord University, Charmahal va bakhtiari, Iran
Department of Biotechnology, Institute of Science and High Technology and Environmental Science, Graduate University of Advanced Technology, Kerman, Iran- email@example.com
- GastroenteroHepatology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
-Legal Medicine Research Center, Legal Medicine Organization of Iran, Tehran, Iran-
Luciferase enzymes are involved in the bioluminescence reaction (light emission by living organisms). The bioluminescence process is a widespread phenomenon in the Nature. These enzymes are identified in some domains of life, but the luciferases from lampyrid genus are considered of for biological applications. The molecular cloning of a new type of firefly luciferase from Luciola lateralis was reported, previously. Here, we study its substrate binding site and rare codon with molecular docking and bioinformatics studies. By molecular modelling, some rare codons were identified that may have a critical role in structure and function of this luciferase. AutoDock Vina was used in the molecular docking that recognizes some residues that yield closely related with luciferin and AMP binding site. These types of studies help in the discovery of the light production reaction. Evaluation of these hidden information’s can improve the knowledge of luciferases folding and protein expression challenges and help in design of new drugs.