Abstract

Luciferase derived from different organism is widely used for various biological process in the cells or tissues. Current in silico study was done to investigate the protein-substrate interactions of Renilla muelleri, Metridia longa and Photinus pyralis luciferase with their respective substrates coelenterazine, Luciferin, and ATP. RaptorX which is an online tool was used for luciferase modeling. PyRx v9.0 was used for protein-substrate binding. Online server Cluspro was used for protein-protein docking. CASTp was used for protein active site pocket prediction. Photinus pyralis luciferase was bonded with ATP molecules through Glu83, Asp153, Asp44, Ser85, Gln87 and His171, while Photinus Pyralis luciferase was bonded with luciferin molecules through five different residues i.e. His171, Arg62, Met90, Leu63 and Val168. Photinus pyralis residues that were docked with ATP and luciferin molecules were present in N terminal domain of Photinus pyralis luciferase. In case of Renilla muelleri, catalytic residues, His285 was present in its all the docking complex. Renilla muelleri and Metridia longa luciferase were also docked with different substrate and found that efficiency of Renilla muelleri and Metridia longa luciferase was lower towards Photinus pyralis substrates as compared to their own substrate coelentereazine. According to the findings, it has been concluded that luciferase of every light emitting organism required specific (its own) substrate for proper light reaction.

Keywords: Renilla muelleri; Metridia longa; Photinus pyralis; luciferase