Structural Characterization of a Novel Luciferase-Like-Monooxygenase from Pseudomonas meliae – An in-Silico Approach

Luciferase is a well-known oxidative enzyme that produces bioluminescence. The Pseudomonas meliae is a plant pathogen that causes wood to rot on nectarine and peach and possesses a luciferase-like monooxygenase. After activation, it produces bioluminescence, and the pathogen’s bioluminescence is a visual indicator of contaminated plants. The present study aims to model and characterize the luciferase-like monooxygenase protein in P. meliae for its similarity to well-established luciferase. In this study, the luciferase-like monooxygenase from P. meliae infects chinaberry plants has been first modeled and then, studied by comparing it with existing known luciferase. In addition, the similarities between uncharacterized luciferase from P. meliae and the template from Geobacillus thermodenitrificans were analyzed. The results suggest that the absence of bioluminescence in P. meliae could be critical for the production of the luciferin substrate and the catalytic activity of the enzyme due to the evolutionary mutation in positions 138 and 311. The active site remains identical except for two amino acids. Therefore, mutation of the residues 138 and 311 in P. meliae Luciferase-like monooxygenase may restore luciferase light-emitting ability.