Renilla-luciferin 2-monooxygenase (RLuc)

Renilla-luciferin 2-monooxygenase (abbreviated as RLuc and also known as Renilla luciferase) is an enzyme originally isolated from the sea pansy *Renilla reniformis*, responsible for the blue light emission observed in this species[1][2][3][4][6][7]. The enzyme is a 36–37 kDa monomeric protein, structurally characterized by an alpha/beta-hydrolase fold and a conserved catalytic triad (Aspartic Acid 120, Glutamic Acid 144, and Histidine 285)[1][3][4][5][6][8]. RLuc catalyzes the oxidative decarboxylation of the substrate coelenterazine in the presence of molecular oxygen, yielding coelenteramide, carbon dioxide, and a photon of blue light (480 nm)[1][3][4][7]. In vivo, this blue light is transferred via resonance energy transfer to a green fluorescent protein (RrGFP), resulting in green bioluminescence[1][2][3].\nUnlike receptors or classical therapeutic targets, RLuc is not involved in normal human physiology or disease processes and is widely used in biotechnology as a genetic reporter in cell lines and animal models to quantify gene expression or to track biological processes by bioluminescence imaging[2][3][5][6]. There are no known drugs that modulate this enzyme for therapeutic purposes, and it does not serve as a biomarker or have direct disease associations.

Other names

Renilla luciferaseCoelenterazine h 2-monooxygenaseRenilla-type luciferase