A coelenterazine-dependent luciferase from the deep-sea coral Anthoptilum murrayi.

Bioluminescence is visible light produced by living organisms through luciferase-catalyzed oxidation of luciferins. Although widespread in anthozoans, the molecular basis of their light emission remains poorly defined. Characterization has focused onRenilla reniformis, leaving anthozoan luciferase diversity underexplored. Here, we report the identification and characterization of a coelenterazine-dependent luciferase from the Murray's sea pen Anthoptilum murrayi (AnmLuc). Transcriptome analysis identified a transcript encoding a ∼35-kDa protein with characteristic motifs. The coding sequence was cloned and the recombinant protein was expressed in Escherichia coli. The reaction catalyzed by the purified enzyme resulted in an intense blue light emission (λmax≈ 495 nm) in the presence of coelenterazine, with an activity optimum near 15 °C and 30-40% of maximal activity still measurable at 2-5 °C. These findings provide the first molecular characterization of a deep-sea anthozoan luciferase, expanding known diversity, and offering insights into Anthozoan light emission.