ENZYME entry: EC

Accepted Name
Renilla-type luciferase.
Alternative Name(s)
Renilla-luciferin 2-monooxygenase.
Reaction catalysed
Coelenterazine h + O(2) <=> excited coelenteramide h monoanion + CO(2)
  • This enzyme has been studied from the soft coral Renilla reniformis.
  • Before the reaction occurs the substrate is sequestered by a coelenterazine-binding protein.
  • Elevation in the concentration of calcium ions releases the substrate, which then interacts with the luciferase.
  • Upon binding the substrate, the enzyme catalyzes an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO(2) molecule.
  • The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion.
  • In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence.
  • In vitro, in the absence of GFP, the product emits blue light.
PRIAM enzyme-specific profiles1.13.12.5
KEGG Ligand Database for Enzyme Nomenclature1.13.12.5
IUBMB Enzyme Nomenclature1.13.12.5
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