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ENZYME entry: EC

Accepted Name
Renilla-type luciferase
Alternative Name(s)
Renilla-luciferin 2-monooxygenase
Reaction catalysed
coelenterazine h + O2 <=> CO2 + excited coelenteramide h monoanion + H(+) + hnu
  • 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 CO2 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
MEDLINEFind literature relating to
Rhea expert-curated reactions1.13.12.5

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