ENZYME entry: EC 18.104.22.168
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|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
- 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
- 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 profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
entries corresponding to 1.13.12.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.13.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-