ENZYME entry: EC 184.108.40.206
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|[Apoaequorin] + coelenterazine + O(2) + 3 Ca(2+) <=> [excited state blue fluorescent protein] + CO(2)|
- Ca(2+)-regulated photoproteins are found in a variety of
bioluminescent marine organisms, mostly coelenterates, and are
responsible for their light emission.
- The best studied enzyme is from the jellyfish Aequorea victoria.
- The enzyme tightly binds the imidazolopyrazinone derivative
coelenterazine, which is then peroxidized by oxygen.
- The hydroperoxide is stably bound until three Ca(2+) ions bind to the
protein, inducing a structural change that results in the formation
of a 1,2-dioxetan-3-one ring, followed by decarboxylation and
generation of a protein-bound coelenteramide in an excited state.
- The calcium-bound protein-product complex is known as a blue
- In vivo the energy is transferred to a green fluorescent protein
(GFP) by Foerster resonance energy transfer.
- In vitro, in the absence of GFP, coelenteramide emits a photon of
blue light while returning to its ground state.
|PRIAM enzyme-specific profiles||220.127.116.11|
|KEGG Ligand Database for Enzyme Nomenclature||18.104.22.168|
|IUBMB Enzyme Nomenclature||22.214.171.124|
|MEDLINE||Find literature relating to 126.96.36.199|
|Rhea expert-curated reactions||188.8.131.52|
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.-.-.-