ENZYME entry: EC 1.13.12.24
| Accepted Name |
|---|
| Calcium-regulated photoprotein.
|
| Alternative Name(s) |
|---|
| Aequorin. |
| Berovin. |
| Ca(2+)-regulated photoprotein. |
| Calcium-activated photoprotein. |
| Clytin. |
| Halistaurin. |
| Mitrocomin. |
| Mnemiopsin. |
| Obelin. |
| Vialidin. |
| Reaction catalysed |
|---|
| [Apoaequorin] + coelenterazine + O(2) + 3 Ca(2+) <=> [excited state blue fluorescent protein] + CO(2) |
| Comment(s) |
|---|
- 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
fluorescent protein.
- 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.
|
| Cross-references |
|---|
| BRENDA | 1.13.12.24 |
| EC2PDB | 1.13.12.24 |
| ExplorEnz | 1.13.12.24 |
| PRIAM enzyme-specific profiles | 1.13.12.24 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.13.12.24 |
| IUBMB Enzyme Nomenclature | 1.13.12.24 |
| IntEnz | 1.13.12.24 |
| MEDLINE | Find literature relating to 1.13.12.24 |
| MetaCyc | 1.13.12.24 |
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot 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.-.-.-